sequence-518.orf

########################################
# Program: patmatmotifs
# Rundate: Wed 25 Nov 2015 13:56:28
# Commandline: patmatmotifs
#    -full
#    -outfile res/sequence-518.orf
#    -sequence res/sequence-518.gb
# Report_format: dbmotif
# Report_file: res/sequence-518.orf
########################################

#=======================================
#
# Sequence: NM_000518     from: 1   to: 626
# HitCount: 11
#
# Full: Yes
# Prune: Yes
# Data_file: /usr/local/Cellar/emboss/6.6.0/share/EMBOSS/data/PROSITE/prosite.lines
#
#=======================================

Length = 12
Start = position 421 of sequence
End = position 432 of sequence

Motif = EGF_1

ATTCACCCCACCAGTGCAGGCT
     |          |
   421          432

Length = 12
Start = position 313 of sequence
End = position 324 of sequence

Motif = EGF_1

TGCCACACTGAGTGAGCTGCAC
     |          |
   313          324

Length = 9
Start = position 369 of sequence
End = position 377 of sequence

Motif = 2FE2S_FER_1

GGCTCCTGGGCAACGTGCT
     |       |
   369       377

Length = 9
Start = position 285 of sequence
End = position 293 of sequence

Motif = 2FE2S_FER_1

CTCACCTGGACAACCTCAA
     |       |
   285       293

Length = 35
Start = position 134 of sequence
End = position 168 of sequence

Motif = ANAPHYLATOXIN_1

GAGGCCCTGGGCAGGCTGCTGGTGGTCTACCCTTGGACCCAGAGG
     |                                 |
   134                                 168

Length = 36
Start = position 133 of sequence
End = position 168 of sequence

Motif = ANAPHYLATOXIN_1

TGAGGCCCTGGGCAGGCTGCTGGTGGTCTACCCTTGGACCCAGAGG
     |                                  |
   133                                  168

Length = 46
Start = position 399 of sequence
End = position 444 of sequence

Motif = VWFC_1

TGGCCCATCACTTTGGCAAAGAATTCACCCCACCAGTGCAGGCTGCCTATCAGAAA
     |                                            |
   399                                            444

Length = 47
Start = position 398 of sequence
End = position 444 of sequence

Motif = VWFC_1

CTGGCCCATCACTTTGGCAAAGAATTCACCCCACCAGTGCAGGCTGCCTATCAGAAA
     |                                             |
   398                                             444

Length = 43
Start = position 362 of sequence
End = position 404 of sequence

Motif = VWFC_1

AACTTCAGGCTCCTGGGCAACGTGCTGGTCTGTGTGCTGGCCCATCACTTTGG
     |                                         |
   362                                         404

Length = 51
Start = position 324 of sequence
End = position 374 of sequence

Motif = VWFC_1

GTGAGCTGCACTGTGACAAGCTGCACGTGGATCCTGAGAACTTCAGGCTCCTGGGCAACGT
     |                                                 |
   324                                                 374

Length = 46
Start = position 43 of sequence
End = position 88 of sequence

Motif = VWFC_1

TCAAACAGACACCATGGTGCATCTGACTCCTGAGGAGAAGTCTGCCGTTACTGCCC
     |                                            |
    43                                            88


#---------------------------------------
#
# Motif: EGF_1
# Count: 2
# 
# ******************************************
# * EGF-like domain signatures and profile *
# ******************************************
# 
# A sequence of  about thirty  to forty amino-acid  residues  long found in  the
# sequence of  epidermal  growth  factor  (EGF)  has been  shown  [1 to 6] to be
# present, in  a more or less conserved form, in a large number of other, mostly
# animal  proteins.  EGF  is  a  polypeptide  of about 50 amino acids with three
# internal  disulfide  bridges.  It  first  binds with high affinity to specific
# cell-surface receptors and then induces their dimerization, which is essential
# for  activating  the  tyrosine  kinase  in  the  receptor  cytoplasmic domain,
# initiating  a  signal  transduction  that  results  in  DNA synthesis and cell
# proliferation.
# 
# A  common  feature  of  all  EGF-like  domains  is  that they are found in the
# extracellular  domain  of  membrane-bound  proteins or in proteins known to be
# secreted (exception: prostaglandin G/H synthase). The EGF-like domain includes
# six cysteine residues which have been shown to be involved in disulfide bonds.
# The  structure  of several EGF-like domains has been solved. The fold consists
# of   two-stranded  beta-sheet  followed  by  a  loop  to  a  C-terminal  short
# two-stranded sheet   (see   <PDB:1EGF>).   Subdomains  between  the  conserved
# cysteines strongly  vary  in  length  as  shown  in  the  following  schematic
# representation of the EGF-like domain:
# 
#                  +-------------------+        +-------------------------+
#                  |                   |        |                         |
#   x(4)-C-x(0,48)-C-x(3,12)-C-x(1,70)-C-x(1,6)-C-x(2)-G-a-x(0,21)-G-x(2)-C-x
#        |                   |         ************************************
#        +-------------------+
# 
# 'C': conserved cysteine involved in a disulfide bond.
# 'G': often conserved glycine
# 'a': often conserved aromatic amino acid
# '*': position of both patterns.
# 'x': any residue
# 
# Some  proteins  known  to contain one or more copies of an EGF-like domain are
# listed below.
# 
#  - Adipocyte differentiation inhibitor (gene PREF-1) from mouse (6 copies).
#  - Agrin, a basal lamina protein  that causes the aggregation of acetylcholine
#    receptors on cultured muscle fibers (4 copies).
#  - Amphiregulin, a growth factor (1 copy).
#  - Betacellulin, a growth factor (1 copy).
#  - Blastula  proteins  BP10  and  Span from sea urchin which are thought to be
#    involved in pattern formation (1 copy).
#  - BM86, a glycoprotein antigen of cattle tick (7 copies).
#  - Bone morphogenic protein 1 (BMP-1), a  protein which induces cartilage  and
#    bone formation  and  which  expresses  metalloendopeptidase  activity  (1-2
#    copies). Homologous proteins are found in sea urchin - suBMP (1 copy) - and
#    in Drosophila - the dorsal-ventral patterning protein tolloid (2 copies).
#  - Caenorhabditis elegans developmental proteins lin-12 (13 copies)  and glp-1
#    (10 copies).
#  - Caenorhabditis elegans apx-1 protein, a patterning protein (4.5 copies).
#  - Calcium-dependent serine proteinase (CASP) which degrades the extracellular
#    matrix proteins type I and IV collagen and fibronectin (1 copy).
#  - Cartilage matrix protein CMP (1 copy).
#  - Cartilage oligomeric matrix protein COMP (4 copies).
#  - Cell surface antigen 114/A10 (3 copies).
#  - Cell surface glycoprotein complex transmembrane subunit ASGP-2  from rat (2
#    copies).
#  - Coagulation associated proteins C, Z (2 copies) and S (4 copies).
#  - Coagulation factors VII, IX, X and XII (2 copies).
#  - Complement C1r components (1 copy).
#  - Complement C1s components (1 copy).
#  - Complement-activating component of Ra-reactive factor (RARF) (1 copy).
#  - Complement components C6, C7, C8 alpha and beta chains, and C9 (1 copy).
#  - Crumbs, an epithelial development protein from Drosophila (29 copies).
#  - Epidermal growth factor precursor (7-9 copies).
#  - Exogastrula-inducing peptides A, C, D and X from sea urchin (1 copy).
#  - Fat protein, a Drosophila cadherin-related tumor suppressor (5 copies).
#  - Fetal  antigen  1, a probable neuroendocrine differentiation protein, which
#    is derived from the delta-like protein (DLK) (6 copies).
#  - Fibrillin 1 (47 copies) and fibrillin 2 (14 copies).
#  - Fibropellins  IA  (21 copies), IB (13 copies), IC (8 copies), II (4 copies)
#    and III   (8   copies)  from  the  apical  lamina  -  a  component  of  the
#    extracellular matrix - of sea urchin.
#  - Fibulin-1 and -2, two extracellular matrix proteins (9-11 copies).
#  - Giant-lens  protein (protein Argos), which regulates cell determination and
#    axon guidance in the Drosophila eye (1 copy).
#  - Growth factor-related proteins from various poxviruses (1 copy).
#  - Gurken protein, a Drosophila developmental protein (1 copy).
#  - Heparin-binding EGF-like growth factor (HB-EGF), transforming growth factor
#    alpha (TGF-alpha), growth factors Lin-3 and Spitz (1 copy);  the precursors
#    are membrane proteins, the mature form is located extracellular.
#  - Hepatocyte growth factor (HGF) activator (EC 3.4.21.-) (2 copies).
#  - LDL  and  VLDL receptors, which bind and transport low-density lipoproteins
#    and very low-density lipoproteins (3 copies).
#  - LDL  receptor-related  protein  (LRP), which  may  act  as  a  receptor for
#    endocytosis of extracellular ligands (22 copies).
#  - Leucocyte  antigen  CD97  (3  copies),  cell  surface  glycoprotein EMR1 (6
#    copies) and cell surface glycoprotein F4/80 (7 copies).
#  - Limulus clotting factor C, which is involved in hemostasis and host defense
#    mechanisms in japanese horseshoe crab (1 copy).
#  - Meprin A alpha subunit, a mammalian membrane-bound endopeptidase (1 copy).
#  - Milk fat globule-EGF factor 8 (MFG-E8) from mouse (2 copies).
#  - Neuregulin GGF-I and GGF-II, two human glial growth factors (1 copy).
#  - Neurexins from mammals (3 copies).
#  - Neurogenic  proteins  Notch, Xotch and the human homolog Tan-1 (36 copies),
#    Delta (9  copies)  and  the  similar  differentiation  proteins  Lag-2 from
#    Caenorhabditis elegans (2  copies), Serrate (14 copies) and Slit (7 copies)
#    from Drosophila.
#  - Nidogen  (also called entactin), a basement membrane protein from chordates
#    (2-6 copies).
#  - Ookinete surface proteins (24 Kd, 25 Kd, 28 Kd) from Plasmodium (4 copies).
#  - Pancreatic secretory granule membrane major glycoprotein GP2 (1 copy).
#  - Perforin, which lyses non-specifically a variety of target cells (1 copy).
#  - Proteoglycans  aggrecan (1 copy), versican (2 copies), perlecan (at least 2
#    copies), brevican (1 copy) and chondroitin sulfate proteoglycan (gene PG-M)
#    (2 copies).
#  - Prostaglandin G/H synthase 1 and 2  (EC 1.14.99.1) (1 copy), which is found
#    in the endoplasmatic reticulum.
#  - Reelin, an extracellular matrix protein  that  plays a role in  layering of
#    neurons in the cerebral cortex and cerebellum of mammals (8 copies).
#  - S1-5,  a  human  extracellular  protein whose ultimate activity is probably
#    modulated by the environment (5 copies).
#  - Schwannoma-derived growth factor (SDGF), an autocrine growth factor as well
#    as a mitogen for different target cells (1 copy).
#  - Selectins. Cell  adhesion  proteins such  as  ELAM-1 (E-selectin),  GMP-140
#    (P-selectin), or the lymph-node homing receptor (L-selectin) (1 copy).
#  - Serine/threonine-protein  kinase  homolog  (gene  Pro25)  from  Arabidopsis
#    thaliana, which  may   be   involved   in   assembly   or   regulation   of
#    light-harvesting chlorophyll A/B protein (2 copies).
#  - Sperm-egg fusion proteins PH-30 alpha and beta from guinea pig (1 copy).
#  - Stromal cell derived protein-1 (SCP-1) from mouse (6 copies).
#  - TDGF-1, human teratocarcinoma-derived growth factor 1 (1 copy).
#  - Tenascin  (or  neuronectin),  an  extracellular matrix protein from mammals
#    (14.5 copies), chicken (TEN-A) (13.5 copies) and the related proteins human
#    tenascin-X (18  copies)  and  tenascin-like  proteins  TEN-A and TEN-M from
#    Drosophila (8 copies).
#  - Thrombomodulin   (fetomodulin),  which  together  with  thrombin  activates
#    protein C (6 copies).
#  - Thrombospondin  1, 2 (3 copies), 3 and 4 (4 copies), adhesive glycoproteins
#    that mediate cell-to-cell and cell-to-matrix interactions.
#  - Thyroid peroxidase 1 and 2 (EC 2.7.10.1) from human (1 copy).
#  - Transforming  growth  factor  beta-1  binding protein (TGF-B1-BP) (16 or 18
#    copies).
#  - Tyrosine-protein kinase receptors Tek and Tie (EC 2.7.1.112) (3 copies).
#  - Urokinase-type  plasminogen  activator  (EC  3.4.21.73)  (UPA)  and  tissue
#    plasminogen activator (EC 3.4.21.68) (TPA) (1 copy).
#  - Uromodulin (Tamm-horsfall urinary glycoprotein) (THP) (3 copies).
#  - Vitamin  K-dependent  anticoagulants  protein C (2 copies) and protein S (4
#    copies) and  the  similar  protein Z, a single-chain plasma glycoprotein of
#    unknown function (2 copies).
#  - 63 Kd sperm flagellar membrane protein from sea urchin (3 copies).
#  - 93 Kd protein (gene nel) from chicken (5 copies).
#  - Hypothetical  337.6  Kd  protein  T20G5.3  from  Caenorhabditis elegans (44
#    copies).
# 
# The region between the 5th and 6th cysteine contains two conserved glycines of
# which at  least  one  is  present  in  most  EGF-like  domains. We created two
# patterns for  this  domain,  each  including one of these C-terminal conserved
# glycine residues. The profile we developed covers the whole domain.
# 
# -Consensus pattern: C-x-C-x(2)-{V}-x(2)-G-{C}-x-C
#                     [The 3 C's are involved in disulfide bonds]
# -Sequences known to belong to this class detected by the pattern: ALL.
#  but not  those  that  have very long or very short regions between the last 3
#  conserved cysteines of their EGF-like domain(s).
# -Other sequence(s)  detected  in  Swiss-Prot:  87 proteins, of which 27 can be
#  considered as possible candidates.
# 
# -Consensus pattern: C-x-C-x(2)-[GP]-[FYW]-x(4,8)-C
#                     [The 3 C's are involved in disulfide bonds]
# -Sequences known to belong to this class detected by the pattern: ALL.
#  but not  those  that  have very long or very short regions between the last 3
#  conserved cysteines of their EGF-like domain(s).
# -Other sequence(s)  detected  in  Swiss-Prot:  83 proteins, of which 49 can be
#  considered as possible candidates.
# 
# -Sequences known to belong to this class detected by the profile: ALL.
# -Other sequence(s) detected in Swiss-Prot: NONE.
# 
# -Note: The  beta chain of the integrin family of proteins contains 2 cysteine-
#  rich repeats  which were said to be dissimilar with the EGF pattern [7].
# -Note: Laminin  EGF-like repeats (see <PDOC00961>) are longer than the average
#  EGF module  and  contain  a further disulfide bond C-terminal of the EGF-like
#  region. Perlecan  and  agrin  contain  both EGF-like domains and laminin-type
#  EGF-like domains.
# -Note: The  pattern do not detect all of the repeats of proteins with multiple
#  EGF-like repeats.
# -Note: See <PDOC00913> for an entry describing specifically the subset of EGF-
#  like domains that bind calcium.
# 
# -Last update: April 2006 / Pattern revised.
# 
# [ 1] Davis C.G.
#      "The many faces of epidermal growth factor repeats."
#      New Biol. 2:410-419(1990).
#      PubMed=2288911
# [ 2] Blomquist M.C., Hunt L.T., Barker W.C.
#      "Vaccinia virus 19-kilodalton protein: relationship to several
#      mammalian proteins, including two growth factors."
#      Proc. Natl. Acad. Sci. U.S.A. 81:7363-7367(1984).
#      PubMed=6334307
# [ 3] Barker W.C., Johnson G.C., Hunt L.T., George D.G.
#      Protein Nucl. Acid Enz. 29:54-68(1986).
# [ 4] Doolittle R.F., Feng D.F., Johnson M.S.
#      "Computer-based characterization of epidermal growth factor
#      precursor."
#      Nature 307:558-560(1984).
#      PubMed=6607417
# [ 5] Appella E., Weber I.T., Blasi F.
#      "Structure and function of epidermal growth factor-like regions in
#      proteins."
#      FEBS Lett. 231:1-4(1988).
#      PubMed=3282918
# [ 6] Campbell I.D., Bork P.
#      Curr. Opin. Struct. Biol. 3:385-392(1993).
# [ 7] Tamkun J.W., DeSimone D.W., Fonda D., Patel R.S., Buck C.,
#      Horwitz A.F., Hynes R.O.
#      "Structure of integrin, a glycoprotein involved in the transmembrane
#      linkage between fibronectin and actin."
#      Cell 46:271-282(1986).
#      PubMed=3487386
# 
# ***************
# 
# Motif: 2FE2S_FER_1
# Count: 2
# 
# ***************************************************************************
# * 2Fe-2S ferredoxin-type iron-sulfur binding domain signature and profile *
# ***************************************************************************
# 
# Ferredoxins  are small, acidic, electron transfer proteins that are ubiquitous
# in  biological  redox  systems.  They  have  either  4Fe-4S, 3Fe-4S, or 2Fe-2S
# cluster.  Among  them,  ferredoxin  with  one  2Fe-2S cluster per molecule are
# present  in  plants, animals, and bacteria, and form a distinct 2Fe-Ferredoxin
# family  [1,2].  They  are proteins of around one hundred amino acids with four
# conserved  cysteine  residues  to  which  the  2Fe-2S cluster is ligated. This
# conserved region is also found as a domain in various metabolic enzymes.
# 
# Several  structures  of the 2Fe-2S ferredoxin domain have been determined (see
# for example <PDB:4FXC>) [3]. The domain is classified as a beta-grasp which is
# characterized  as  having  a beta-sheet comprised of four beta-strands and one
# alpha-helix  flanking  the  sheet  [4].  The  two  Fe  atoms  are  coordinated
# tetrahedrally by the two inorganic S atoms and four cysteinyl S atoms.
# 
# Some proteins that contains a 2Fe-2S ferredoxin-type domain are listed below:
# 
#  - Ferredoxin from photosynthetic organisms;  namely plants and algae where it
#    is located in the chloroplast or cyanelle; and cyanobacteria.
#  - Ferredoxin from archaebacteria of the Halobacterium genus.
#  - Ferredoxin IV (gene pftA) and V (gene fdxD) from Rhodobacter capsulatus.
#  - Ferredoxin in the  toluene  degradation  operon (gene xylT) and naphthalene
#    degradation operon (gene nahT) of Pseudomonas putida.
#  - Hypothetical Escherichia coli protein yfaE.
# 
#  - The N-terminal domain  of the  bifunctional ferredoxin/ferredoxin reductase
#    electron  transfer  component of the benzoate 1,2-dioxygenase complex (gene
#    benC) from Acinetobacter calcoaceticus, the toluene 4-monooxygenase complex
#    (gene tmoF), the toluate 1,2-dioxygenase system (gene xylZ), and the xylene
#    monooxygenase system (gene xylA) from Pseudomonas.
#  - The N-terminal domain of  phenol  hydroxylase  protein  p5 (gene dmpP) from
#    Pseudomonas Putida.
#  - The N-terminal domain of  methane  monooxygenase   component C  (gene mmoC)
#    from Methylococcus capsulatus .
#  - The C-terminal domain of the vanillate degradation pathway  protein vanB in
#    a Pseudomonas species.
#  - The N-terminal domain of bacterial  fumarate  reductase iron-sulfur protein
#    (gene frdB).
#  - The  N-terminal  domain  of CDP-6-deoxy-3,4-glucoseen reductase (gene ascD)
#    from Yersinia pseudotuberculosis.
#  - The central domain of eukaryotic succinate dehydrogenase (ubiquinone) iron-
#    sulfur protein.
#  - The N-terminal domain of eukaryotic xanthine dehydrogenase.
#  - The N-terminal domain of eukaryotic aldehyde oxidase.
# 
# Three  of  the  four  conserved  cysteines  are clustered together in the same
# region  of  the  protein. Our signature pattern spans that iron-sulfur binding
# region. We also developed a profile that covers the whole domain.
# 
# -Consensus pattern: C-{C}-{C}-[GA]-{C}-C-[GAST]-{CPDEKRHFYW}-C
#                     [The 3 C's are 2Fe-2S ligands]
# -Sequences known to belong to this class detected by the profile: ALL.
# -Other sequence(s) detected in Swiss-Prot: NONE.
# 
# -Sequences known to belong to this class detected by the profile: ALL.
# -Other sequence(s) detected in Swiss-Prot: NONE.
# 
# -Note:  Ferredoxins  from the adrenodoxin subfamily are slightly divergent and
#  are not picked up by our pattern (but they are recognized by the profile). We
#  have  thus  developed  a  second  pattern  specific  for  this subfamily (see
#  <PDOC00642>).
# 
# -Last update: March 2005 / Text revised; profile added.
# 
# [ 1] Meyer J.
#      Trends Ecol. Evol. 3:222-226(1988).
# [ 2] Harayama S., Polissi A., Rekik M.
#      "Divergent evolution of chloroplast-type ferredoxins."
#      FEBS Lett. 285:85-88(1991).
#      PubMed=2065785
# [ 3] Fukuyama K., Ueki N., Nakamura H., Tsukihara T., Matsubara H.
#      "Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis
#      refined at 2.5 A resolution: structural comparisons of plant-type
#      ferredoxins and an electrostatic potential analysis."
#      J. Biochem. 117:1017-1023(1995).
#      PubMed=8586613
# [ 4] Overington J.P.
#      Curr. Opin. Struct. Biol. 2:394-401(1992).
# 
# ***************
# 
# Motif: ANAPHYLATOXIN_1
# Count: 2
# 
# **********************************************
# * Anaphylatoxin domain signature and profile *
# **********************************************
# 
# Anaphylatoxins [1]  are  mediators  of  local inflammatory process that act by
# inducing smooth muscle contraction. There are three  different anaphylatoxins:
# C3a, C4a  and  C5a. They are peptides of about 75 amino-acid residues that are
# derived from the proteolytic degradation of complement C3, C4 and C5 and which
# contains six  disulfide-bonded cysteines [2] (see the schematic representation
# below).
# 
#                           +--------------------+
#             +-------------|------------+       |
#             |             |            |       |
#          xxxCCxxxxxxxxxxxxCxxxxxxxxxxxxCxxxxxxCCxxx
#              |                                |
#              +--------------------------------+
# 
# 'C': conserved cysteine involved in a disulfide bond.
# 
# This cysteine-rich region shares similarity with a three times repeated domain
# found in  the  mammalian extracellular matrix proteins fibulins 1 and 2 [3,4].
# The three disulfide bonds are conserved in the first and last repeats, but the
# first disulfide bond is missing in the second repeat.
# 
# Our consensus pattern spans the entire cysteine-rich domain.
# 
# -Consensus pattern: [CSH]-C-x(2)-[GAP]-x(7,8)-[GASTDEQR]-C-[GASTDEQL]-x(3,9)-
#                     [GASTDEQN]-x(2)-[CE]-x(6,7)-C-C
#                     [The 6 C's are involved in disulfide bonds]
# -Sequences known to belong to this class detected by the pattern: ALL.
# -Other sequence(s) detected in Swiss-Prot: NONE.
# 
# -Sequences known to belong to this class detected by the profile: ALL.
# -Other sequence(s) detected in Swiss-Prot: NONE.
# 
# -Last update: May 2004 / Text revised.
# 
# [ 1] Hugli T.E.
#      "Biochemistry and biology of anaphylatoxins."
#      Complement 3:111-127(1986).
#      PubMed=3542363
# [ 2] Huber R., Scholze H., Paques E.P., Deisenhofer J.
#      "Crystal structure analysis and molecular model of human C3a
#      anaphylatoxin."
#      Hoppe-Seyler's Z. Physiol. Chem. 361:1389-1399(1980).
#      PubMed=7439885
# [ 3] Argraves W.S., Tran H., Burgess W.H., Dickerson K.
#      "Fibulin is an extracellular matrix and plasma glycoprotein with
#      repeated domain structure."
#      J. Cell Biol. 111:3155-3164(1990).
#      PubMed=2269669
# [ 4] Pan T.-C., Sasaki T., Zhang R.-Z., Faessler R., Timpl R., Chu M.L.
#      "Structure and expression of fibulin-2, a novel extracellular matrix
#      protein with multiple EGF-like repeats and consensus motifs for
#      calcium binding."
#      J. Cell Biol. 123:1269-1277(1993).
#      PubMed=8245130
# 
# ***************
# 
# Motif: VWFC_1
# Count: 5
# 
# *************************************
# * VWFC domain signature and profile *
# *************************************
# 
# The VWFC  domain  is named after the von Willebrand factor (VWF) type C repeat
# which is  found  twice  in  this multidomain protein [1,2]. It has a length of
# about 70  amino acids covering 10 well conserved cysteines. Proteins with such
# a domain [1-4] are listed below.
# 
#  - Human  von Willebrand factor  (VWF),  a multifunctional protein involved in
#    maintaining homeostasis.  It consists of 4 VWFD domains,  3 VWFA domains, 3
#    VWFB domains, 3 VWFC domains, an X domain and a C-terminal cystine knot [2].
#  - Silk  moth hemocytin, an humoral lectin which is involved in a self-defence
#    mechanism. It  is  composed  of 2 FA58C domains (see <PDOC00988>), a C-type
#    lectin domain   (see   <PDOC00537>),  2  VWFC  domains,  and  a  CTCK  (see
#    <PDOC00912>).
#  - Several  vertebrate heavily glycosylated  mucins. Human mucin 2 is secreted
#    by the  epithelia  of  different  mucus membrane-containing organs. It is a
#    highly polymorphic  multidomain molecule. Rat intestinal mucin-like peptide
#    coats the  epithelia  of  the  intestines.  Both  proteins  share a modular
#    architecture similar  to  VWF. Xenopus mucin B.1 contains a Sushi domain, a
#    VWFC domain,  a  X  domain and a C-terminal cystine knot. Other mucins that
#    contain the  VWFC  domain  are  human tracheobronchial mucin (MUC5), bovine
#    submaxillary mucin-like protein, human and pig apomucin.
#  - Cef-10/cyr61/CTGF/fisp-12/nov  protein  family.  The members of this family
#    are structurally  related  to   insulin-like growth factor binding proteins
#    (see <PDOC00194>) and could  function  as  growth  factor-binding proteins.
#    They contain an insulin-like growth factor-binding domain, a VWFC repeat, a
#    thrombospondin type 1 repeat (Tsp1) and a C-terminal cystine knot.
#  - Vertebrate  thrombospondins  1  and 2. These adhesive glycoproteins mediate
#    cell-to-cell and cell-to-matrix interactions. They are composed of a common
#    thrombospondin N-terminal  domain  (TspN),  a VWFC domain, three Tsp type 1
#    repeats (Tsp1), 3 to 4 EGF-like domains and 7 calcium-binding Tsp3 repeats.
#  - Vertebrate propeptides of fibrillar collagens alpha 1(I, II & III) and 2(V)
#    chains that  contain  an  N-terminal  VWFC  domain, a collagenous region of
#    about 1000  amino  acids  and  a  C-terminus  common to fibrillar collagens
#    (COLFI domain).
#  - Vertebrate  integral  membrane  protein  DGCR2/IDD,  a  potential  adhesion
#    receptor with  1  LDL-receptor  class  A domain (see <PDOC00929>), a C-type
#    lectin and a VWFC domain.
#  - Chordin, a Xenopus developmental protein that contains four VWFC domains.
# 
# Of these proteins, the best characterized one is the von Willebrand factor for
# which the duplicated VWFC domain is thought to participate in oligomerization,
# but not in  the initial dimerization step [4].  The presence of this region in
# other  complex-forming  proteins leads to the assumption  that the VWFC domain
# might be involved in forming larger protein complexes [1,2].
# 
# The profile we developed covers the entire VWFC domain.
# 
# -Consensus pattern: C-x(2,3)-C-{CG}-C-x(6,14)-C-x(3,4)-C-x(2,10)-C-x(9,16)-
#                     C-C-x(2,4)-C
# -Sequences known to belong to this class detected by the pattern: ALL.
# -Other sequence(s) detected in Swiss-Prot: 7.
# 
# -Sequences known to belong to this class detected by the profile: ALL.
# -Other sequence(s) detected in Swiss-Prot: NONE.
# 
# -Expert(s) to contact by email:
#            Bork P.; bork@embl-heidelberg.de
# 
# -Last update: December 2004 / Pattern and text revised.
# 
# [ 1] Hunt L.T., Barker W.C.
#      "von Willebrand factor shares a distinctive cysteine-rich domain with
#      thrombospondin and procollagen."
#      Biochem. Biophys. Res. Commun. 144:876-882(1987).
#      PubMed=3495268
# [ 2] Bork P.
#      "The modular architecture of a new family of growth regulators related
#      to connective tissue growth factor."
#      FEBS Lett. 327:125-130(1993).
#      PubMed=7687569
# [ 3] Bork P.
#      "Shuffled domains in extracellular proteins."
#      FEBS Lett. 286:47-54(1991).
#      PubMed=1864378
# [ 4] Voorberg J., Fontijn R., Calafat J., Janssen H., van Mourik J.A.,
#      Pannekoek H.
#      "Assembly and routing of von Willebrand factor variants: the
#      requirements for disulfide-linked dimerization reside within the
#      carboxy-terminal 151 amino acids."
#      J. Cell Biol. 113:195-205(1991).
#      PubMed=2007623
# 
# ***************
# 
#
#---------------------------------------