ID VPS27_CHAGB Reviewed; 737 AA.
AC Q2GS33;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 27-NOV-2024, entry version 82.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=VPS27; ORFNames=CHGG_09221;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC receptor for ubiquitinated cargo proteins at the multivesicular body
CC (MVB) and recruits ESCRT-I to the MVB outer membrane. {ECO:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- DOMAIN: The FYVE domain is involved in the binding to
CC phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the
CC association to endosomal membranes.
CC -!- DOMAIN: Both IUM domains are necessary for efficient binding to
CC ubiquitin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ85207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAQ85207.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH408034; EAQ85207.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001227148.1; XM_001227147.1.
DR AlphaFoldDB; Q2GS33; -.
DR SMR; Q2GS33; -.
DR STRING; 306901.Q2GS33; -.
DR GeneID; 4394663; -.
DR VEuPathDB; FungiDB:CHGG_09221; -.
DR HOGENOM; CLU_011862_1_0_1; -.
DR InParanoid; Q2GS33; -.
DR OrthoDB; 922060at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:TreeGrafter.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:TreeGrafter.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:TreeGrafter.
DR CDD; cd15735; FYVE_spVPS27p_like; 1.
DR CDD; cd21385; GAT_Vps27; 1.
DR CDD; cd16979; VHS_Vps27; 1.
DR FunFam; 1.20.5.1940:FF:000001; Vacuolar protein sorting-associated protein 27; 1.
DR FunFam; 1.25.40.90:FF:000031; Vacuolar protein sorting-associated protein 27; 1.
DR FunFam; 3.30.40.10:FF:000161; Vacuolar protein sorting-associated protein 27; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 6.10.140.100; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR InterPro; IPR049425; Vps27_GAT-like.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF00790; VHS; 1.
DR Pfam; PF21356; Vps27_GAT-like; 1.
DR PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..737
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292513"
FT DOMAIN 18..150
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 267..286
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 317..336
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 168..228
FT /note="FYVE-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 229..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 80463 MW; A49F9DD9BEDE4624 CRC64;
MMGWWSSGAN NALDEQIDKA TSSSLEDIAL NLEISDIIRS KTVQPKEAMR SLKKRINNKN
PNTQLSALNL TDTCVKNGGA HFLAEIASRE FMESLVSLLK AVGPGTVNAE VRAKILELIQ
SWATAAEGRY ELGYIGEVYK TLQREGYQFP PRVTVASSMI DSNAPPEWVD SDVCMRCRTA
FTFTNRKHHC RNCGNCFDQQ CSTKSLPLPH LGILQAVRVD DGCYAKLTDK SSKASGAPPE
RSFTYSSSPA KPKGSSMQPR NARVDDGFDE DLKKALAMSL EEVKSHSRGY VSSPAANGVT
SNQPKPNGHA APKAVEEEDE DLKAAIAASL ADMEEQKKQH AAALKQQASG AASSSSAAPS
ALPKNDYELT PLEAENINLF STLVDRLQTQ PPGTILREPQ IQELYDSIGA LRPKLARTYG
ETMSKHDTLL DLHARLSTVV RYYDRMLEER LSKAYSQHSI GGYNLPPPRQ APGPYPSLQP
NAPPAAGPAE NFYTGEQQQE YSHPTTHQPY PQPTLAQYGA YDKRGSVSAP SSNQYPPQQV
PQHTGNWGPA SSAQQYGQQP SYPPNEPPQT AQLQQTPNPA HLSAPAPAPN DSIGTTPTAD
PSASFYFSSQ AQQQQQQQQQ QQQQQQQQPQ QVPSSPPDPN MSPYPNLAQP LHSYQPSLPQ
TPASIPAQPS QPQQAHQAPP QAQQPYWQHS AAQQTQLPPV WQPPPSAAYA GYTQESFPSA
PHHAPKQPVV EESLIDL
//
