ID ACP2_SPIOL Reviewed; 130 AA.
AC P23235;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Acyl carrier protein 2, chloroplastic;
DE AltName: Full=Acyl carrier protein II;
DE Short=ACP II;
DE Flags: Precursor;
GN Name=ACL1.2;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ferry Morse Hyb.424; TISSUE=Root;
RX PubMed=2102885; DOI=10.1007/bf00016126;
RA Schmid K.M., Ohlrogge J.B.;
RT "A root acyl carrier protein-II from spinach is also expressed in leaves
RT and seeds.";
RL Plant Mol. Biol. 15:765-778(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=3891750; DOI=10.1016/s0021-9258(17)39559-5;
RA Ohlrogge J.B., Kuo T.M.;
RT "Plants have isoforms for acyl carrier protein that are expressed
RT differently in different tissues.";
RL J. Biol. Chem. 260:8032-8037(1985).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Roots, leaves and seeds.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-ACP by acpS. This modification is essential for activity because
CC fatty acids are bound in thioester linkage to the sulfhydryl of the
CC prosthetic group (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; X52065; CAA36288.1; -; mRNA.
DR PIR; S12310; S12310.
DR AlphaFoldDB; P23235; -.
DR SMR; P23235; -.
DR OrthoDB; 180066at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP001155700; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR003231; ACP.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR044813; ACP_chloroplastic.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR00517; acyl_carrier; 1.
DR PANTHER; PTHR46153; ACYL CARRIER PROTEIN; 1.
DR PANTHER; PTHR46153:SF20; ACYL CARRIER PROTEIN 2, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Phosphopantetheine; Phosphoprotein; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT CHAIN 49..130
FT /note="Acyl carrier protein 2, chloroplastic"
FT /id="PRO_0000000585"
FT DOMAIN 52..127
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 87
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 130 AA; 14098 MW; 87238CB3526BC4FB CRC64;
MASITGSSVS FKCAPLQSSF NSKNYALKSS VTFWRRTPVM PRGLSVSCAA KPEMVTKVSD
IVKSQLALAE DAKVTGETKF SEIGADSLDT VEIVMKLEEE FGVTVEEENA QTITTIQEAA
DMIEALQQNK
//
