ACP1_ARATH
ID ACP1_ARATH Reviewed; 137 AA.
AC P11829;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Acyl carrier protein 1, chloroplastic;
DE Short=ACP-1;
DE Flags: Precursor;
GN Name=ACP1; OrderedLocusNames=At3g05020; ORFNames=T9J14.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2922299; DOI=10.1093/nar/17.4.1777;
RA Post-Beittenmiller M.A., Hlousek-Radojcic A., Ohlrogge J.B.;
RT "DNA sequence of a genomic clone encoding an Arabidopsis acyl carrier
RT protein (ACP).";
RL Nucleic Acids Res. 17:1777-1777(1989).
RN [2]
RP SEQUENCE REVISION.
RA Post-Beittenmiller M.A.;
RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHARACTERIZATION.
RX PubMed=16668615; DOI=10.1104/pp.98.1.206;
RA Hlousek-Radojcic A., Post-Beittenmiller D., Ohlrogge J.B.;
RT "Expression of constitutive and tissue-specific acyl carrier protein
RT isoforms in Arabidopsis.";
RL Plant Physiol. 98:206-214(1992).
RN [8]
RP FUNCTION.
RX PubMed=11553750; DOI=10.1104/pp.127.1.222;
RA Branen J.K., Chiou T.J., Engeseth N.J.;
RT "Overexpression of acyl carrier protein-1 alters fatty acid composition of
RT leaf tissue in Arabidopsis.";
RL Plant Physiol. 127:222-229(2001).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis. {ECO:0000269|PubMed:11553750}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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 -!- MISCELLANEOUS: Plants over-expressing ACP1 show altered composition of
CC fatty acids, with significant decrease in levels of hexadecatrienoic
CC acid (16:3) and increase in linolenate (18:3) content.
CC {ECO:0000305|PubMed:11553750}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; X13708; CAA31991.1; -; Genomic_DNA.
DR EMBL; AC009465; AAG51406.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74176.1; -; Genomic_DNA.
DR EMBL; BT006397; AAP21205.1; -; mRNA.
DR EMBL; AY085288; AAM62520.1; -; mRNA.
DR PIR; S03267; S03267.
DR RefSeq; NP_187153.1; NM_111374.2.
DR AlphaFoldDB; P11829; -.
DR SMR; P11829; -.
DR STRING; 3702.AT3G05020.1; -.
DR iPTMnet; P11829; -.
DR PaxDb; P11829; -.
DR PRIDE; P11829; -.
DR ProteomicsDB; 244352; -.
DR EnsemblPlants; AT3G05020.1; AT3G05020.1; AT3G05020.
DR GeneID; 819664; -.
DR Gramene; AT3G05020.1; AT3G05020.1; AT3G05020.
DR KEGG; ath:AT3G05020; -.
DR Araport; AT3G05020; -.
DR TAIR; locus:2114820; AT3G05020.
DR eggNOG; KOG1748; Eukaryota.
DR HOGENOM; CLU_108696_1_0_1; -.
DR InParanoid; P11829; -.
DR OMA; RVQVMCS; -.
DR OrthoDB; 1473625at2759; -.
DR PhylomeDB; P11829; -.
DR PRO; PR:P11829; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P11829; baseline and differential.
DR Genevisible; P11829; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0000036; F:acyl carrier activity; IDA:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; TAS:TAIR.
DR Gene3D; 1.10.1200.10; -; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR044813; ACP_chloroplastic.
DR InterPro; IPR003231; Acyl_carrier.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR46153; PTHR46153; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR00517; acyl_carrier; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT CHAIN 55..137
FT /note="Acyl carrier protein 1, chloroplastic"
FT /id="PRO_0000000568"
FT DOMAIN 58..133
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 93
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 137 AA; 15055 MW; 6AA3431A78640C6D CRC64;
MATQFSASVS LQTSCLATTR ISFQKPALIS NHGKTNLSFN LRRSIPSRRL SVSCAAKQET
IEKVSAIVKK QLSLTPDKKV VAETKFADLG ADSLDTVEIV MGLEEEFNIQ MAEEKAQKIA
TVEQAAELIE ELINEKK
