BCCP1_ARATH
ID BCCP1_ARATH Reviewed; 280 AA.
AC Q42533; O04845; Q9LL78;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase 1, chloroplastic;
DE Short=AtBCCP1;
DE Short=BCCP-1;
DE Flags: Precursor;
GN Name=BCCP1; Synonyms=CAC1; OrderedLocusNames=At5g16390; ORFNames=MQK4.12;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7480350; DOI=10.1104/pp.109.2.619;
RA Choi J.K., Yu F., Wurtele E.S., Nikolau B.J.;
RT "Molecular cloning and characterization of the cDNA coding for the biotin-
RT containing subunit of the chloroplastic acetyl-coenzyme A carboxylase.";
RL Plant Physiol. 109:619-625(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9046589; DOI=10.1104/pp.113.2.357;
RA Ke J., Choi J.K., Smith M., Horner H.T., Nikolau B.J., Wurtele E.S.;
RT "Structure of the CAC1 gene and in situ characterization of its expression.
RT The Arabidopsis thaliana gene coding for the biotin-containing subunit of
RT the plastidic acetyl-coenzyme A carboxylase.";
RL Plant Physiol. 113:357-365(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11299381; DOI=10.1104/pp.125.4.2016;
RA Thelen J.J., Mekhedov S., Ohlrogge J.B.;
RT "Brassicaceae express multiple isoforms of biotin carboxyl carrier protein
RT in a tissue-specific manner.";
RL Plant Physiol. 125:2016-2028(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [5]
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 [6]
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 [7]
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 [8]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10759501; DOI=10.1104/pp.122.4.1057;
RA Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.;
RT "Coordinate regulation of the nuclear and plastidic genes coding for the
RT subunits of the heteromeric acetyl-coenzyme A carboxylase.";
RL Plant Physiol. 122:1057-1071(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and 2 subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11299381, ECO:0000269|PubMed:18431481}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42533-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Present in developing tissues from roots, leaves,
CC flowers, siliques and seeds (at protein level).
CC {ECO:0000269|PubMed:10759501, ECO:0000269|PubMed:11299381}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23155; AAC49114.1; -; mRNA.
DR EMBL; U62029; AAB51193.1; -; Genomic_DNA.
DR EMBL; AF236873; AAF80594.1; -; mRNA.
DR EMBL; AB005242; BAB09606.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92286.1; -; Genomic_DNA.
DR EMBL; AY054617; AAK96808.1; -; mRNA.
DR EMBL; AY072460; AAL66875.1; -; mRNA.
DR EMBL; AY087857; AAM65409.1; -; mRNA.
DR RefSeq; NP_197143.1; NM_121644.4. [Q42533-1]
DR AlphaFoldDB; Q42533; -.
DR SMR; Q42533; -.
DR BioGRID; 16776; 1.
DR DIP; DIP-58514N; -.
DR IntAct; Q42533; 1.
DR STRING; 3702.AT5G16390.1; -.
DR PaxDb; Q42533; -.
DR PRIDE; Q42533; -.
DR ProteomicsDB; 240649; -. [Q42533-1]
DR EnsemblPlants; AT5G16390.1; AT5G16390.1; AT5G16390. [Q42533-1]
DR GeneID; 831500; -.
DR Gramene; AT5G16390.1; AT5G16390.1; AT5G16390. [Q42533-1]
DR KEGG; ath:AT5G16390; -.
DR Araport; AT5G16390; -.
DR TAIR; locus:2171307; AT5G16390.
DR eggNOG; ENOG502QUI2; Eukaryota.
DR HOGENOM; CLU_016733_1_0_1; -.
DR InParanoid; Q42533; -.
DR OMA; SPAQYVM; -.
DR PhylomeDB; Q42533; -.
DR BioCyc; ARA:AT5G16390-MON; -.
DR BioCyc; MetaCyc:AT5G16390-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q42533; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42533; baseline and differential.
DR Genevisible; Q42533; AT.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001249; AcCoA_biotinCC.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR PRINTS; PR01071; ACOABIOTINCC.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00531; BCCP; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biotin; Chloroplast; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 83..280
FT /note="Biotin carboxyl carrier protein of acetyl-CoA
FT carboxylase 1, chloroplastic"
FT /id="PRO_0000002831"
FT DOMAIN 203..279
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 52..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 267..280
FT /note="KPVSLDTPLFVVQP -> SLSASTLLCLWFN (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="P -> PVESAP (in Ref. 1; AAC49114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 29613 MW; F2580372B92A257A CRC64;
MASSSFSVTS PAAAASVYAV TQTSSHFPIQ NRSRRVSFRL SAKPKLRFLS KPSRSSYPVV
KAQSNKVSTG ASSNAAKVDG PSSAEGKEKN SLKESSASSP ELATEESISE FLTQVTTLVK
LVDSRDIVEL QLKQLDCELV IRKKEALPQP QAPASYVMMQ QPNQPSYAQQ MAPPAAPAAA
APAPSTPASL PPPSPPTPAK SSLPTVKSPM AGTFYRSPAP GEPPFIKVGD KVQKGQVLCI
VEAMKLMNEI ESDHTGTVVD IVAEDGKPVS LDTPLFVVQP
