BCCP2_ARATH
ID BCCP2_ARATH Reviewed; 255 AA.
AC Q9LLC1; Q9LF29;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase 2, chloroplastic;
DE Short=AtBCCP2;
DE Short=BCCP-2;
DE Flags: Precursor;
GN Name=BCCP2; OrderedLocusNames=At5g15530; ORFNames=T20K14_140;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- INTERACTION:
CC Q9LLC1; Q9ZST4: GLB1; NbExp=2; IntAct=EBI-15823091, EBI-701245;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11299381}.
CC -!- TISSUE SPECIFICITY: Primarily expressed in 7 to 10 days after flowering
CC seeds at levels approximately 2-fold less abundant than BCCP1.
CC {ECO:0000269|PubMed:11299381}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF223948; AAF80592.1; -; mRNA.
DR EMBL; AL391143; CAC01752.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92173.1; -; Genomic_DNA.
DR EMBL; AY086528; AAM63527.1; -; mRNA.
DR EMBL; BT028902; ABI49449.1; -; mRNA.
DR PIR; T51531; T51531.
DR RefSeq; NP_568316.1; NM_121557.4.
DR AlphaFoldDB; Q9LLC1; -.
DR SMR; Q9LLC1; -.
DR DIP; DIP-58513N; -.
DR IntAct; Q9LLC1; 1.
DR STRING; 3702.AT5G15530.1; -.
DR PaxDb; Q9LLC1; -.
DR PRIDE; Q9LLC1; -.
DR ProteomicsDB; 240650; -.
DR EnsemblPlants; AT5G15530.1; AT5G15530.1; AT5G15530.
DR GeneID; 831406; -.
DR Gramene; AT5G15530.1; AT5G15530.1; AT5G15530.
DR KEGG; ath:AT5G15530; -.
DR Araport; AT5G15530; -.
DR TAIR; locus:2180927; AT5G15530.
DR eggNOG; ENOG502QUI2; Eukaryota.
DR HOGENOM; CLU_016733_1_0_1; -.
DR InParanoid; Q9LLC1; -.
DR OMA; CELIICK; -.
DR OrthoDB; 1492148at2759; -.
DR PhylomeDB; Q9LLC1; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9LLC1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LLC1; baseline and differential.
DR Genevisible; Q9LLC1; AT.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
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 Biotin; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..87
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 88..255
FT /note="Biotin carboxyl carrier protein of acetyl-CoA
FT carboxylase 2, chloroplastic"
FT /id="PRO_0000295893"
FT DOMAIN 178..254
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 148..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 255 AA; 27280 MW; F868E344EAC89CDA CRC64;
MASLSVPCVK ICALNRRVGS LPGISTQRWQ PQPNGISFPS DVSQNHSAFW RLRATTNEVV
SNSTPMTNGG YMNGKAKTNV PEPAELSEFM AKVSGLLKLV DSKDIVELEL KQLDCEIVIR
KKEALQQAVP PAPVYHSMPP VMADFSMPPA QPVALPPSPT PTSTPATAKP TSAPSSSHPP
LKSPMAGTFY RSPGPGEPPF VKVGDKVQKG QIVCIIEAMK LMNEIEAEKS GTIMELLAED
GKPVSVDTPL FVIAP
