GenomeNet

Database: UniProt
Entry: Q9LLC1
LinkDB: Q9LLC1
Original site: Q9LLC1 
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   16-JAN-2019, entry version 102.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   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
RT   protein 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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   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
RT   reference 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
CC       biotin carboxyl carrier protein, biotin carboxylase and 2 subunits
CC       each of ACCase subunit alpha and ACCase plastid-coded subunit beta
CC       (accD).
CC   -!- INTERACTION:
CC       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
CC       flowering seeds at levels approximately 2-fold less abundant than
CC       BCCP1. {ECO:0000269|PubMed:11299381}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC01752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   UniGene; At.20538; -.
DR   UniGene; At.69216; -.
DR   ProteinModelPortal; Q9LLC1; -.
DR   SMR; Q9LLC1; -.
DR   DIP; DIP-58513N; -.
DR   IntAct; Q9LLC1; 1.
DR   STRING; 3702.AT5G15530.1; -.
DR   PaxDb; Q9LLC1; -.
DR   PRIDE; Q9LLC1; -.
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; ENOG410IWH6; Eukaryota.
DR   eggNOG; COG0511; LUCA.
DR   HOGENOM; HOG000008876; -.
DR   InParanoid; Q9LLC1; -.
DR   KO; K02160; -.
DR   OMA; MAGLQMA; -.
DR   OrthoDB; 1492148at2759; -.
DR   PhylomeDB; Q9LLC1; -.
DR   BioCyc; ARA:GQT-2156-MONOMER; -.
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:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     87       Chloroplast. {ECO:0000255}.
FT   CHAIN        88    255       Biotin carboxyl carrier protein of
FT                                acetyl-CoA carboxylase 2, chloroplastic.
FT                                /FTId=PRO_0000295893.
FT   DOMAIN      178    254       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   MOD_RES     220    220       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-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
//
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