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AB9A_ARATH
ID   AB9A_ARATH              Reviewed;         950 AA.
AC   Q9FLT5; F4K3L7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=ABC transporter A family member 9;
DE            Short=ABC transporter ABCA.9;
DE            Short=AtABCA9;
DE   AltName: Full=ABC2 homolog 11;
GN   Name=ABCA9; Synonyms=ATH11; OrderedLocusNames=At5g61730; ORFNames=MAC9.4;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
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   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA   Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT   "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL   J. Biol. Chem. 276:30231-30244(2001).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA   Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA   Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA   Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT   "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL   Trends Plant Sci. 13:151-159(2008).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, BIOTECHNOLOGY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=23269834; DOI=10.1073/pnas.1214159110;
RA   Kim S., Yamaoka Y., Ono H., Kim H., Shim D., Maeshima M., Martinoia E.,
RA   Cahoon E.B., Nishida I., Lee Y.;
RT   "AtABCA9 transporter supplies fatty acids for lipid synthesis to the
RT   endoplasmic reticulum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:773-778(2013).
CC   -!- FUNCTION: Mediates the transport of acyl-CoAs and/or free fatty acids
CC       to the endoplasmic reticulum. Has no effect on the selectivity of fatty
CC       acid incorporation into triacylglycerol or further desaturation steps.
CC       {ECO:0000269|PubMed:23269834}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:23269834}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:23269834}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in siliques. Detected in
CC       seedlings, rosette leaves, stems and flowers.
CC       {ECO:0000269|PubMed:23269834}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the middle and late stages of
CC       seed development. {ECO:0000269|PubMed:23269834}.
CC   -!- DISRUPTION PHENOTYPE: Reduced seed size with abnormal morphology and
CC       reduced triacylglycerol content. Retarded growth on medium lacking
CC       sucrose. {ECO:0000269|PubMed:23269834}.
CC   -!- BIOTECHNOLOGY: Overexpression of ABCA9 increases seed oil content.
CC       {ECO:0000269|PubMed:23269834}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC       CPR flippase (TC 3.A.1.211) subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AED97510.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB010069; BAB10073.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97510.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; ANM69292.1; -; Genomic_DNA.
DR   RefSeq; NP_001330984.1; NM_001345493.1.
DR   RefSeq; NP_200981.1; NM_125567.2.
DR   AlphaFoldDB; Q9FLT5; -.
DR   SMR; Q9FLT5; -.
DR   STRING; 3702.AT5G61730.1; -.
DR   TCDB; 3.A.1.211.20; the atp-binding cassette (abc) superfamily.
DR   iPTMnet; Q9FLT5; -.
DR   PaxDb; Q9FLT5; -.
DR   PRIDE; Q9FLT5; -.
DR   ProteomicsDB; 244532; -.
DR   EnsemblPlants; AT5G61730.2; AT5G61730.2; AT5G61730.
DR   GeneID; 836295; -.
DR   Gramene; AT5G61730.2; AT5G61730.2; AT5G61730.
DR   KEGG; ath:AT5G61730; -.
DR   Araport; AT5G61730; -.
DR   eggNOG; KOG0059; Eukaryota.
DR   HOGENOM; CLU_000604_19_5_1; -.
DR   InParanoid; Q9FLT5; -.
DR   OrthoDB; 131191at2759; -.
DR   PRO; PR:Q9FLT5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLT5; baseline and differential.
DR   Genevisible; Q9FLT5; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR   GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR   GO; GO:0048316; P:seed development; IMP:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR026082; ABCA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19229; PTHR19229; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Endoplasmic reticulum; Lipid transport; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..950
FT                   /note="ABC transporter A family member 9"
FT                   /id="PRO_0000240330"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          520..765
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         566..573
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   950 AA;  105431 MW;  BEC9BE912192DB5E CRC64;
     MTLREGLPLF HQQFTALFKK NLLLSWRNKR ATCLHLFSSF FFILLIFSIE ESSKASDLTS
     TRHKNVTDPK ALVSLPILPC EDKFFVRLPC FDFVWSGNQS RRVTDIVSAI MANNPGRPIP
     TNKVQSFTKP EEVDAWFMSH PSQVTGALHF VEKNATVISY GIQTNSSSEK KRGRREDPTF
     KFLVPLQIAA EREIARSLIG DPKFSWDFGF KEFARPAIGG EVIISAFYLM GPVFFLAFSM
     FGFVLQLGSV VTEKELKLRE AMTTMGVYES AYWLSWLIWE GILTFVSSLF LVLFGMMFQF
     EFFLKNSFVL VFLLFFLFQF NMIGLAFALS SIISKSSSAT TVGFLVFLVG FITQIVTTAG
     FPYSSAYSIG SRVIWSLFPP NTFSAGLQLL LEATSSPGDS GISWSERAIC AGGESTCVIT
     TNKIYIWLVG TFFFWFVLAL YFDNIIPNAS GVRKSIFYFL KPSYWTGKEG NKVEEGSICS
     CIGSVPPVEH ITPEDEDVLE EEILVKQQAM DGRVDPNIAV QIHGLAKTYP GTTKLGCCKC
     TKTSPFHAVK GLWMNIAKDQ LFCLLGPNGA GKTTTISCLT GINPVTGGDA KIYGNSIRSS
     VGMSNIRKMI GVCPQFDILW DALSSEEHLH LFASIKGLPP SSIKSIAEKL LVDVKLTGSA
     KIRAGSYSGG MKRRLSVAIA LIGDPKLVFL DEPTTGMDPI TRRHVWDIIQ ESKKGRAIIL
     TTHSMEEADI LSDRIGIMAK GRLRCIGTSI RLKSRFGTGF VATVSFIENK KDGAPEPLKR
     FFKERLKVEP TEENKAFMTF VIPHDKEQLL KGFFAELQDR ESEFGIADIQ LGLATLEEVF
     LNIARRAELE SATVEGTMVT LELESGIAVE IPVGARFVGI PGTENAENPR GLMVEVYWQQ
     DGSGSMCISG HSAEMRIPEN VSVIYEPSSQ VLGHGQRRVR GIVIDYESNN
 
 
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