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AB11C_ARATH
ID   AB11C_ARATH             Reviewed;        1495 AA.
AC   Q9C8H1; Q9S9R0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=ABC transporter C family member 11;
DE            Short=ABC transporter ABCC.11;
DE            Short=AtABCC11;
DE            EC=7.6.2.2;
DE   AltName: Full=ATP-energized glutathione S-conjugate pump 12;
DE   AltName: Full=Glutathione S-conjugate-transporting ATPase 12;
DE   AltName: Full=Multidrug resistance-associated protein 12;
GN   Name=ABCC11; Synonyms=MRP11, MRP12; OrderedLocusNames=At1g30420;
GN   ORFNames=F26G16.1, T4K22.1;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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.
RX   PubMed=11855639; DOI=10.1007/s004250100661;
RA   Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA   Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT   "Multifunctionality of plant ABC transporters -- more than just
RT   detoxifiers.";
RL   Planta 214:345-355(2002).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12430019; DOI=10.1007/s00425-002-0890-6;
RA   Kolukisaoglu U.H., Bovet L., Klein M., Eggmann T., Geisler M., Wanke D.,
RA   Martinoia E., Schulz B.;
RT   "Family business: the multidrug-resistance related protein (MRP) ABC
RT   transporter genes in Arabidopsis thaliana.";
RL   Planta 216:107-119(2002).
RN   [6]
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).
CC   -!- FUNCTION: Pump for glutathione S-conjugates. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12430019}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF19743.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG51094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009917; AAF19743.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC025295; AAG51094.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31215.1; -; Genomic_DNA.
DR   PIR; F86428; F86428.
DR   RefSeq; NP_001319112.1; NM_001332898.1.
DR   AlphaFoldDB; Q9C8H1; -.
DR   SMR; Q9C8H1; -.
DR   STRING; 3702.AT1G30420.1; -.
DR   PaxDb; Q9C8H1; -.
DR   PRIDE; Q9C8H1; -.
DR   ProteomicsDB; 243293; -.
DR   EnsemblPlants; AT1G30420.1; AT1G30420.1; AT1G30420.
DR   GeneID; 839922; -.
DR   Gramene; AT1G30420.1; AT1G30420.1; AT1G30420.
DR   KEGG; ath:AT1G30420; -.
DR   Araport; AT1G30420; -.
DR   TAIR; locus:2028155; AT1G30420.
DR   eggNOG; KOG0054; Eukaryota.
DR   HOGENOM; CLU_000604_27_6_1; -.
DR   InParanoid; Q9C8H1; -.
DR   OMA; ICALETD; -.
DR   OrthoDB; 138195at2759; -.
DR   PhylomeDB; Q9C8H1; -.
DR   BioCyc; ARA:AT1G30420-MON; -.
DR   PRO; PR:Q9C8H1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C8H1; baseline and differential.
DR   Genevisible; Q9C8H1; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:TAIR.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR   CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR044746; ABCC_6TM_D1.
DR   InterPro; IPR044726; ABCC_6TM_D2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1495
FT                   /note="ABC transporter C family member 11"
FT                   /id="PRO_0000226083"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        907..927
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        949..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1042..1062
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1142..1162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1166..1186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          303..583
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          615..839
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          914..1198
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1235..1469
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         650..657
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1269..1276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   1495 AA;  168104 MW;  9318F5DC045C35F2 CRC64;
     MGFEALNWYC KPIAEGFWEK TPDGAFGAYT PCAIDSLVMI VSNSVLLGLC FYRIWITLYN
     AKAQIYVLRK MYYHCVLWIL ACCCVVEPVL RLVMGISLFD MGDETDLPPF EVASLMVEAF
     AWFAMLVLIG LETKQYVKEF RWYVRFGVVY VLVADAVLLD LVLPLKNSIN RTALYLCISS
     RCCQALFGIL LLVYIPELDL YPDYHILNNE SLDNVEYDAL PGGVNICPER YASIFSGIYF
     SWMTPLMQLG YRKPITERDV WQLDQWDQTE TLIKRFQRCW TEESRRPKPW LLRALNNSLG
     RRFWLGGIFK VGHDLSQFVG PVILSHILQS MIEGDPAWVG YVYAFLIFFG VTFGVLCQSQ
     YFQHVGRVGF RLRSTLVAAI FHKSLRLTNK ARKNFASGKV TNMITTDANA LQLIAEQLHG
     LWSAPFRIIV SMVLLYQQLG VASIFGSLIL FLLIPFQTLI VRKMRKLTKE GLQWTDKRVG
     IIYEILASMD IVKCYAWEKS FESRIQGIRN EELSWFRKAQ LLSAFNSFIL NSTPVVVTLV
     SFGVYVLLGG DLTPARAFTS LSLFAVLRSP LSTLPNLISQ AVNANVSLQR IEELLLSEER
     ILAQNPPLQP GAPAISIKNG YFSWDSKTSK PTLSDINLEI PVGSLVAIVG GTGEGKTSLI
     SAMLGELSHA ETSSVDIRGS VAYVPQVSWI FNATLRENIL FGSDFESERY WRAIDVTALQ
     HDLDLFPGRD RTEIGERGVN ISGGQKQRVS MARAVYSNSD IYIFDDPFSA LDAHVAHQVF
     DSCVKHELKG KTRVLVTNQL HFLPLMDRII LVSEGMIKEE GNFAELSKSG TLFKKLMENA
     GKMDATQEVN TNDENISKLG PTVTIDVSER SLGSIQQGKW GRSMLVKQEE RETGIISWDV
     VMRYNKAVGG LWVVMILLVC YLTTEVLRVL SSTWLSIWTD QSTPKSYSPG FYIVVYALLG
     FGQVAVTFTN SFWLISSSLH AAKRLHDAML NSILRAPMLF FETNPTGRVI NRFSKDIGDI
     DRNVANLMNM FMNQLWQLLS TFALIGIVST ISLWAIMPLL ILFYATYIYY QSTSREVRRL
     DSVTRSPIYA LFGEALNGLS SIRAYKAYDR MAKINGKSMD NNIRFTLAST SSNRWLTIRS
     ESLGGVMIWL TATFAVLRYG NAENQAVFAS TMGLLLSYTL NITTLLSGVL RQASKAENSL
     NSVERVGNYI DLPSEATAII ENNRPVSGWP SRGSIQFEDV HLRYRPGLPP VLHGLSFFVY
     PSEKVGVVGR TGAGKSSMLN ALYRIVELEK GRILIDDYDV AKFGLTDLRR VLSIIPQSPV
     LFSGTVRFNI DPFSEHNDAD LWEALERAHI KDVIDRNPFG LDAEVSEGGE NFSVGQRQLL
     SLARALLRRS KILFLDEATA SVDVRTDSLI QRTIREEFKS CTMLIIAHRL NTIIDCDKIL
     VLSSGQVLEY DSPQELLSRD TSAFFKMVHS TGPENGQYLS NLVFERRGNG MSQGG
 
 
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