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AB12C_ARATH
ID   AB12C_ARATH             Reviewed;        1495 AA.
AC   Q9C8H0; F4I4U8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=ABC transporter C family member 12;
DE            Short=ABC transporter ABCC.12;
DE            Short=AtABCC12;
DE            EC=7.6.2.2;
DE   AltName: Full=ATP-energized glutathione S-conjugate pump 13;
DE   AltName: Full=Glutathione S-conjugate-transporting ATPase 13;
DE   AltName: Full=Multidrug resistance-associated protein 13;
GN   Name=ABCC12; Synonyms=MRP12, MRP13; OrderedLocusNames=At1g30410;
GN   ORFNames=T4K22.13;
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}.
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DR   EMBL; AC025295; AAG51100.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60872.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60873.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60875.1; -; Genomic_DNA.
DR   PIR; E86428; E86428.
DR   RefSeq; NP_001323123.1; NM_001332893.1.
DR   RefSeq; NP_001323124.1; NM_001332895.1.
DR   RefSeq; NP_001323126.1; NM_001332897.1.
DR   AlphaFoldDB; Q9C8H0; -.
DR   SMR; Q9C8H0; -.
DR   STRING; 3702.AT1G30410.1; -.
DR   TCDB; 3.A.1.208.43; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q9C8H0; -.
DR   PRIDE; Q9C8H0; -.
DR   ProteomicsDB; 245098; -.
DR   EnsemblPlants; AT1G30410.2; AT1G30410.2; AT1G30410.
DR   EnsemblPlants; AT1G30410.4; AT1G30410.4; AT1G30410.
DR   EnsemblPlants; AT1G30410.6; AT1G30410.6; AT1G30410.
DR   GeneID; 839921; -.
DR   Gramene; AT1G30410.2; AT1G30410.2; AT1G30410.
DR   Gramene; AT1G30410.4; AT1G30410.4; AT1G30410.
DR   Gramene; AT1G30410.6; AT1G30410.6; AT1G30410.
DR   KEGG; ath:AT1G30410; -.
DR   Araport; AT1G30410; -.
DR   eggNOG; KOG0054; Eukaryota.
DR   HOGENOM; CLU_000604_27_3_1; -.
DR   InParanoid; Q9C8H0; -.
DR   OrthoDB; 138195at2759; -.
DR   PhylomeDB; Q9C8H0; -.
DR   BioCyc; ARA:AT1G30410-MON; -.
DR   PRO; PR:Q9C8H0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C8H0; baseline and differential.
DR   Genevisible; Q9C8H0; 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; IBA:GO_Central.
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 12"
FT                   /id="PRO_0000226084"
FT   TRANSMEM        38..58
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        173..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        303..323
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        558..578
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        1140..1160
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;  167956 MW;  D29EF05C6D6BDE13 CRC64;
     MGFEALNWYC KPVADGFWEK AVDGAFGAYT PCAIDSLVML VSHFVLLGLC FYRIWIIFHN
     TKAQIYVLRK KYYNCVLGLL ACYCVVEPVL RLVMGISLFD MDEETDFPPF EVASLMVEAF
     AWFSMLVLIG LETKQYVKEF RWYVRFGVLY VLVADAVLLD LVLPLKNSIN RTALYLFISS
     RCSQALFGIL LLIYIPELDP YPGYHIVNNE PLDNVEYDAL RGGEHICPER HASIFSRIYF
     GWITPLMQLG YRKPITEKDV WQLDKWDQTE TLIKRFQRCW TEESRRPKPW LLRALNNSLG
     GRFWLAGIFK IGNDLSQFVG PVILSHLLRS MQEGDPAWVG YVYAFIIFVG VTLGVLCEAQ
     YFQNVWRVGF RLRSTLVAAI FHKSLRLTHE ARKNFASGKV TNMITTDANA LQQISQQLHG
     LWSAPFRIIV SMILLYQQLG VASLFGSLIL FLLIPLQTLI ISKMRKLTKE GLQWTDKRVG
     ITNEILSSMD TVKCYAWEKS FESRIQGIRN EELSWFRKAQ LLSAFNSFIL NSIPVVVTVV
     SFGVFVLLGG DLTPARAFTS LSLFAVLRFP LNMLPNLLSQ VVNANVSLQR IEELLLSEER
     ILAQNPPLQP GTPAISIKNG YFSWDSKTTK PTLSDINLEI PVGTLVAIVG GTGEGKTSLI
     SAMLGELSHA ETTSVVIRGS VAYVPQVSWI FNATVRENIL FGSDFESERY WRAIDATALQ
     HDLDLLPGRD LTEIGERGVN ISGGQKQRVS MARAVYSNSD VYIFDDPLSA LDAHVAHQVF
     DSCMKDELRG KTRVLVTNQL HFLPLMDKII LVSEGMIKEE GTFVELSKSG ILFKKLMENA
     GKMDATQEVN TNDENILKLG PTVTVDVSER NLGSTKQGKR RRSVLIKQEE RETGIISWNV
     LMRYKEAVGG LWVVMILLAC YLATEVLRVS SSTWLSIWTD QSTSKNYSPG FYIVVYALLG
     FGQVAVTFTN SFWLITSSLH AARRLHDAML SSILRAPMLF FHTNPTGRVI NRFSKDIGDI
     DRNVANLMNM FMNQLWQLLS TFALIGTVST ISLWAIMPLL ILFYAAYLYY QSTSREVRRL
     DSVTRSPIYA QFGEALNGLS SIRAYKAYDR MAKINGKSMD NNIRFTLANT SSNRWLTIRL
     ETLGGVMIWL TATFAVLQNG NTNNQAGFAS TMGLLLSYTL NITSLLSGVL RQASRAENSL
     NSVERVGNYI DLPSEATDII ENNRPVCGWP SGGSIKFEDV HLRYRPGLPP VLHGLTFFVS
     PSEKVGVVGR TGAGKSSMLN ALFRIVEVEK GRIMIDDCDV AKFGLTDVRR VLSIIPQSPV
     LFSGTVRFNI DPFSEHNDAG LWEALHRAHI KDVISRNPFG LDAEVCEGGE NFSVGQRQLL
     SLARALLRRS KILVLDEATA SVDVRTDSLI QRTIREEFKS CTMLVIAHRL NTIIDCDKIL
     VLSSGQVLEY DSPQELLSRD TSAFFRMVHS TGPANAQYLS NLVFERRENG MSVGG
 
 
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