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AB12B_ARATH
ID   AB12B_ARATH             Reviewed;        1273 AA.
AC   Q9FWX8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=ABC transporter B family member 12;
DE            Short=ABC transporter ABCB.12;
DE            Short=AtABCB12;
DE   AltName: Full=Multidrug resistance protein 16;
DE   AltName: Full=P-glycoprotein 12;
GN   Name=ABCB12; Synonyms=MDR16, PGP12; OrderedLocusNames=At1g02530;
GN   ORFNames=T14P4.14;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG10627.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AK228647; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC022521; AAG10627.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE27441.1; -; Genomic_DNA.
DR   EMBL; AK228647; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; F86155; F86155.
DR   RefSeq; NP_171754.1; NM_100134.4.
DR   AlphaFoldDB; Q9FWX8; -.
DR   SMR; Q9FWX8; -.
DR   BioGRID; 24517; 1.
DR   STRING; 3702.AT1G02530.1; -.
DR   PaxDb; Q9FWX8; -.
DR   PRIDE; Q9FWX8; -.
DR   ProteomicsDB; 245140; -.
DR   EnsemblPlants; AT1G02530.1; AT1G02530.1; AT1G02530.
DR   GeneID; 839282; -.
DR   Gramene; AT1G02530.1; AT1G02530.1; AT1G02530.
DR   KEGG; ath:AT1G02530; -.
DR   Araport; AT1G02530; -.
DR   TAIR; locus:2196135; AT1G02530.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   InParanoid; Q9FWX8; -.
DR   OMA; FGYMQIS; -.
DR   OrthoDB; 186078at2759; -.
DR   PhylomeDB; Q9FWX8; -.
DR   BioCyc; ARA:AT1G02530-MON; -.
DR   PRO; PR:Q9FWX8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FWX8; baseline and differential.
DR   Genevisible; Q9FWX8; AT.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; 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:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 1.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
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; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1273
FT                   /note="ABC transporter B family member 12"
FT                   /id="PRO_0000227927"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        706..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        746..766
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        840..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        927..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        961..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          45..333
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          368..604
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          705..992
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1027..1266
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         403..410
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1062..1069
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        555
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        648
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        801
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        279
FT                   /note="I -> T (in Ref. 3; AK228647)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1273 AA;  136774 MW;  1CCA06FB3D472241 CRC64;
     MNRDGAGEGD SVSHEHSTSK TDEKAKTVPL YKLFAFADSF DVFLMICGSL GAIGNGVCLP
     LMTLLFGDLI DSFGKNQNNK DIVDVVSKVC LKFVYLGLGR LGAAFLQVAC WMITGERQAA
     KIRSNYLKTI LRQDIGFFDV ETNTGEVVGR MSGDTVHIQD AMGEKVGKFI QLVSTFVGGF
     ALAFAKGWLL TLVMLTSIPF LAMAGAAMAL LVTRASSRGQ AAYAKAATVV EQTIGSIRTV
     ASFTGEKQAI NSYKKYITSA YKSSIQQGFS TGLGLGVMIY VFFSSYALAI WFGGKMILEK
     GYTGGSVINV IIIVVAGSMS LGQTSPCVTA FAAGQAAAYK MFETIKRKPL IDAYDVNGKV
     LGDIRGDIEL KDVHFSYPAR PDEEIFDGFS LFIPSGATAA LVGESGSGKS TVINLIERFY
     DPKAGEVLID GINLKEFQLK WIRSKIGLVC QEPVLFSSSI MENIAYGKEN ATLQEIKVAT
     ELANAAKFIN NLPQGLDTKV GEHGTQLSGG QKQRIAIARA ILKDPRVLLL DEATSALDTE
     SERVVQEALD RVMVNRTTVV VAHRLSTVRN ADMIAVIHSG KMVEKGSHSE LLKDSVGAYS
     QLIRCQEINK GHDAKPSDMA SGSSFRNSNL NISREGSVIS GGTSSFGNSS RHHSLNVLGL
     FAGLDLGSGS QRVGQEETGT TSQEPLRKVS LTRIAALNKP EIPVLLLGTV VAAINGAIFP
     LFGILISRVI EAFFKPADQL KKDSRFWAII FVALGVTSLI VSPSQMYLFA VAGGKLIRRI
     QSMCFEKAVH MEVSWFDEPE NSSGTMGARL STDAALIRAL VGDALSLAVQ NAASAASGLI
     IAFTASWELA LIILVMLPLI GINGFLQVKF MKGFSADAKS KYEEASQVAN DAVGSIRTVA
     SFCAEEKVMQ MYNKQCEGPI KDGVKQGFIS GLGFGFSFFI LFCVYATSFY AAARLVEDGK
     TTFIDVFQVF FALTMAAIGI SQSSTFAPDS SKAKVAAASI FAIIDRKSKI DSSDETGTVL
     ENVKGDIELR HLSFTYPARP GIQIFRDLCL TIRAGKTVAL VGESGSGKST VISLLQRFYD
     PDSGQITLDG VELKKLQLKW LRQQMGLVGQ EPVLFNDTIR ANIAYGKGSE EAATESEIIA
     AAELANAHKF ISSIQQGYDT VVGEKGIQLS GGQKQRVAIA RAIVKEPKIL LLDEATSALD
     AESERLVQDA LDRVIVNRTT VVVAHRLSTI KNADVIAIVK NGVIAENGTH ETLIKIDGGV
     YASLVQLHMT ASN
 
 
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