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AB13B_ARATH
ID   AB13B_ARATH             Reviewed;        1245 AA.
AC   Q9C7F8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=ABC transporter B family member 13;
DE            Short=ABC transporter ABCB.13;
DE            Short=AtABCB13;
DE   AltName: Full=P-glycoprotein 13;
DE   AltName: Full=Putative multidrug resistance protein 15;
GN   Name=ABCB13; Synonyms=MDR15, PGP13; OrderedLocusNames=At1g27940;
GN   ORFNames=F13K9.5;
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, 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}.
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DR   EMBL; AC069471; AAG51482.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30893.1; -; Genomic_DNA.
DR   PIR; G86404; G86404.
DR   RefSeq; NP_174115.1; NM_102559.2.
DR   AlphaFoldDB; Q9C7F8; -.
DR   SMR; Q9C7F8; -.
DR   BioGRID; 24922; 2.
DR   STRING; 3702.AT1G27940.1; -.
DR   PaxDb; Q9C7F8; -.
DR   PRIDE; Q9C7F8; -.
DR   ProteomicsDB; 245143; -.
DR   EnsemblPlants; AT1G27940.1; AT1G27940.1; AT1G27940.
DR   GeneID; 839687; -.
DR   Gramene; AT1G27940.1; AT1G27940.1; AT1G27940.
DR   KEGG; ath:AT1G27940; -.
DR   Araport; AT1G27940; -.
DR   TAIR; locus:2010464; AT1G27940.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   InParanoid; Q9C7F8; -.
DR   OMA; WGSKQVR; -.
DR   OrthoDB; 186078at2759; -.
DR   PhylomeDB; Q9C7F8; -.
DR   BioCyc; ARA:AT1G27940-MON; -.
DR   PRO; PR:Q9C7F8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C7F8; baseline and differential.
DR   Genevisible; Q9C7F8; AT.
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; -; 3.
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   3: Inferred from homology;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1245
FT                   /note="ABC transporter B family member 13"
FT                   /id="PRO_0000227926"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        725..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        805..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        828..848
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        913..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        947..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          47..336
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          372..607
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          681..969
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1004..1240
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   REGION          610..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         406..413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1039..1046
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        778
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1008
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1245 AA;  135776 MW;  FDCE513FC3F14A1C CRC64;
     MDNTERSSNG NIQAETEAKE EKKNIKKESV SLMGLFSAAD KLDYFLMLLG GLGACIHGAT
     LPLFFVFFGK MLDSLGNLST DPKAISSRVS QNALYLVYLG LVNFVSAWIG VSCWMQTGER
     QTARLRINYL KSILAKDITF FDTEARDSNL IFHISSDAIL VQDAIGDKTD HVLRYLSQFI
     AGFVIGFLSV WQLTLLTLGV VPLIAIAGGG YAIVMSTISE KSETAYADAG KVAEEVMSQV
     RTVYAFVGEE KAVKSYSNSL KKALKLGKRS GLAKGLGVGL TYSLLFCAWA LLLWYASLLV
     RHGKTNGAKA FTTILNVIFS GFALGQAAPS LSAIAKGRVA AANIFRMIGN NNSESSQRLD
     EGTTLQNVAG RIEFQKVSFA YPSRPNMVFE NLSFTIRSGK TFAFVGPSGS GKSTIISMVQ
     RFYEPNSGEI LLDGNDIKSL KLKWFREQLG LVSQEPALFA TTIASNILLG KENANMDQII
     EAAKAANADS FIKSLPNGYN TQVGEGGTQL SGGQKQRIAI ARAVLRNPKI LLLDEATSAL
     DAESEKIVQQ ALDNVMEKRT TIVVAHRLST IRNVDKIVVL RDGQVRETGS HSELMLRGGD
     YATLVNCQET EPQENSRSIM SETCKSQAGS SSSRRVSSSR RTSSFRVDQE KTKNDDSKKD
     FSSSSMIWEL IKLNSPEWPY ALLGSIGAVL AGAQTPLFSM GIAYVLTAFY SPFPNVIKRD
     VEKVAIIFAG AGIVTAPIYL LQHYFYTLMG ERLTSRVRLS LFSAILSNEI GWFDLDENNT
     GSLTSILAAD ATLVRSALAD RLSTIVQNLS LTVTALALAF FYSWRVAAVV TACFPLLIAA
     SLTEQLFLKG FGGDYTRAYS RATSVAREAI ANIRTVAAYG AEKQISEQFT CELSKPTKNA
     FVRGHISGFG YGLSQFLAFC SYALGLWYVS VLINHKETNF GDSIKSFMVL IVTAFSVSET
     LALTPDIVKG TQALGSVFRV LHRETKISPD QPNSRMVSQV KGDIEFRNVS FVYPTRPEID
     IFKNLNLRVS AGKSLAVVGP SGSGKSTVIG LIMRFYDPSN GNLCIDGQDI KTLNLRSLRK
     KLALVQQEPA LFSTTIYENI KYGNENASEA EIMEAAKAAN AHEFIIKMEE GYKTHAGDKG
     VQLSGGQKQR VAIARAVLKD PSVLLLDEAT SALDTSSEKL VQEALDKLMK GRTTVLVAHR
     LSTIRKADTV AVLHKGRVVE KGSHRELVSI PNGFYKQLTS LQEVL
 
 
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