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AB16B_ARATH
ID   AB16B_ARATH             Reviewed;        1228 AA.
AC   Q9LSJ8; Q8RXD2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=ABC transporter B family member 16;
DE            Short=ABC transporter ABCB.16;
DE            Short=AtABCB16;
DE   AltName: Full=Multidrug resistance protein 18;
DE   AltName: Full=P-glycoprotein 16;
GN   Name=ABCB16; Synonyms=MDR18, PGP16; OrderedLocusNames=At3g28360;
GN   ORFNames=MFJ20.4;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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] OF 612-1228.
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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=AAL91219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB026644; BAB02852.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77437.1; -; Genomic_DNA.
DR   EMBL; AY081330; AAL91219.1; ALT_INIT; mRNA.
DR   EMBL; BT008368; AAP37727.1; -; mRNA.
DR   RefSeq; NP_189477.4; NM_113756.5.
DR   AlphaFoldDB; Q9LSJ8; -.
DR   SMR; Q9LSJ8; -.
DR   BioGRID; 7794; 7.
DR   IntAct; Q9LSJ8; 6.
DR   STRING; 3702.AT3G28360.1; -.
DR   PaxDb; Q9LSJ8; -.
DR   PRIDE; Q9LSJ8; -.
DR   ProteomicsDB; 245120; -.
DR   EnsemblPlants; AT3G28360.1; AT3G28360.1; AT3G28360.
DR   GeneID; 822465; -.
DR   Gramene; AT3G28360.1; AT3G28360.1; AT3G28360.
DR   KEGG; ath:AT3G28360; -.
DR   Araport; AT3G28360; -.
DR   TAIR; locus:2088912; AT3G28360.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   InParanoid; Q9LSJ8; -.
DR   OMA; QRIAYHE; -.
DR   OrthoDB; 186078at2759; -.
DR   PhylomeDB; Q9LSJ8; -.
DR   BioCyc; ARA:AT3G28360-MON; -.
DR   PRO; PR:Q9LSJ8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSJ8; baseline and differential.
DR   Genevisible; Q9LSJ8; 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; -; 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..1228
FT                   /note="ABC transporter B family member 16"
FT                   /id="PRO_0000227929"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        145..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        171..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        667..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        700..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        781..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        805..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        881..901
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        920..940
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          22..311
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          346..582
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          658..946
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          981..1219
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         381..388
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1016..1023
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        593
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        628
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        755
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        827
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1001
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1228 AA;  135916 MW;  B1FE531C4DF920CB CRC64;
     MKTWGSMRSI FMHADGVDWM LMGLGLIGAV GDGFITPILF FITAMLLNDF GSFSFNDETF
     MQPISKNALA MLYVACASWV ICFLEGYCWT RTGERQAAKM RERYLRAVLR QDVGYFDLHV
     TSTSDIITSV SSDSLVIQDF LSEKLPNILM NASAFVGSYI VGFMLLWRLT IVGFPFIILL
     LIPGLMYGRA LIGISRKIRE EYNEAGSIAE QAISSVRTVY AFVSEKKMIE KFSDALQGSV
     KLGLRQGLAK GIAIGSNGIV YAIWGFLTWY GSRMVMNYGY KGGTVSTVTV CVTFGGTALG
     QALSNLKYFS EAFVAGERIQ KMIKRVPDID SDNLNGHILE TIRGEVEFNN VKCKYPSRPE
     TLIFDDLCLK IPSGKTVALV GGSGSGKSTV ISLLQRFYDP NEGDILIDSV SINNMQVKWL
     RSQMGMVSQE PSLFATSIKE NILFGKEDAS FDEVVEAAKA SNAHNFISQF PHGYQTQVGE
     RGVHMSGGQK QRIAIARALI KSPIILLLDE ATSALDLESE RVVQEALDNA SVGRTTIVIA
     HRLSTIRNAD IICVLHNGCI VETGSHDKLM EIDGKYTSLV RLQQMKNEES CDNTSVGVKE
     GRVSSLRNDL DYNPRDLAHS MSSSIVTNLS DSIPQDKKPL VPSFKRLMAM NRPEWKHALC
     GCLSASLGGA VQPIYAYSSG LMISVFFLTN HEQIKENTRI YVLLFFGLAL FTFFTSISQQ
     YSFSYMGEYL TKRIREQMLS KILTFEVNWF DEEENSSGAI CSRLAKDANV VRSLVGERMS
     LLVQTISTVM VACTIGLVIA WRFTIVMISV QPVIIVCYYI QRVLLKNMSK KAIIAQDESS
     KLAAEAVSNI RTITTFSSQE RIMKLLERVQ EGPRRESARQ SWLAGIMLGT TQSLITCTSA
     LNFWYGGKLI ADGKMVSKAF FELFLIFKTT GRAIAEAGTM TTDLAKGSNS VDSVFTVLDR
     RTTIEPENPD GYILEKIKGQ ITFLNVDFAY PTRPNMVIFN NFSIEIHEGK STAIVGPSRS
     GKSTVIGLIE RFYDPLQGIV KIDGRDIRSY HLRSLRQHMS LVSQEPTLFA GTIRENIMYG
     RASNKIDESE IIEAGKTANA HEFITSLSDG YDTYCGDRGV QLSGGQKQRI AIARTILKNP
     SILLLDEATS ALDSQSERVV QDALEHVMVG KTSVVIAHRL STIQNCDTIA VLDKGKVVES
     GTHASLLAKG PTGSYFSLVS LQRKVRYV
 
 
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