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S226B_XENLA
ID   S226B_XENLA             Reviewed;         552 AA.
AC   Q66J52;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Solute carrier family 22 member 6-B;
DE   AltName: Full=Organic cation transporter 1-B;
DE   AltName: Full=Renal organic anion transporter 1-B;
DE            Short=ROAT1-B;
GN   Name=slc22a6-b; Synonyms=oat1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the renal elimination of endogenous and exogenous
CC       organic anions. Mediates the sodium-independent uptake of p-
CC       aminohippurate (PAH), cidofovir, adefovir, 9-(2-phosphonylmethoxyethyl)
CC       guanine (PMEG), 9-(2-phosphonylmethoxyethyl) diaminopurine (PMEDAP) and
CC       edaravone sulfate. PAH uptake is inhibited by furosemide, steviol,
CC       phorbol 12-myristate 13-acetate (PMA), calcium ionophore A23187,
CC       benzylpenicillin, furosemide, indomethacin, bumetamide, losartan,
CC       probenecid, phenol red, urate, and alpha-ketoglutarate (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- PTM: Glycosylated. Glycosylation is necessary for proper targeting of
CC       the transporter to the plasma membrane (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR   EMBL; BC081057; AAH81057.1; -; mRNA.
DR   RefSeq; NP_001087663.1; NM_001094194.1.
DR   AlphaFoldDB; Q66J52; -.
DR   SMR; Q66J52; -.
DR   MaxQB; Q66J52; -.
DR   DNASU; 447487; -.
DR   GeneID; 447487; -.
DR   KEGG; xla:447487; -.
DR   CTD; 447487; -.
DR   Xenbase; XB-GENE-5842265; slc22a6.S.
DR   OrthoDB; 704438at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 447487; Expressed in kidney.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004749; Orgcat_transp/SVOP.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00898; 2A0119; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..552
FT                   /note="Solute carrier family 22 member 6-B"
FT                   /id="PRO_0000324176"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..137
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..336
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        379..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..426
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        448..459
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        481..487
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..552
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   552 AA;  61665 MW;  CC5FCB5A11A97454 CRC64;
     MAFQEILESL GGMGRYQVIH VVLLSLPVFM LASHNLMQNF TAATPSHHCR INGTYEETNF
     TGPWLRALLP MTPTGEFSKC LRYTTPQYEL LENNLTQSYD DLETEPCLDG WVYDHSEFAS
     TIITQWDLVC NHRRMRQVAQ SIYMAGVLVG SILFGGLSDK FGRRPLNIWS NLQMFVTGIC
     AAFSPNYIWY CIFRFLTGVA FSGIVLNSYS LTVEWIPTGN RAFTSTATGY CYTMGQLVLV
     GLAFIIRDWQ WLQLAASIPF FFYFLYSWWI PESGRWLVLS GKPEVACKAL KKVAQINGKK
     EAGEKLTVEI LKSSMQREIN ASHNSTYSAL DLVRTPVVRR ISFCISCTWF STSFAYYGLA
     LDLQSFGVSI YIIQIIFGTV DIPAKFISYF ITTYVGRRVS QAITLILAGI AILVNISVPQ
     DFQTVRTAMA VFGKGCLAAS FNCLYLYTGE LYPTVIRQTG MGLGAMMARL GGIIAPLAQM
     TGDIYHSLPL IIFGCLPILS GIAGCFLPET LGVPLPETIE EVESPDKQQK DVNVSAKIPL
     KETELYNMKT DV
 
 
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