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SO1A1_RAT
ID   SO1A1_RAT               Reviewed;         670 AA.
AC   P46720;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Solute carrier organic anion transporter family member 1A1;
DE   AltName: Full=Organic anion-transporting polypeptide 1;
DE            Short=OATP-1;
DE   AltName: Full=Sodium-independent organic anion transporter 1;
DE   AltName: Full=Solute carrier family 21 member 1;
GN   Name=Slco1a1; Synonyms=Oatp1, Oatp1a1, Slc21a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND GLYCOSYLATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8278353; DOI=10.1073/pnas.91.1.133;
RA   Jacquemin E., Hagenbuch B., Stieger B., Wolkoff A.W., Meier P.J.;
RT   "Expression cloning of a rat liver Na(+)-independent organic anion
RT   transporter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:133-137(1994).
RN   [2]
RP   INTERACTION WITH PDZK1, AND MUTAGENESIS OF 666-LYS--LEU-670.
RX   PubMed=15994332; DOI=10.1074/jbc.m503969200;
RA   Wang P., Wang J.J., Xiao Y., Murray J.W., Novikoff P.M., Angeletti R.H.,
RA   Orr G.A., Lan D., Silver D.L., Wolkoff A.W.;
RT   "Interaction with PDZK1 is required for expression of organic anion
RT   transporting protein 1A1 on the hepatocyte surface.";
RL   J. Biol. Chem. 280:30143-30149(2005).
RN   [3]
RP   PHOSPHORYLATION AT SER-634 AND SER-635.
RX   PubMed=16519530; DOI=10.1021/bi052437v;
RA   Xiao Y., Nieves E., Angeletti R.H., Orr G.A., Wolkoff A.W.;
RT   "Rat organic anion transporting protein 1A1 (Oatp1a1): purification and
RT   phosphopeptide assignment.";
RL   Biochemistry 45:3357-3369(2006).
RN   [4]
RP   SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-124;
RP   ASN-135 AND ASN-492.
RX   PubMed=18308854; DOI=10.1152/ajpgi.00584.2007;
RA   Wang P., Hata S., Xiao Y., Murray J.W., Wolkoff A.W.;
RT   "Topological assessment of oatp1a1: a 12-transmembrane domain integral
RT   membrane protein with three N-linked carbohydrate chains.";
RL   Am. J. Physiol. 294:G1052-G1059(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Mediates the Na(+)-independent transport of organic anions
CC       such as bromosulfobromophthalein (BSP) and conjugated (taurocholate)
CC       and unconjugated (cholate) bile acids.
CC   -!- SUBUNIT: Binds to PDZK1. Interaction with PDZK1 is required for
CC       expression on hepatocyte surface.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000269|PubMed:18308854}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:18308854}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney, and at lower
CC       levels in brain, lung, skeletal muscle and proximal colon.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:18308854,
CC       ECO:0000269|PubMed:8278353}.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000305}.
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DR   EMBL; L19031; AAA16451.1; -; mRNA.
DR   PIR; A49580; A49580.
DR   RefSeq; NP_058807.1; NM_017111.1.
DR   AlphaFoldDB; P46720; -.
DR   SMR; P46720; -.
DR   STRING; 10116.ENSRNOP00000040752; -.
DR   BindingDB; P46720; -.
DR   ChEMBL; CHEMBL1781859; -.
DR   TCDB; 2.A.60.1.1; the organo anion transporter (oat) family.
DR   GlyGen; P46720; 3 sites.
DR   iPTMnet; P46720; -.
DR   PhosphoSitePlus; P46720; -.
DR   PaxDb; P46720; -.
DR   PRIDE; P46720; -.
DR   Ensembl; ENSRNOT00000102966; ENSRNOP00000078030; ENSRNOG00000036984.
DR   GeneID; 50572; -.
DR   KEGG; rno:50572; -.
DR   CTD; 28248; -.
DR   RGD; 3700; Slco1a1.
DR   eggNOG; KOG3626; Eukaryota.
DR   GeneTree; ENSGT01050000244856; -.
DR   HOGENOM; CLU_008954_4_0_1; -.
DR   InParanoid; P46720; -.
DR   OMA; PETASEW; -.
DR   OrthoDB; 1029129at2759; -.
DR   PhylomeDB; P46720; -.
DR   SABIO-RK; P46720; -.
DR   PRO; PR:P46720; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000036984; Expressed in adult mammalian kidney and 2 other tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0015125; F:bile acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; TAS:RGD.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015721; P:bile acid and bile salt transport; IBA:GO_Central.
DR   GO; GO:0015711; P:organic anion transport; IEP:RGD.
DR   GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl.
DR   GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   PANTHER; PTHR11388; PTHR11388; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00805; oat; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..670
FT                   /note="Solute carrier organic anion transporter family
FT                   member 1A1"
FT                   /id="PRO_0000191041"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..40
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..59
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..111
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..155
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..184
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..203
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..267
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        268..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..333
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..353
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..377
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        378..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..405
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..513
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..536
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        537..545
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        546..571
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        572..605
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        606..623
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        624..670
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          433..488
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          645..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16519530"
FT   MOD_RES         635
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16519530"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18308854"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18308854"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18308854"
FT   DISULFID        439..469
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        445..465
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        454..486
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   MUTAGEN         666..670
FT                   /note="Missing: Abolishes binding to PDZK1."
FT                   /evidence="ECO:0000269|PubMed:15994332"
SQ   SEQUENCE   670 AA;  74178 MW;  3D53A4E8E1E21536 CRC64;
     MEETEKKIAT QEGRLFSKMK VFLLSLTCAC LTKSLSGVYM NSMLTQIERQ FDISTSVAGL
     INGSFEIGNL FFIVFVSYFG TKLHRPVVIG IGCVIMGLGC LLMSLPHFFM GRYEYETTIS
     PTGNLSSNSF LCMENRTQTL KPTQDPAECV KEMKSLMWIC VMVGNIIRGI GETPIVPLGI
     SYIEDFAKSE NSPLYIGILE MGKVAGPIFG LLLGSYCAQI YVDIGSVNTD DLTITPSDTR
     WVGAWWIGFL VCAGVNILTS IPFFFLPKAL PKKGQQENVA VTKDGKVEKY GGQAREENLG
     ITKDFLTFMK RLFCNPIYML FILTSVLQVN GFINKFTFLP KYLEQQYGKS TAEAIFLIGV
     YSLPPICLGY LIGGFIMKKF KITVKKAAYL AFCLSVFEYL LFLCHFMLTC DNAAVAGLTT
     SYKGVQHQLH VESKVLADCN TRCSCSTNTW DPVCGDNGVA YMSACLAGCK KFVGTGTNMV
     FQDCSCIQSL GNSSAVLGLC KKGPECANRL QYFLILTIII SFIYSLTAIP GYMVFLRCVK
     SEEKSLGVGL HTFCIRVFAG IPAPVYFGAL IDRTCLHWGT LKCGQRGACR MYDINSFRHI
     YLGLPIALRG SSYLPAFFIL ILMRKFQFPG DIDSSATDHT EMMLGEKESE HTDVHGSPQV
     ENDGELKTKL
 
 
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