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S1PR3_MOUSE
ID   S1PR3_MOUSE             Reviewed;         378 AA.
AC   Q9Z0U9; Q8BP20;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Sphingosine 1-phosphate receptor 3;
DE            Short=S1P receptor 3;
DE            Short=S1P3;
DE   AltName: Full=Endothelial differentiation G-protein coupled receptor 3;
DE   AltName: Full=Lysophospholipid receptor B3;
DE   AltName: Full=Sphingosine 1-phosphate receptor Edg-3;
DE            Short=S1P receptor Edg-3;
GN   Name=S1pr3; Synonyms=Edg3, Lpb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=9931453; DOI=10.1016/s0378-1119(98)00589-7;
RA   Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J.;
RT   "Comparative analysis of three murine G-protein coupled receptors activated
RT   by sphingosine-1-phosphate.";
RL   Gene 227:89-99(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, Lung, Mesonephros, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ohta K., Wada A., Igarashi Y.;
RT   "Mus musculus sphingosine 1-phosphate receptor Edg3 gene, complete.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate
CC       (S1P). S1P is a bioactive lysophospholipid that elicits diverse
CC       physiological effect on most types of cells and tissues.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Most abundant in heart, lung, kidney and spleen;
CC       low but detectable in brain, thymus, muscle and testis; and nearly
CC       undetectable in liver, stomach, and intestine. Expressed in embryonic
CC       lung from embryonic day 14-18. Also abundantly detected in embryonic
CC       nasal cartilage, sphenoid bone, vena cava, Meckel's cartilage/incisor
CC       teeth, genital tubercle and bladder. {ECO:0000269|PubMed:9931453}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF108021; AAD16977.1; -; Genomic_DNA.
DR   EMBL; AK028043; BAC25715.1; -; mRNA.
DR   EMBL; AK029852; BAC26645.1; -; mRNA.
DR   EMBL; AK030134; BAC26800.1; -; mRNA.
DR   EMBL; AK047268; BAC33008.1; -; mRNA.
DR   EMBL; AK081919; BAC38373.1; -; mRNA.
DR   EMBL; AK084944; BAC39316.1; -; mRNA.
DR   EMBL; AK085180; BAC39383.1; -; mRNA.
DR   EMBL; AK078443; BAC37277.1; -; mRNA.
DR   EMBL; AB028143; BAA78207.1; -; mRNA.
DR   EMBL; BC064007; AAH64007.1; -; mRNA.
DR   EMBL; BC068176; AAH68176.1; -; mRNA.
DR   CCDS; CCDS26512.1; -.
DR   RefSeq; NP_034231.1; NM_010101.4.
DR   AlphaFoldDB; Q9Z0U9; -.
DR   SMR; Q9Z0U9; -.
DR   STRING; 10090.ENSMUSP00000085293; -.
DR   GuidetoPHARMACOLOGY; 277; -.
DR   GlyGen; Q9Z0U9; 1 site.
DR   iPTMnet; Q9Z0U9; -.
DR   PhosphoSitePlus; Q9Z0U9; -.
DR   MaxQB; Q9Z0U9; -.
DR   PaxDb; Q9Z0U9; -.
DR   PRIDE; Q9Z0U9; -.
DR   ProteomicsDB; 256861; -.
DR   Antibodypedia; 13485; 548 antibodies from 37 providers.
DR   DNASU; 13610; -.
DR   Ensembl; ENSMUST00000087978; ENSMUSP00000085293; ENSMUSG00000067586.
DR   GeneID; 13610; -.
DR   KEGG; mmu:13610; -.
DR   UCSC; uc007qmf.2; mouse.
DR   CTD; 1903; -.
DR   MGI; MGI:1339365; S1pr3.
DR   VEuPathDB; HostDB:ENSMUSG00000067586; -.
DR   eggNOG; ENOG502R61K; Eukaryota.
DR   GeneTree; ENSGT01050000244887; -.
DR   HOGENOM; CLU_047979_1_0_1; -.
DR   InParanoid; Q9Z0U9; -.
DR   OMA; DVACRVK; -.
DR   OrthoDB; 981486at2759; -.
DR   PhylomeDB; Q9Z0U9; -.
DR   TreeFam; TF330052; -.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR   Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR   BioGRID-ORCS; 13610; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; S1pr3; mouse.
DR   PRO; PR:Q9Z0U9; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q9Z0U9; protein.
DR   Bgee; ENSMUSG00000067586; Expressed in internal carotid artery and 234 other tissues.
DR   Genevisible; Q9Z0U9; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IEA:InterPro.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:1903141; P:negative regulation of establishment of endothelial barrier; ISO:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR   GO; GO:0032651; P:regulation of interleukin-1 beta production; IMP:MGI.
DR   GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR   InterPro; IPR004062; EDG3_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR004061; S1P_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01524; EDG3RECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01523; S1PRECEPTOR.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..378
FT                   /note="Sphingosine 1-phosphate receptor 3"
FT                   /id="PRO_0000069422"
FT   TOPO_DOM        1..44
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        66..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        75..95
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        96..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        116..136
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        137..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        155..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        176..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        197..217
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        218..244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        245..265
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        266..281
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        282..302
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        303..378
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          323..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99500"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        106
FT                   /note="S -> R (in Ref. 2; BAC37277)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  42270 MW;  F466B25E77ECDCC8 CRC64;
     MATTHAQGHQ PVLGNDTLRE HYDYVGKLAG RLRDPPEGGT LITTILFLVT CSFIVLENLM
     VLIAIWKNNK FHNRMYFFIG NLALCDLLAG IAYKVNILMS GRKTFSLSPT VWFLREGSMF
     VALGASTCSL LAIAIERHLT MIKMRPYDAN KKHRVFLLIG MCWLIAFSLG ALPILGWNCL
     ENFPDCSTIL PLYSKKYIAF LISIFTAILV TIVILYARIY CLVKSSSRRV ANHNSERSMA
     LLRTVVIVVS VFIACWSPLF ILFLIDVACR AKECSILFKS QWFIMLAVLN SAMNPVIYTL
     ASKEMRRAFF RLVCGCLVKG KGTQASPMQP ALDPSRSKSS SSNNSSHSPK VKEDLPRVAT
     SSCIIDKNRS FQNGVLCK
 
 
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