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O08530 (S1PR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sphingosine 1-phosphate receptor 1

Short name=S1P receptor 1
Short name=S1P1
Alternative name(s):
Endothelial differentiation G-protein coupled receptor 1
Lysophospholipid receptor B1
Sphingosine 1-phosphate receptor Edg-1
Short name=S1P receptor Edg-1
CD_antigen=CD363
Gene names
Name:S1pr1
Synonyms:Edg1, Lpb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

Subunit structure

Interacts with GNAI1 and GNAI3 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Endosome By similarity. Membranecaveola By similarity. Note: Recruited to caveolin-enriched plasma membrane microdomains in response to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine. Ligand binding leads to receptor internalization By similarity.

Tissue specificity

Expressed in a wide variety of tissues with highest levels in brain, heart and spleen. Lower levels found in kidney, liver, lung, muscle, placenta, thymus, and uterus. Very low levels in intestine, stomach and testis. According to Ref.2, expressed modestly in apparent endothelial cells surrounding some blood vessels (e.g. aortic trunk). Ref.2 Ref.6

Disruption phenotype

Embryonic lethality, due to impaired vascular maturation and defects in heart development. Embryos appear normal up to 11.5 dpc, but after that they display massive hemorrhage. They have a normally arborized vascular network, but present excessive sprouting angiogenesis and severe aberrations in vessel size. Their aorta and other arteries are not properly enveloped by vascular smooth muscle cells, causing hemorrhage. Likewise, small blood vessels show a marked reduction in the number of vascular pericytes. In addition, mutants display defects in heart morphogenesis, with reduced myocardial tissue and altered morphology of the heart wall and the trabeculae. Conditional knockout in endothelial cells leads to the same vascular maturation defect as that seen in homozygous knockout mice. Conditional knockout in fibroblasts leads to defects in chemotaxis, probably due to defects in the activation of SRC and PTK2/FAK1, resulting in defects in the reorganization of the actin cytoskeleton and lamellipodia formation. A T-cell-specific knockout leads to a defect in the egress of mature T-cells from the thymus into the periphery. Conditional knockout in osteoclast precursors leads to osteoporosis, due to impaired migration of osteoclast precursors and increased osteoclast attachment to the bone. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processAngiogenesis
Chemotaxis
   Cellular componentCell membrane
Endosome
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMAcetylation
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell migration

Inferred from mutant phenotype Ref.10. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 11443127. Source: MGI

angiogenesis

Inferred from direct assay PubMed 15371328. Source: MGI

blood vessel maturation

Inferred from mutant phenotype Ref.6. Source: UniProtKB

brain development

Inferred from mutant phenotype PubMed 16314531. Source: MGI

cardiac muscle tissue growth involved in heart morphogenesis

Inferred from mutant phenotype Ref.15. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.14. Source: UniProtKB

chemotaxis

Inferred from mutant phenotype Ref.6Ref.7. Source: UniProtKB

endothelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

heart trabecula morphogenesis

Inferred from mutant phenotype Ref.15. Source: UniProtKB

lamellipodium assembly

Inferred from mutant phenotype Ref.7. Source: UniProtKB

negative regulation of stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of Ras GTPase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 16314531. Source: MGI

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of positive chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of bone mineralization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of bone resorption

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of cell adhesion

Inferred from direct assay PubMed 15371328. Source: MGI

sphingosine-1-phosphate signaling pathway

Inferred from mutant phenotype Ref.6. Source: UniProtKB

transmission of nerve impulse

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

external side of plasma membrane

Inferred from mutant phenotype PubMed 18836449. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionsphingolipid binding

Inferred from electronic annotation. Source: Ensembl

sphingosine-1-phosphate receptor activity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 382381Sphingosine 1-phosphate receptor 1
PRO_0000069413

Regions

Topological domain2 – 4645Extracellular By similarity
Transmembrane47 – 6822Helical; Name=1; By similarity
Topological domain69 – 8214Cytoplasmic By similarity
Transmembrane83 – 10422Helical; Name=2; By similarity
Topological domain105 – 11612Extracellular By similarity
Transmembrane117 – 13822Helical; Name=3; By similarity
Topological domain139 – 16022Cytoplasmic By similarity
Transmembrane161 – 18222Helical; Name=4; By similarity
Topological domain183 – 19614Extracellular By similarity
Transmembrane197 – 22428Helical; Name=5; By similarity
Topological domain225 – 25733Cytoplasmic By similarity
Transmembrane258 – 27821Helical; Name=6; By similarity
Topological domain279 – 28911Extracellular By similarity
Transmembrane290 – 31021Helical; Name=7; By similarity
Topological domain311 – 38272Cytoplasmic By similarity
Region120 – 1212Sphingosine 1-phosphate binding By similarity
Region265 – 2695Sphingosine 1-phosphate binding By similarity

Amino acid modifications

Modified residue21N-acetylvaline Ref.17
Modified residue101N6-acetyllysine Ref.17
Modified residue2361Phosphothreonine By similarity
Modified residue3531Phosphoserine Potential
Lipidation3281S-palmitoyl cysteine By similarity
Glycosylation301N-linked (GlcNAc...) Potential
Disulfide bond184 ↔ 191 By similarity
Disulfide bond282 ↔ 287 By similarity

Experimental info

Sequence conflict1791I → S in AAC53294. Ref.1
Sequence conflict1791I → S in AAD16975. Ref.2
Sequence conflict2181V → A in AAC53294. Ref.1
Sequence conflict2441A → G in AAC53294. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08530 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 5FE4C9A2BD65CB2A

FASTA38242,639
        10         20         30         40         50         60 
MVSTSIPEVK ALRSSVSDYG NYDIIVRHYN YTGKLNIGAE KDHGIKLTSV VFILICCFII 

        70         80         90        100        110        120 
LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA NLLLSGATTY KLTPAQWFLR 

       130        140        150        160        170        180 
EGSMFVALSA SVFSLLAIAI ERYITMLKMK LHNGSNSSRS FLLISACWVI SLILGGLPIM 

       190        200        210        220        230        240 
GWNCISSLSS CSTVLPLYHK HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN 

       250        260        270        280        290        300 
ISKASRSSEK SLALLKTVII VLSVFIACWA PLFILLLLDV GCKAKTCDIL YKAEYFLVLA 

       310        320        330        340        350        360 
VLNSGTNPII YTLTNKEMRR AFIRIVSCCK CPNGDSAGKF KRPIIPGMEF SRSKSDNSSH 

       370        380 
PQKDDGDNPE TIMSSGNVNS SS 

« Hide

References

« Hide 'large scale' references
[1]"The mouse gene for the inducible G-protein-coupled receptor edg-1."
Liu C.H., Hla T.
Genomics 43:15-24(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Liver.
[2]"Comparative analysis of three murine G-protein coupled receptors activated by sphingosine-1-phosphate."
Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J.
Gene 227:89-99(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: 129/SvJ.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart and Lung.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Eye.
[6]"Edg-1, the G protein-coupled receptor for sphingosine-1-phosphate, is essential for vascular maturation."
Liu Y., Wada R., Yamashita T., Mi Y., Deng C.X., Hobson J.P., Rosenfeldt H.M., Nava V.E., Chae S.S., Lee M.J., Liu C.H., Hla T., Spiegel S., Proia R.L.
J. Clin. Invest. 106:951-961(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN VASCULAR MATURATION AND CHEMOTAXIS, TISSUE SPECIFICITY.
[7]"EDG-1 links the PDGF receptor to Src and focal adhesion kinase activation leading to lamellipodia formation and cell migration."
Rosenfeldt H.M., Hobson J.P., Maceyka M., Olivera A., Nava V.E., Milstien S., Spiegel S.
FASEB J. 15:2649-2659(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FIBROBLAST CHEMOTAXIS, DISRUPTION PHENOTYPE.
[8]"Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced cell motility."
Hobson J.P., Rosenfeldt H.M., Barak L.S., Olivera A., Poulton S., Caron M.G., Milstien S., Spiegel S.
Science 291:1800-1803(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"G-protein-coupled receptor S1P1 acts within endothelial cells to regulate vascular maturation."
Allende M.L., Yamashita T., Proia R.L.
Blood 102:3665-3667(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN VASCULAR MATURATION.
[10]"Expression of the sphingosine 1-phosphate receptor, S1P1, on T-cells controls thymic emigration."
Allende M.L., Dreier J.L., Mandala S., Proia R.L.
J. Biol. Chem. 279:15396-15401(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN T CELL MIGRATION.
[11]"Lymphocyte egress from thymus and peripheral lymphoid organs is dependent on S1P receptor 1."
Matloubian M., Lo C.G., Cinamon G., Lesneski M.J., Xu Y., Brinkmann V., Allende M.L., Proia R.L., Cyster J.G.
Nature 427:355-360(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN T CELL MIGRATION.
[12]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"Akt-mediated transactivation of the S1P1 receptor in caveolin-enriched microdomains regulates endothelial barrier enhancement by oxidized phospholipids."
Singleton P.A., Chatchavalvanich S., Fu P., Xing J., Birukova A.A., Fortune J.A., Klibanov A.M., Garcia J.G., Birukov K.G.
Circ. Res. 104:978-986(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Sphingosine-1-phosphate mobilizes osteoclast precursors and regulates bone homeostasis."
Ishii M., Egen J.G., Klauschen F., Meier-Schellersheim M., Saeki Y., Vacher J., Proia R.L., Germain R.N.
Nature 458:524-528(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN OSTEOCLAST MIGRATION AND BONE HOMEOSTASIS.
[15]"The Sphingosine-1-phospate receptor 1 mediates S1P action during cardiac development."
Poulsen R.R., McClaskey C.M., Rivkees S.A., Wendler C.C.
BMC Dev. Biol. 11:37-37(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN HEART MORPHOGENESIS AND DEVELOPMENT.
[16]"S1P1 inhibits sprouting angiogenesis during vascular development."
Ben Shoham A., Malkinson G., Krief S., Shwartz Y., Ely Y., Ferrara N., Yaniv K., Zelzer E.
Development 139:3859-3869(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN SPROUTING ANGIOGENESIS.
[17]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2 AND LYS-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40811 Genomic DNA. Translation: AAC53294.1.
AF108019 Genomic DNA. Translation: AAD16975.1.
AK004591 mRNA. Translation: BAB23393.1.
AK146501 mRNA. Translation: BAE27216.1.
CH466532 Genomic DNA. Translation: EDL12402.1.
BC049094 mRNA. Translation: AAH49094.1.
BC051023 mRNA. Translation: AAH51023.1.
CCDSCCDS17781.1.
RefSeqNP_031927.2. NM_007901.5.
UniGeneMm.982.

3D structure databases

ProteinModelPortalO08530.
SMRO08530. Positions 16-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199373. 2 interactions.
DIPDIP-32248N.
IntActO08530. 1 interaction.

Chemistry

BindingDBO08530.
ChEMBLCHEMBL1914262.
GuidetoPHARMACOLOGY275.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO08530.

Proteomic databases

PaxDbO08530.
PRIDEO08530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055676; ENSMUSP00000050897; ENSMUSG00000045092.
GeneID13609.
KEGGmmu:13609.
UCSCuc008rbo.2. mouse.

Organism-specific databases

CTD1901.
MGIMGI:1096355. S1pr1.

Phylogenomic databases

eggNOGNOG148018.
GeneTreeENSGT00750000117544.
HOGENOMHOG000233501.
HOVERGENHBG103071.
InParanoidQ9DC35.
KOK04288.
OMASAFIACW.
OrthoDBEOG708W0B.
TreeFamTF330052.

Gene expression databases

ArrayExpressO08530.
BgeeO08530.
GenevestigatorO08530.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000987. EDG1_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR004061. S1P_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00642. EDG1RECEPTOR.
PR00237. GPCRRHODOPSN.
PR01523. S1PRECEPTOR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284254.
PROO08530.
SOURCESearch...

Entry information

Entry nameS1PR1_MOUSE
AccessionPrimary (citable) accession number: O08530
Secondary accession number(s): Q9DC35, Q9R235
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries