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P52592

- S1PR2_MOUSE

UniProt

P52592 - S1PR2_MOUSE

Protein

Sphingosine 1-phosphate receptor 2

Gene

S1pr2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues.

    GO - Molecular functioni

    1. sphingosine-1-phosphate receptor activity Source: InterPro

    GO - Biological processi

    1. negative regulation of excitatory postsynaptic membrane potential Source: MGI

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sphingosine 1-phosphate receptor 2
    Short name:
    S1P receptor 2
    Short name:
    S1P2
    Alternative name(s):
    Endothelial differentiation G-protein coupled receptor 5
    Lysophospholipid receptor B2
    Sphingosine 1-phosphate receptor Edg-5
    Short name:
    S1P receptor Edg-5
    Gene namesi
    Name:S1pr2
    Synonyms:Edg5, Gpcr13, Lpb2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:99569. S1pr2.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Sphingosine 1-phosphate receptor 2PRO_0000069428Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi19 – 191N-linked (GlcNAc...)2 Publications
    Lipidationi305 – 3051S-palmitoyl cysteineBy similarity

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiP52592.
    PRIDEiP52592.

    PTM databases

    PhosphoSiteiP52592.

    Expressioni

    Tissue specificityi

    Most abundant in heart and lung; low, but clearly observed in kidney, liver and thymus; much lower but detectable in brain, testis, stomach and intestine. Not significantly detected in any of the sections of embryonic day (E) 14-18, except in embryonic brain.1 Publication

    Gene expression databases

    BgeeiP52592.
    GenevestigatoriP52592.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-60681N.
    STRINGi10090.ENSMUSP00000053394.

    Structurei

    3D structure databases

    ProteinModelPortaliP52592.
    SMRiP52592. Positions 6-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3434ExtracellularBy similarityAdd
    BLAST
    Topological domaini60 – 667CytoplasmicBy similarity
    Topological domaini96 – 10914ExtracellularBy similarityAdd
    BLAST
    Topological domaini129 – 14719CytoplasmicBy similarityAdd
    BLAST
    Topological domaini174 – 18916ExtracellularBy similarityAdd
    BLAST
    Topological domaini211 – 23323CytoplasmicBy similarityAdd
    BLAST
    Topological domaini256 – 27116ExtracellularBy similarityAdd
    BLAST
    Topological domaini293 – 35260CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei35 – 5925Helical; Name=1By similarityAdd
    BLAST
    Transmembranei67 – 9529Helical; Name=2By similarityAdd
    BLAST
    Transmembranei110 – 12819Helical; Name=3By similarityAdd
    BLAST
    Transmembranei148 – 17326Helical; Name=4By similarityAdd
    BLAST
    Transmembranei190 – 21021Helical; Name=5By similarityAdd
    BLAST
    Transmembranei234 – 25522Helical; Name=6By similarityAdd
    BLAST
    Transmembranei272 – 29221Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG149362.
    GeneTreeiENSGT00750000117544.
    HOGENOMiHOG000233501.
    HOVERGENiHBG103071.
    InParanoidiQ8C3Q7.
    KOiK04292.
    OMAiKFHSAMY.
    OrthoDBiEOG708W0B.
    TreeFamiTF330052.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR004063. EDG5_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR004061. S1P_rcpt.
    [Graphical view]
    PANTHERiPTHR22750:SF17. PTHR22750:SF17. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR01525. EDG5RECEPTOR.
    PR00237. GPCRRHODOPSN.
    PR01523. S1PRECEPTOR.
    PROSITEiPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P52592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGGLYSEYLN PEKVLEHYNY TKETLDMQET TSRKVASAFI IILCCAIVVE    50
    NLLVLIAVAR NSKFHSAMYL FLGNLAASDL LAGVAFVANT LLSGHVTLSL 100
    TPVQWFAREG SAFITLSASV FSLLAIAIER QVALAKVKLY GSDKSCRMLM 150
    LIGASWLISL ILGGLPILGW NCLNQLEACS TVLPLYAKHY VLCVVTIFSV 200
    ILLAIVALYV RIYFVVRSSH ADVAGPQTLA LLKTVTIVLG VFIICWLPAF 250
    SILLLDSTCP VRACPVLYKA HYFFAFATLN SLLNPVIYTW RSRDLRREVL 300
    RPLQCWRRGK GVTGRRGGNP GHRLLPLRSS SSLERGMHMP TSPTFLEGNT 350
    VV 352
    Length:352
    Mass (Da):38,829
    Last modified:July 27, 2011 - v3
    Checksum:i6A3E426B0FE54406
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101G → V in AAD16976. (PubMed:9931453)Curated
    Sequence conflicti110 – 1101G → V in AAA16846. (PubMed:8288218)Curated
    Sequence conflicti166 – 1661P → S in AAA16846. (PubMed:8288218)Curated
    Sequence conflicti175 – 1751Q → K in AAA16846. (PubMed:8288218)Curated
    Sequence conflicti189 – 1891H → R in AAA16846. (PubMed:8288218)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF108020 Genomic DNA. Translation: AAD16976.1.
    AK085114 mRNA. Translation: BAC39368.1.
    AK134275 mRNA. Translation: BAE22078.1.
    AK151062 mRNA. Translation: BAE30079.1.
    AK159605 mRNA. Translation: BAE35224.1.
    AK170436 mRNA. Translation: BAE41795.1.
    CH466522 Genomic DNA. Translation: EDL25146.1.
    BC096760 mRNA. Translation: AAH96760.1.
    L20334 mRNA. Translation: AAA16846.1.
    CCDSiCCDS22888.1.
    PIRiE48909.
    RefSeqiNP_034463.2. NM_010333.4.
    XP_006510082.1. XM_006510019.1.
    UniGeneiMm.46493.

    Genome annotation databases

    EnsembliENSMUST00000054197; ENSMUSP00000053394; ENSMUSG00000043895.
    GeneIDi14739.
    KEGGimmu:14739.
    UCSCiuc009ojt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF108020 Genomic DNA. Translation: AAD16976.1 .
    AK085114 mRNA. Translation: BAC39368.1 .
    AK134275 mRNA. Translation: BAE22078.1 .
    AK151062 mRNA. Translation: BAE30079.1 .
    AK159605 mRNA. Translation: BAE35224.1 .
    AK170436 mRNA. Translation: BAE41795.1 .
    CH466522 Genomic DNA. Translation: EDL25146.1 .
    BC096760 mRNA. Translation: AAH96760.1 .
    L20334 mRNA. Translation: AAA16846.1 .
    CCDSi CCDS22888.1.
    PIRi E48909.
    RefSeqi NP_034463.2. NM_010333.4.
    XP_006510082.1. XM_006510019.1.
    UniGenei Mm.46493.

    3D structure databases

    ProteinModelPortali P52592.
    SMRi P52592. Positions 6-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60681N.
    STRINGi 10090.ENSMUSP00000053394.

    Chemistry

    GuidetoPHARMACOLOGYi 276.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P52592.

    Proteomic databases

    PaxDbi P52592.
    PRIDEi P52592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000054197 ; ENSMUSP00000053394 ; ENSMUSG00000043895 .
    GeneIDi 14739.
    KEGGi mmu:14739.
    UCSCi uc009ojt.2. mouse.

    Organism-specific databases

    CTDi 9294.
    MGIi MGI:99569. S1pr2.

    Phylogenomic databases

    eggNOGi NOG149362.
    GeneTreei ENSGT00750000117544.
    HOGENOMi HOG000233501.
    HOVERGENi HBG103071.
    InParanoidi Q8C3Q7.
    KOi K04292.
    OMAi KFHSAMY.
    OrthoDBi EOG708W0B.
    TreeFami TF330052.

    Miscellaneous databases

    ChiTaRSi S1PR2. mouse.
    NextBioi 286795.
    PROi P52592.
    SOURCEi Search...

    Gene expression databases

    Bgeei P52592.
    Genevestigatori P52592.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR004063. EDG5_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR004061. S1P_rcpt.
    [Graphical view ]
    PANTHERi PTHR22750:SF17. PTHR22750:SF17. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01525. EDG5RECEPTOR.
    PR00237. GPCRRHODOPSN.
    PR01523. S1PRECEPTOR.
    PROSITEi PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "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.
      , 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 and NOD.
      Tissue: Bone marrow, Forelimb and Lung.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Identification, chromosomal location, and genome organization of mammalian G-protein-coupled receptors."
      Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., Copeland N.G., Jenkins N.A.
      Genomics 18:175-184(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-241.
      Tissue: Testis.
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.
      Tissue: Myoblast.
    8. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.

    Entry informationi

    Entry nameiS1PR2_MOUSE
    AccessioniPrimary (citable) accession number: P52592
    Secondary accession number(s): Q8C3Q7, Q9R236
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3