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SSR4_MOUSE
ID   SSR4_MOUSE              Reviewed;         385 AA.
AC   P49660; Q8BQ97;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   25-MAY-2022, entry version 149.
DE   RecName: Full=Somatostatin receptor type 4;
DE            Short=SS-4-R;
DE            Short=SS4-R;
DE            Short=SS4R;
GN   Name=Sstr4; Synonyms=Smstr4;
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].
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   PubMed=8654950; DOI=10.1016/0378-1119(95)00748-2;
RA   Schwabe W., Brennan M.B., Hochgeschwender U.;
RT   "Isolation and characterization of the mouse (Mus musculus) somatostatin
RT   receptor type-4-encoding gene (mSSTR4).";
RL   Gene 168:233-235(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CAST/EiJ; TISSUE=Brain;
RX   PubMed=16670015; DOI=10.1186/1471-2164-7-102;
RA   Farber C.R., Corva P.M., Medrano J.F.;
RT   "Genome-wide isolation of growth and obesity QTL using mouse speed congenic
RT   strains.";
RL   BMC Genomics 7:102-102(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 somatostatin-14. The activity of this receptor
CC       is mediated by G proteins which inhibits adenylyl cyclase. It is
CC       functionally coupled not only to inhibition of adenylate cyclase, but
CC       also to activation of both arachidonate release and mitogen-activated
CC       protein (MAP) kinase cascade.
CC   -!- INTERACTION:
CC       P49660; Q62108: Dlg4; NbExp=3; IntAct=EBI-7665342, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U26176; AAA67561.1; -; Genomic_DNA.
DR   EMBL; AY902332; AAX90617.1; -; Genomic_DNA.
DR   EMBL; AK051189; BAC34552.1; -; mRNA.
DR   EMBL; AL935149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC138487; AAI38488.1; -; mRNA.
DR   EMBL; BC138488; AAI38489.1; -; mRNA.
DR   CCDS; CCDS38260.1; -.
DR   PIR; JC4629; JC4629.
DR   RefSeq; NP_033245.2; NM_009219.3.
DR   AlphaFoldDB; P49660; -.
DR   SMR; P49660; -.
DR   IntAct; P49660; 2.
DR   MINT; P49660; -.
DR   STRING; 10090.ENSMUSP00000105588; -.
DR   BindingDB; P49660; -.
DR   ChEMBL; CHEMBL4397; -.
DR   DrugCentral; P49660; -.
DR   GuidetoPHARMACOLOGY; 358; -.
DR   GlyGen; P49660; 1 site.
DR   PhosphoSitePlus; P49660; -.
DR   SwissPalm; P49660; -.
DR   PaxDb; P49660; -.
DR   PRIDE; P49660; -.
DR   ABCD; P49660; 22 sequenced antibodies.
DR   DNASU; 20608; -.
DR   GeneID; 20608; -.
DR   KEGG; mmu:20608; -.
DR   UCSC; uc008mtc.1; mouse.
DR   CTD; 6754; -.
DR   MGI; MGI:105372; Sstr4.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P49660; -.
DR   OrthoDB; 1011272at2759; -.
DR   TreeFam; TF315737; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 20608; 0 hits in 72 CRISPR screens.
DR   PRO; PR:P49660; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P49660; protein.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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:0042923; F:neuropeptide binding; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0004994; F:somatostatin receptor activity; ISO:MGI.
DR   GO; GO:0016477; P:cell migration; ISO:MGI.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IBA:GO_Central.
DR   GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0090238; P:positive regulation of arachidonic acid secretion; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000586; Somatstn_rcpt.
DR   InterPro; IPR001512; Somatstn_rcpt_4.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00246; SOMATOSTATNR.
DR   PRINTS; PR00590; SOMATOSTTN4R.
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   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..385
FT                   /note="Somatostatin receptor type 4"
FT                   /id="PRO_0000070128"
FT   TOPO_DOM        1..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..70
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..106
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..139
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..229
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..281
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..312
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           324
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        8..9
FT                   /note="PP -> LR (in Ref. 1; AAA67561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27..29
FT                   /note="DEE -> EQ (in Ref. 1; AAA67561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="A -> V (in Ref. 1; AAA67561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="A -> R (in Ref. 1; AAA67561)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="A -> R (in Ref. 1; AAA67561)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   385 AA;  41932 MW;  64B3A272947A81BC CRC64;
     MNAPATLPPG VEDTTWTPGI NASWAPDEEE EDAMGSDGTG TAGMVTIQCI YALVCLVGLV
     GNALVIFVIL RYAKMKTATN IYLLNLAVAD ELFMLSVPFA RSAAALRHWP FGAVLCRAVL
     SVDGLNMFTS VFCLTVLSVD RYVAVVHPLA TATYRRPSVA KLINLGVWLA SLLVTLPIAV
     FADTRPARGG EAVACNLHWP HPAWSAVFVI YTFLLGFLPP VLAIGLCYLL IVGKMRAVAL
     AGGWQQRRRS EKKITRLVLM VVTVFVLCWM PFYVVQLLNL FVTSLDATVN HVSLILSYAN
     SCANPILYGF LSDNFRRSFQ RVLCLRCCLL ETTGGAEEEP LDYYATALKS RGGAGCICPP
     LPCQQEPVQA EPGCKQVPFT KTTTF
 
 
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