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RL3R1_MOUSE
ID   RL3R1_MOUSE             Reviewed;         472 AA.
AC   Q8BGE9;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Relaxin-3 receptor 1;
DE            Short=RLN3 receptor 1;
DE   AltName: Full=G protein-coupled receptor SALPR homolog;
DE   AltName: Full=Relaxin family peptide receptor 3;
GN   Name=Rxfp3; Synonyms=Rln3r1, Salpr;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, and 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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 RNL3/relaxin-3. Binding of the ligand inhibit
CC       cAMP accumulation (By similarity). {ECO:0000250}.
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; AK043414; BAC31542.1; -; mRNA.
DR   EMBL; AK046367; BAC32691.1; -; mRNA.
DR   EMBL; AK084001; BAC39091.1; -; mRNA.
DR   EMBL; BC053073; AAH53073.1; -; mRNA.
DR   CCDS; CCDS27383.1; -.
DR   RefSeq; NP_848832.1; NM_178717.3.
DR   AlphaFoldDB; Q8BGE9; -.
DR   SMR; Q8BGE9; -.
DR   STRING; 10090.ENSMUSP00000062741; -.
DR   GlyGen; Q8BGE9; 2 sites.
DR   iPTMnet; Q8BGE9; -.
DR   PhosphoSitePlus; Q8BGE9; -.
DR   PaxDb; Q8BGE9; -.
DR   PRIDE; Q8BGE9; -.
DR   DNASU; 239336; -.
DR   Ensembl; ENSMUST00000058007; ENSMUSP00000062741; ENSMUSG00000060735.
DR   GeneID; 239336; -.
DR   KEGG; mmu:239336; -.
DR   UCSC; uc007vgy.1; mouse.
DR   CTD; 51289; -.
DR   MGI; MGI:2441827; Rxfp3.
DR   VEuPathDB; HostDB:ENSMUSG00000060735; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234534; -.
DR   HOGENOM; CLU_009579_8_1_1; -.
DR   InParanoid; Q8BGE9; -.
DR   OMA; IVTSMNM; -.
DR   OrthoDB; 880755at2759; -.
DR   PhylomeDB; Q8BGE9; -.
DR   TreeFam; TF330024; -.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-444821; Relaxin receptors.
DR   BioGRID-ORCS; 239336; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Rxfp3; mouse.
DR   PRO; PR:Q8BGE9; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8BGE9; protein.
DR   Bgee; ENSMUSG00000060735; Expressed in humerus cartilage element and 18 other tissues.
DR   ExpressionAtlas; Q8BGE9; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IC:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IDA:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..472
FT                   /note="Relaxin-3 receptor 1"
FT                   /id="PRO_0000070105"
FT   TOPO_DOM        1..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..119
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..156
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..298
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..332
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        155..247
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   472 AA;  51573 MW;  A0688FCBE06022B1 CRC64;
     MQVASATPAA TVRKAAAGDE LSEFFALTPD LLEVANASGN ASLQLQDLWW ELGLELPDGA
     APGHPPGGGG AESTDTEARV RILISAVYWV VCALGLAGNL LVLYLMKSKQ GWRKSSINLF
     VTNLALTDFQ FVLTLPFWAV ENALDFKWPF GKAMCKIVSM VTSMNMYASV FFLTAMSVAR
     YHSVASALKS HRTRGRGRGD CCGQSLRESC CFSAKVLCGL IWASAALASL PNAIFSTTIR
     VLGEELCLMH FPDKLLGWDR QFWLGLYHLQ KVLLGFLLPL SIISLCYLLL VRFISDRRVV
     GTTDAVGAAA APGGGLSTAS ARRRSKVTKS VTIVVLSFFL CWLPNQALTT WSILIKFNAV
     PFSQEYFQCQ VYAFPVSVCL AHSNSCLNPI LYCLVRREFR KALKNLLWRI ASPSLTNMRP
     FTATTKPEPE DHGLQALAPL NAAAEPDLIY YPPGVVVYSG GRYDLLPSSS AY
 
 
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