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RXFP1_PONAB
ID   RXFP1_PONAB             Reviewed;         757 AA.
AC   Q5R5V8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Relaxin receptor 1;
DE   AltName: Full=Relaxin family peptide receptor 1;
GN   Name=RXFP1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for relaxins. The activity of this receptor is
CC       mediated by G proteins leading to stimulation of adenylate cyclase and
CC       an increase of cAMP. Binding of the ligand may also activate a tyrosine
CC       kinase pathway that inhibits the activity of a phosphodiesterase that
CC       degrades cAMP (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with C1QTNF8. {ECO:0000250|UniProtKB:Q9HBX9}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; CR860744; CAH92858.1; -; mRNA.
DR   RefSeq; NP_001126672.1; NM_001133200.1.
DR   AlphaFoldDB; Q5R5V8; -.
DR   SMR; Q5R5V8; -.
DR   STRING; 9601.ENSPPYP00000016938; -.
DR   GeneID; 100173672; -.
DR   KEGG; pon:100173672; -.
DR   CTD; 59350; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   eggNOG; KOG2087; Eukaryota.
DR   InParanoid; Q5R5V8; -.
DR   OrthoDB; 559381at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 3.80.10.10; -; 2.
DR   Gene3D; 4.10.400.10; -; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR008112; Relaxin_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01739; RELAXINR.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS51450; LRR; 10.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Leucine-rich repeat; Membrane; Metal-binding; Receptor;
KW   Reference proteome; Repeat; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..757
FT                   /note="Relaxin receptor 1"
FT                   /id="PRO_0000312668"
FT   TOPO_DOM        1..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..443
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        465..486
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        508..527
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        528..548
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        549..577
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        578..598
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        599..629
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        630..650
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        651..660
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        661..681
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        682..757
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..63
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          91..127
FT                   /note="LRRNT"
FT   REPEAT          151..172
FT                   /note="LRR 1"
FT   REPEAT          175..196
FT                   /note="LRR 2"
FT   REPEAT          199..220
FT                   /note="LRR 3"
FT   REPEAT          223..244
FT                   /note="LRR 4"
FT   REPEAT          248..269
FT                   /note="LRR 5"
FT   REPEAT          272..293
FT                   /note="LRR 6"
FT   REPEAT          296..317
FT                   /note="LRR 7"
FT   REPEAT          320..341
FT                   /note="LRR 8"
FT   REPEAT          344..365
FT                   /note="LRR 9"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..40
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        485..563
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   757 AA;  86703 MW;  140A8E16F8A6ACDB CRC64;
     MTSGSVFFYI LIIGKYFSHG GGQDVKCSLG YFPCGNITKC LPQLLHCNGV DDCGNQADED
     NCGDNNGWSL QFDKYFASYY KMTSQYPFEA ETPECLVGSV PVQCLCRGLE LDCDETNLRA
     VPSVSSNVTA MSLQWNLIRK LPPDCFKNYH DLQKLYLQNN KITSISIYAF RGLNSLTKLY
     LSHNRITFLK PGVFEDLHRL EWLIIEDNHL SRISPPTFYG LNSLILLVLM NNVLTRLPDK
     PLCQHMPRLH WLDLEGNHIH NLRNLTLISC SNLTVLVMGK NKINHLNENT FAPLQKLDEL
     DLGSNKIENL PPLIFKDLKE LSQLNLSYNP IQKIQANQFD YLVKLKSLSL EGIEISNIQQ
     RMFRPLMNLS HIYFKKFQYC GYAPHVRSGK PNTDGISSLE NLLASIIQRV FVWVVSAVTC
     FGNVFVICMR PYIRSENKLY AMSIISLCCA DCLMGIYLFV IGGFDLKFRG EYNKHAQLWM
     ESTHCQLVGS LAILSTEVSV LLLTFLTLEK YICIVYPFRC VRPGKCRTIT VLILIWITGF
     IVAFIPLSNK EFFKNYYGTN GVCFPLHSED TESIGAQVYS VAIFLGINLA AFIIIVFSYG
     SMFYSVHQSA ITATEIRNQV KKEMILAKRF FFIVFTDALC WIPIFVVKFL SLLQVEIPGT
     ITSWVVIFIL PINSALNPIL YTLTTRPFKE MIHRFWYNYR QRKSMDSKGQ KTYAPSFIWV
     EMWPLQEMPP ELMKPGLFTY PCEMSLISQS TRLNSYS
 
 
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