位置:首页 > 蛋白库 > GPR9_AMPAM
GPR9_AMPAM
ID   GPR9_AMPAM              Reviewed;         476 AA.
AC   Q93126; Q93128;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Probable G-protein coupled receptor No9;
OS   Amphibalanus amphitrite (Striped barnacle) (Balanus amphitrite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Cirripedia; Thoracica; Thoracicalcarea; Balanomorpha; Balanoidea;
OC   Balanidae; Amphibalaninae; Amphibalanus.
OX   NCBI_TaxID=1232801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Darwin;
RX   PubMed=8917082; DOI=10.1016/0378-1119(96)00130-8;
RA   Isoai A., Kawahara H., Okazaki Y., Shizuri Y.;
RT   "Molecular cloning of a new member of the putative G protein-coupled
RT   receptor gene from barnacle Balanus amphitrite.";
RL   Gene 175:95-100(1996).
CC   -!- FUNCTION: Orphan G-protein coupled receptor.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D78363; BAA11375.1; -; Genomic_DNA.
DR   EMBL; D78587; BAA11424.1; -; Genomic_DNA.
DR   PIR; JC5042; JC5042.
DR   AlphaFoldDB; Q93126; -.
DR   SMR; Q93126; -.
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:0004935; F:adrenergic receptor activity; IEA:InterPro.
DR   InterPro; IPR002233; ADR_fam.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..476
FT                   /note="Probable G-protein coupled receptor No9"
FT                   /id="PRO_0000069659"
FT   TOPO_DOM        1..36
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..60
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..103
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..127
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..172
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..430
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          266..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            113
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   SITE            208
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        106..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        454
FT                   /note="R -> A (in Ref. 1; BAA11424)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  53246 MW;  0F55B51595D5CD06 CRC64;
     MEGPPLSPAP ADNVTLNVSC GRPATLFDWA DHRLISLLAL AFLNLMVVAG NLLVVMAVFV
     HSKLRTVTNL FIVSLACADL LVGMLVLPFS ATLEVLDVWL YGDVWCSVWL AVDVWMCTSS
     ILNLCAISLD RYLAVSQPIS YPSLMSTRRA KQLIAAVWVL SFVICFPPLV GWNDRPGTLI
     GSRGSSACRL TCELTNERGY VIYSALGSFF LPSTVMLFFY GRIYRTAVST TRAIAQGFRT
     TKEDEEGRLT LRIHRGRSVT QRAEQAAAGG ARAHGQVRLT LSEPGARRQN KPSFVVHCRE
     DSRAKNQYEI YTVVEGDSRP GRRVPQPQRP AKKLSSASQS SEDDSRPPRF ISRVSRRNVR
     HQARRFRMET KAAKTVGIIV GLFILCWLPF FVCYLVRGFC ADCVPPLLFS VFFWLGYCNS
     AVNPCVYALC SRDFRFAFSS ILCKCVCRRG AMERRFRRTL LVGNRSQTEE DCEVAD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024