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Database: UniProt
Entry: A0A091S203_NESNO
LinkDB: A0A091S203_NESNO
Original site: A0A091S203_NESNO 
ID   A0A091S203_NESNO        Unreviewed;       430 AA.
AC   A0A091S203;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Cholecystokinin receptor type A {ECO:0000256|ARBA:ARBA00022044};
DE   AltName: Full=Cholecystokinin-1 receptor {ECO:0000256|ARBA:ARBA00030703};
DE   Flags: Fragment;
GN   ORFNames=N333_07512 {ECO:0000313|EMBL:KFQ48593.1};
OS   Nestor notabilis (Kea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX   NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ48593.1, ECO:0000313|Proteomes:UP000053840};
RN   [1] {ECO:0000313|EMBL:KFQ48593.1, ECO:0000313|Proteomes:UP000053840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ48593.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and
CC       enzyme secretion, smooth muscle contraction of the gall bladder and
CC       stomach. Has a 1000-fold higher affinity for CCK rather than for
CC       gastrin. It modulates feeding and dopamine-induced behavior in the
CC       central and peripheral nervous system. This receptor mediates its
CC       action by association with G proteins that activate a
CC       phosphatidylinositol-calcium second messenger system.
CC       {ECO:0000256|ARBA:ARBA00025653}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU000688}.
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DR   EMBL; KK938212; KFQ48593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091S203; -.
DR   Proteomes; UP000053840; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004951; F:cholecystokinin receptor activity; IEA:InterPro.
DR   CDD; cd15978; 7tmA_CCK-AR; 1.
DR   Gene3D; 4.10.670.10; Cholecystokinin A receptor, N-terminal domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR   InterPro; IPR009126; Cholcskin_rcpt.
DR   InterPro; IPR000596; Cholcy_rcpt_A.
DR   InterPro; IPR015276; CholecystokininA_recpt_N.
DR   InterPro; IPR036472; CholecystokininA_recpt_N_sf.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24238:SF57; CHOLECYSTOKININ-2 RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24238; G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF09193; CholecysA-Rec_N; 1.
DR   PRINTS; PR01822; CCYSTOKININR.
DR   PRINTS; PR00524; CCYSTOKNINAR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU000688};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        49..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..373
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ48593.1"
FT   NON_TER         430
FT                   /evidence="ECO:0000313|EMBL:KFQ48593.1"
SQ   SEQUENCE   430 AA;  48523 MW;  E35EE5475C294069 CRC64;
     RMEIVDASFL GNGTNFTAFL CDIILENDTF FCVDDPPYPS KDLHQIIRIL LYCLIFLLSA
     LGNILVITVL IRNKRMRTVT NTFLLSLAVS DLMLCLFCMP FTLIPNLLKD FIFGSTVCKT
     ATYFMGVSVS VSTFNLVAIS LERYSAICKP LQSRVWQTKS HALKVIAATW CVSFTIMAPY
     PIYSKLVPFT KYNNTTANMC RLLWPSDVIQ QSWYTFLLLI LFLIPGIIMM VAYGLISLEL
     YRGIKFDASQ RKPSRERKVS TCSAKYEDGD GCYLNKTKRK RKMPLQQLSA TSHSKIDRVR
     SSSSSANLMA KKLVIRMLMV IVVLFFLCWT PIFSVNAWRA FDTASADQRL SGAPISFIHL
     LSYTSACVNP IIYCFMNKRF RMGFLDTFTC CAKQKPPAIR GEVGDEEEGK TTGASLSKCS
     YMHMNASAPP
//
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