ID   ITR_CATCO               Reviewed;         390 AA.
AC   Q90334;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Isotocin receptor;
DE            Short=ITR;
OS   Catostomus commersonii (White sucker) (Cyprinus commersonnii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Catostomoidei; Catostomidae; Catostomus.
OX   NCBI_TaxID=7971;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7656982; DOI=10.1016/0014-5793(95)00832-t;
RA   Hausmann H., Meyerhof W., Zwiers H., Lederis K., Richter D.;
RT   "Teleost isotocin receptor: structure, functional expression, mRNA
RT   distribution and phylogeny.";
RL   FEBS Lett. 370:227-230(1995).
CC   -!- FUNCTION: Binds to isotocin. Can also be activated by vasotocin,
CC       mesotocin, oxytocin and Arg-vasopressin, although these have lower
CC       potencies than isotocin. Produces an induction of membrane chloride
CC       currents indicating that it is coupled to the inositol
CC       phosphate/calcium pathway.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, intestine, bladder, skeletal
CC       muscle, lateral line, gills and kidney.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Vasopressin/oxytocin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00521}.
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DR   EMBL; X87783; CAA61050.1; -; mRNA.
DR   PIR; S66497; S66497.
DR   AlphaFoldDB; Q90334; -.
DR   SMR; Q90334; -.
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:0004990; F:oxytocin receptor activity; IEA:InterPro.
DR   GO; GO:0005000; F:vasopressin receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR002062; Oxytocn_rcpt.
DR   InterPro; IPR001817; Vasoprsn_rcpt.
DR   PANTHER; PTHR24241:SF89; PTHR24241:SF89; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00665; OXYTOCINR.
DR   PRINTS; PR00896; VASOPRESSINR.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..390
FT                   /note="Isotocin receptor"
FT                   /id="PRO_0000069694"
FT   TOPO_DOM        1..48
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   390 AA;  44504 MW;  2C3E9BA244FD6913 CRC64;
     MEEMFKEQDF WSFNESSRNS TVGNETFGGN QTVNPLKRNE EVAKVEVTVL ALVLFLALAG
     NLCVLIAIYT AKHTQSRMYY LMKHLSIADL VVAVFQVLPQ LIWDITFRFY GPDFLCRLVK
     YLQTVGMFAS TYMLVLMSID RCIAICQPLR SLHKRKDRCY VIVSWALSLV FSVPQVYIFS
     LREIGNGVYD CWGDFVQPWG AKAYITWISL TIYIIPVAIL GGCYGLISFK IWQNFKRKTK
     KDQCITLTTA ASKANALARV SSVKLVSKAK ITTVKMTFVI VLAYIVCWTP FFFVQMWSAW
     DPEAPREAMP FIISMLLASL NSCCNPWIYM FFAGHLFHDL KQSLLCCSTL YLKSSQCRCD
     QEHDSRKSNC STYVIKSTSS QRSITQSSIT