ID   MTR_RHIMB               Reviewed;         389 AA.
AC   Q90252;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Mesotocin receptor;
DE            Short=MTR;
OS   Rhinella marina (Cane toad) (Bufo marinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX   NCBI_TaxID=8386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Urinary bladder;
RX   PubMed=8647123; DOI=10.1111/j.1432-1033.1996.0759p.x;
RA   Akhundova A., Getmanova E., Gorboulev V., Garnazzi E., Eggena P.,
RA   Fahrenholz F.;
RT   "Cloning and functional characterization of the amphibian mesotocin
RT   receptor, a member of the oxytocin/vasopressin receptor superfamily.";
RL   Eur. J. Biochem. 237:759-767(1996).
CC   -!- FUNCTION: Binds to mesotocin and may play a role in the regulation of
CC       water and salt transport.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the bladder. Also expressed in
CC       kidney, brain and skeletal muscle.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Vasopressin/oxytocin receptor subfamily. {ECO:0000255|PROSITE-
CC       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; X93313; CAA63713.1; -; mRNA.
DR   PIR; S71336; S71336.
DR   AlphaFoldDB; Q90252; -.
DR   SMR; Q90252; -.
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   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..389
FT                   /note="Mesotocin receptor"
FT                   /id="PRO_0000069882"
FT   TOPO_DOM        1..50
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..119
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          360..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        117..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   389 AA;  44384 MW;  D24EBF372EBB6B38 CRC64;
     MEGLCLNLDC SELPNSSWVN SSMENQNHSS NSTRDPLKRN EEVAKVEVTV LALILFLALA
     GNICVLLGIY INRHKHSRMY FFMKHLSIAD LVVAIFQVLP QLIWDITFRF YAPDLVCRLV
     TYLQVVGMFA STYMLLLMSL DRCLAICQPL RSLHRRSDCV YVLFTWILSF LLSTPQTVIF
     SLTEVGNGVY DCRADFIQPW GPKAYITWIT LAVYIIPVMI LSVCYGLISY KIWQNIRLKT
     VCESNLRLST SRRATLSRVS SVRLISKAKI RTVKMTFIIV LAYIVCWTPF FFVQMWSVWD
     PNPPKEASLF IIAMLLGSLN SCCNPWIYML FTGHLFHDLL QSFLCCSARY LKTQQQGSDL
     SASRKSNSST FVLSRKSSSQ KSITQPSTA