ID   MTLR_HUMAN              Reviewed;         412 AA.
AC   O43193;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Motilin receptor;
DE   AltName: Full=G-protein coupled receptor 38;
GN   Name=MLNR; Synonyms=GPR38, MTLR, MTLR1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX   PubMed=9441746; DOI=10.1006/geno.1997.5069;
RA   McKee K.K., Tan C.P., Palyha O.C., Liu J., Feighner S.D., Hreniuk D.L.,
RA   Smith R.G., Howard A.D., van der Ploeg L.H.T.;
RT   "Cloning and characterization of two human G protein-coupled receptor genes
RT   (GPR38 and GPR39) related to the growth hormone secretagogue and
RT   neurotensin receptors.";
RL   Genomics 46:426-434(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS A AND B).
RX   PubMed=10381885; DOI=10.1126/science.284.5423.2184;
RA   Feighner S.D., Tan C.P., McKee K.K., Palyha O.C., Hreniuk D.L., Pong S.-S.,
RA   Austin C.P., Figueroa D., MacNeil D., Cascieri M.A., Nargund R., Bakshi R.,
RA   Abramovitz M., Stocco R., Kargman S., O'Neill G., van Der Ploeg L.H.T.,
RA   Evans J., Patchett A.A., Smith R.G., Howard A.D.;
RT   "Receptor for motilin identified in the human gastrointestinal system.";
RL   Science 284:2184-2188(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   TISSUE=Stomach;
RA   King M.M., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=11322507; DOI=10.1385/endo:14:1:009;
RA   Smith R.G., Leonard R., Bailey A.R.T., Palyha O.C., Feighner S.D.,
RA   Tan C.P., Mckee K.K., Pong S.-S., Griffin P.R., Howard A.D.;
RT   "Growth hormone secretagogue receptor family members and ligands.";
RL   Endocrine 14:9-14(2001).
CC   -!- FUNCTION: Receptor for motilin. {ECO:0000269|PubMed:11322507}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=O43193-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=O43193-2; Sequence=VSP_001894;
CC   -!- TISSUE SPECIFICITY: Expressed only in thyroid, stomach, and bone
CC       marrow.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF034632; AAC26081.1; -; Genomic_DNA.
DR   EMBL; AY603964; AAT35806.1; -; mRNA.
DR   EMBL; AL137000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS9414.1; -. [O43193-1]
DR   RefSeq; NP_001498.1; NM_001507.1. [O43193-1]
DR   PDB; 8IBU; EM; 3.51 A; R=1-412.
DR   PDB; 8IBV; EM; 3.19 A; R=1-412.
DR   PDBsum; 8IBU; -.
DR   PDBsum; 8IBV; -.
DR   AlphaFoldDB; O43193; -.
DR   SMR; O43193; -.
DR   BioGRID; 109120; 64.
DR   STRING; 9606.ENSP00000218721; -.
DR   BindingDB; O43193; -.
DR   ChEMBL; CHEMBL2203; -.
DR   DrugBank; DB00199; Erythromycin.
DR   DrugBank; DB06587; Mitemcinal.
DR   DrugCentral; O43193; -.
DR   GuidetoPHARMACOLOGY; 297; -.
DR   GlyCosmos; O43193; 2 sites, No reported glycans.
DR   GlyGen; O43193; 2 sites.
DR   iPTMnet; O43193; -.
DR   PhosphoSitePlus; O43193; -.
DR   BioMuta; MLNR; -.
DR   MassIVE; O43193; -.
DR   PaxDb; 9606-ENSP00000218721; -.
DR   PeptideAtlas; O43193; -.
DR   ProteomicsDB; 48807; -. [O43193-1]
DR   ProteomicsDB; 48808; -. [O43193-2]
DR   Antibodypedia; 42284; 242 antibodies from 25 providers.
DR   DNASU; 2862; -.
DR   Ensembl; ENST00000218721.1; ENSP00000218721.1; ENSG00000102539.5. [O43193-1]
DR   GeneID; 2862; -.
DR   KEGG; hsa:2862; -.
DR   MANE-Select; ENST00000218721.1; ENSP00000218721.1; NM_001507.1; NP_001498.1.
DR   UCSC; uc010tgj.2; human. [O43193-1]
DR   AGR; HGNC:4495; -.
DR   CTD; 2862; -.
DR   DisGeNET; 2862; -.
DR   GeneCards; MLNR; -.
DR   HGNC; HGNC:4495; MLNR.
DR   HPA; ENSG00000102539; Tissue enhanced (bone marrow, thyroid gland).
DR   MIM; 602885; gene.
DR   neXtProt; NX_O43193; -.
DR   OpenTargets; ENSG00000102539; -.
DR   PharmGKB; PA28884; -.
DR   VEuPathDB; HostDB:ENSG00000102539; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263484; -.
DR   HOGENOM; CLU_009579_6_5_1; -.
DR   InParanoid; O43193; -.
DR   OMA; ERRCSPF; -.
DR   OrthoDB; 3471593at2759; -.
DR   PhylomeDB; O43193; -.
DR   TreeFam; TF336314; -.
DR   PathwayCommons; O43193; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   SignaLink; O43193; -.
DR   SIGNOR; O43193; -.
DR   BioGRID-ORCS; 2862; 7 hits in 1146 CRISPR screens.
DR   GeneWiki; Motilin_receptor; -.
DR   GenomeRNAi; 2862; -.
DR   Pharos; O43193; Tchem.
DR   PRO; PR:O43193; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; O43193; Protein.
DR   Bgee; ENSG00000102539; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 25 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IPI:GO_Central.
DR   GO; GO:0042562; F:hormone binding; IPI:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR003905; GHS-R/MTLR.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24243; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24243:SF3; MOTILIN RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 2.
DR   PRINTS; PR01417; GHSRECEPTOR.
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.
DR   Genevisible; O43193; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..412
FT                   /note="Motilin receptor"
FT                   /id="PRO_0000069860"
FT   TOPO_DOM        1..35
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..94
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..134
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..246
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..270
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..298
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..320
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..334
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..358
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..412
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        111..235
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         301..412
FT                   /note="LVVVLAFIICWLPFHVGRIIYINTEDSRMMYFSQYFNIVALQLFYLSASINP
FT                   ILYNLISKKYRAAAFKLLLARKSRPRGFHRSRDTAGEVAGDTGGDTVGYTETSANVKTM
FT                   G -> RKWSRRGSKDACLQSAPPGTAQTLGPLPLLAQLWAPLPAPFPISIPASTRRGGG
FT                   SGIYNLLVALPRWQNHLHKHGRFADDVLLSVL (in isoform B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001894"
FT   HELIX           35..65
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           72..88
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           91..99
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           108..140
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           152..169
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           171..174
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           226..230
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           242..252
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           254..274
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           293..321
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           327..355
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   TURN            356..358
FT                   /evidence="ECO:0007829|PDB:8IBV"
FT   HELIX           360..370
FT                   /evidence="ECO:0007829|PDB:8IBV"
SQ   SEQUENCE   412 AA;  45344 MW;  C13FF6165012DEF3 CRC64;
     MGSPWNGSDG PEGAREPPWP ALPPCDERRC SPFPLGALVP VTAVCLCLFV VGVSGNVVTV
     MLIGRYRDMR TTTNLYLGSM AVSDLLILLG LPFDLYRLWR SRPWVFGPLL CRLSLYVGEG
     CTYATLLHMT ALSVERYLAI CRPLRARVLV TRRRVRALIA VLWAVALLSA GPFLFLVGVE
     QDPGISVVPG LNGTARIASS PLASSPPLWL SRAPPPSPPS GPETAEAAAL FSRECRPSPA
     QLGALRVMLW VTTAYFFLPF LCLSILYGLI GRELWSSRRP LRGPAASGRE RGHRQTVRVL
     LVVVLAFIIC WLPFHVGRII YINTEDSRMM YFSQYFNIVA LQLFYLSASI NPILYNLISK
     KYRAAAFKLL LARKSRPRGF HRSRDTAGEV AGDTGGDTVG YTETSANVKT MG
//