MTLR_HUMAN
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 03-AUG-2022, entry version 172.
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 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 GlyGen; O43193; 2 sites.
DR iPTMnet; O43193; -.
DR PhosphoSitePlus; O43193; -.
DR BioMuta; MLNR; -.
DR MassIVE; O43193; -.
DR PaxDb; O43193; -.
DR PeptideAtlas; O43193; -.
DR PRIDE; O43193; -.
DR ProteomicsDB; 48807; -. [O43193-1]
DR ProteomicsDB; 48808; -. [O43193-2]
DR Antibodypedia; 42284; 220 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 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; ENSGT01050000244813; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; O43193; -.
DR OMA; SRMMYFS; -.
DR OrthoDB; 890529at2759; -.
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; 6 hits in 1070 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 bone marrow and 24 other tissues.
DR Genevisible; O43193; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004930; F:G protein-coupled receptor activity; IBA: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 InterPro; IPR003905; GHS-R/MTLR.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR039132; MTLR.
DR PANTHER; PTHR24243:SF3; PTHR24243:SF3; 1.
DR Pfam; PF00001; 7tm_1; 2.
DR PRINTS; PR01417; GHSRECEPTOR.
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 2: Evidence at transcript level;
KW 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"
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
