MOTI_HUMAN
ID MOTI_HUMAN Reviewed; 115 AA.
AC P12872; B7ZLR7; E9PDN2; J3KN51; Q2M1L2; Q5T975; Q6NSY7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Promotilin;
DE Contains:
DE RecName: Full=Motilin;
DE Contains:
DE RecName: Full=Motilin-associated peptide;
DE Short=MAP;
DE Flags: Precursor;
GN Name=MLN;
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 [MRNA] (ISOFORM 1).
RX PubMed=3666144; DOI=10.1016/0014-5793(87)80512-4;
RA Seino Y., Tanaka K., Takeda J., Takahashi H., Mitani T., Kurono M.,
RA Kayano T., Koh G., Fukumoto H., Yano H., Fujita J., Inagaki N., Yamada Y.,
RA Imura H.;
RT "Sequence of an intestinal cDNA encoding human motilin precursor.";
RL FEBS Lett. 223:74-76(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2737284; DOI=10.1016/0014-5793(89)80633-7;
RA Yano H., Seino Y., Fujita J., Yamada Y., Inagaki N., Takeda J., Bell G.I.,
RA Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Imura H.;
RT "Exon-intron organization, expression, and chromosomal localization of the
RT human motilin gene.";
RL FEBS Lett. 249:248-252(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2574660; DOI=10.1089/dna.1989.8.615;
RA Daikh D.I., Douglass J.O., Adelman J.P.;
RT "Structure and expression of the human motilin gene.";
RL DNA 8:615-621(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2914635; DOI=10.1016/0016-5085(89)90892-5;
RA Dea D., Boileau G., Poitras P., Lahaie R.G.;
RT "Molecular heterogeneity of human motilin-like immunoreactivity explained
RT by the processing of prepromotilin.";
RL Gastroenterology 96:695-703(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-15.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 26-40.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP STRUCTURE BY NMR OF 26-47.
RX PubMed=12495026; DOI=10.1023/a:1020902915969;
RA Andersson A., Maler L.;
RT "NMR solution structure and dynamics of motilin in isotropic phospholipid
RT bicellar solution.";
RL J. Biomol. NMR 24:103-112(2002).
CC -!- FUNCTION: Plays an important role in the regulation of interdigestive
CC gastrointestinal motility and indirectly causes rhythmic contraction of
CC duodenal and colonic smooth muscle.
CC -!- INTERACTION:
CC P12872; Q9Y320: TMX2; NbExp=3; IntAct=EBI-18053274, EBI-6447886;
CC P12872; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-18053274, EBI-948354;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P12872-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12872-2; Sequence=VSP_045484;
CC Name=3;
CC IsoId=P12872-3; Sequence=VSP_047653;
CC -!- SIMILARITY: Belongs to the motilin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Motilin entry;
CC URL="https://en.wikipedia.org/wiki/Motilin";
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DR EMBL; Y00695; CAA68690.1; -; mRNA.
DR EMBL; X15393; CAA33448.1; -; Genomic_DNA.
DR EMBL; X15396; CAA33448.1; JOINED; Genomic_DNA.
DR EMBL; X15395; CAA33448.1; JOINED; Genomic_DNA.
DR EMBL; X15394; CAA33448.1; JOINED; Genomic_DNA.
DR EMBL; M30281; AAA59860.1; -; Genomic_DNA.
DR EMBL; M30278; AAA59860.1; JOINED; Genomic_DNA.
DR EMBL; M30279; AAA59860.1; JOINED; Genomic_DNA.
DR EMBL; M30280; AAA59860.1; JOINED; Genomic_DNA.
DR EMBL; AL138889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03752.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03753.1; -; Genomic_DNA.
DR EMBL; BC069675; AAH69675.1; -; mRNA.
DR EMBL; BC112314; AAI12315.1; -; mRNA.
DR EMBL; BC143981; AAI43982.1; -; mRNA.
DR CCDS; CCDS47412.1; -. [P12872-3]
DR CCDS; CCDS4786.1; -. [P12872-1]
DR CCDS; CCDS54993.1; -. [P12872-2]
DR PIR; A33323; A33323.
DR RefSeq; NP_001035198.1; NM_001040109.1. [P12872-3]
DR RefSeq; NP_001171627.1; NM_001184698.1. [P12872-2]
DR RefSeq; NP_002409.1; NM_002418.2. [P12872-1]
DR PDB; 1LBJ; NMR; -; A=26-47.
DR PDBsum; 1LBJ; -.
DR AlphaFoldDB; P12872; -.
DR BMRB; P12872; -.
DR SMR; P12872; -.
DR BioGRID; 110441; 2.
DR IntAct; P12872; 2.
DR STRING; 9606.ENSP00000388825; -.
DR BindingDB; P12872; -.
DR iPTMnet; P12872; -.
DR PhosphoSitePlus; P12872; -.
DR BioMuta; MLN; -.
DR DMDM; 127253; -.
DR MassIVE; P12872; -.
DR PaxDb; P12872; -.
DR PeptideAtlas; P12872; -.
DR PRIDE; P12872; -.
DR ProteomicsDB; 19710; -.
DR ProteomicsDB; 52881; -. [P12872-1]
DR Antibodypedia; 45691; 222 antibodies from 25 providers.
DR DNASU; 4295; -.
DR Ensembl; ENST00000266003.9; ENSP00000266003.5; ENSG00000096395.11. [P12872-3]
DR Ensembl; ENST00000430124.7; ENSP00000388825.2; ENSG00000096395.11. [P12872-1]
DR Ensembl; ENST00000507738.1; ENSP00000425467.1; ENSG00000096395.11. [P12872-2]
DR GeneID; 4295; -.
DR KEGG; hsa:4295; -.
DR MANE-Select; ENST00000430124.7; ENSP00000388825.2; NM_002418.3; NP_002409.1.
DR UCSC; uc003off.2; human. [P12872-1]
DR CTD; 4295; -.
DR DisGeNET; 4295; -.
DR GeneCards; MLN; -.
DR HGNC; HGNC:7141; MLN.
DR HPA; ENSG00000096395; Tissue enriched (intestine).
DR MIM; 158270; gene.
DR neXtProt; NX_P12872; -.
DR OpenTargets; ENSG00000096395; -.
DR PharmGKB; PA30856; -.
DR VEuPathDB; HostDB:ENSG00000096395; -.
DR eggNOG; ENOG502SS7F; Eukaryota.
DR GeneTree; ENSGT00390000000489; -.
DR HOGENOM; CLU_154278_0_0_1; -.
DR InParanoid; P12872; -.
DR OMA; PIFTHSE; -.
DR OrthoDB; 1512819at2759; -.
DR PhylomeDB; P12872; -.
DR TreeFam; TF336217; -.
DR PathwayCommons; P12872; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P12872; -.
DR SIGNOR; P12872; -.
DR BioGRID-ORCS; 4295; 8 hits in 1062 CRISPR screens.
DR ChiTaRS; MLN; human.
DR EvolutionaryTrace; P12872; -.
DR GenomeRNAi; 4295; -.
DR Pharos; P12872; Tbio.
DR PRO; PR:P12872; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P12872; protein.
DR Bgee; ENSG00000096395; Expressed in duodenum and 101 other tissues.
DR Genevisible; P12872; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0031788; F:motilin receptor binding; IPI:GO_Central.
DR InterPro; IPR006737; Motilin_assoc.
DR InterPro; IPR006738; Motilin_ghrelin.
DR InterPro; IPR015662; Promotilin.
DR PANTHER; PTHR14156; PTHR14156; 1.
DR Pfam; PF04643; Motilin_assoc; 1.
DR Pfam; PF04644; Motilin_ghrelin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cleavage on pair of basic residues;
KW Direct protein sequencing; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 26..115
FT /note="Promotilin"
FT /id="PRO_0000342171"
FT PEPTIDE 26..47
FT /note="Motilin"
FT /id="PRO_0000019184"
FT PEPTIDE 50..115
FT /note="Motilin-associated peptide"
FT /id="PRO_0000019185"
FT REGION 39..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 106..113
FT /note="SEMLPQHA -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045484"
FT VAR_SEQ 114..115
FT /note="AK -> K (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047653"
FT VARIANT 15
FT /note="V -> A (in dbSNP:rs2281820)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_020372"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1LBJ"
SQ SEQUENCE 115 AA; 12920 MW; 30D4BB59B2F42783 CRC64;
MVSRKAVAAL LVVHVAAMLA SQTEAFVPIF TYGELQRMQE KERNKGQKKS LSVWQRSGEE
GPVDPAEPIR EEENEMIKLT APLEIGMRMN SRQLEKYPAT LEGLLSEMLP QHAAK
