ID   MOTI_HUMAN              Reviewed;         115 AA.
AC   P12872; Q2M1L2; Q5T975; Q6NSY7;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-JAN-2012, entry version 110.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88030048; 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.,
RA   Yamada Y., 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   MEDLINE=89289989; PubMed=2737284; DOI=10.1016/0014-5793(89)80633-7;
RA   Yano H., Seino Y., Fujita J., Yamada Y., Inagaki N., Takeda J.,
RA   Bell G.I., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Imura H.;
RT   "Exon-intron organization, expression, and chromosomal localization of
RT   the human motilin gene.";
RL   FEBS Lett. 249:248-252(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90091748; PubMed=2574660;
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].
RX   MEDLINE=89121385; PubMed=2914635;
RA   Dea D., Boileau G., Poitras P., Lahaie R.G.;
RT   "Molecular heterogeneity of human motilin-like immunoreactivity
RT   explained by the processing of prepromotilin.";
RL   Gastroenterology 96:695-703(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22935763; 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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT 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
RT   project: 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
RT   verified 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
RT   phospholipid bicellar solution.";
RL   J. Biomol. NMR 24:103-112(2002).
CC   -!- FUNCTION: Plays an important role in the regulation of
CC       interdigestive gastrointestinal motility and indirectly causes
CC       rhythmic contraction of duodenal and colonic smooth muscle.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the motilin family.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Motilin entry;
CC       URL="http://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; CAI21441.2; -; Genomic_DNA.
DR   EMBL; AL158049; CAI21441.2; JOINED; Genomic_DNA.
DR   EMBL; AL158049; CAI21526.2; -; Genomic_DNA.
DR   EMBL; AL138889; CAI21526.2; JOINED; Genomic_DNA.
DR   EMBL; CH471081; EAX03753.1; -; Genomic_DNA.
DR   EMBL; BC069675; AAH69675.1; -; mRNA.
DR   EMBL; BC112314; AAI12315.1; -; mRNA.
DR   IPI; IPI00025878; -.
DR   PIR; A33323; A33323.
DR   RefSeq; NP_001035198.1; NM_001040109.1.
DR   RefSeq; NP_001171627.1; NM_001184698.1.
DR   RefSeq; NP_002409.1; NM_002418.2.
DR   UniGene; Hs.2813; -.
DR   PDB; 1LBJ; NMR; -; A=26-47.
DR   PDBsum; 1LBJ; -.
DR   STRING; P12872; -.
DR   DMDM; 127253; -.
DR   PRIDE; P12872; -.
DR   Ensembl; ENST00000266003; ENSP00000266003; ENSG00000096395.
DR   GeneID; 4295; -.
DR   KEGG; hsa:4295; -.
DR   UCSC; uc003off.1; human.
DR   CTD; 4295; -.
DR   GeneCards; GC06M033809; -.
DR   H-InvDB; HIX0032938; -.
DR   HGNC; HGNC:7141; MLN.
DR   MIM; 158270; gene.
DR   neXtProt; NX_P12872; -.
DR   PharmGKB; PA30856; -.
DR   eggNOG; prNOG20517; -.
DR   GeneTree; ENSGT00390000000489; -.
DR   HOGENOM; HBG100930; -.
DR   HOVERGEN; HBG003618; -.
DR   InParanoid; P12872; -.
DR   OMA; ERNKGQK; -.
DR   OrthoDB; EOG4RV2SZ; -.
DR   PhylomeDB; P12872; -.
DR   Reactome; REACT_111102; Signal Transduction.
DR   NextBio; 16905; -.
DR   ArrayExpress; P12872; -.
DR   Bgee; P12872; -.
DR   CleanEx; HS_MLN; -.
DR   Genevestigator; P12872; -.
DR   GermOnline; ENSG00000096395; Homo sapiens.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005625; C:soluble fraction; TAS:ProtInc.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
DR   InterPro; IPR015662; Motilin.
DR   InterPro; IPR006737; Motilin_assoc.
DR   InterPro; IPR006738; Motilin_ghrelin.
DR   KO; K05265; -.
DR   PANTHER; PTHR14156; Motilin; 1.
DR   Pfam; PF04643; Motilin_assoc; 1.
DR   Pfam; PF04644; Motilin_ghrelin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Hormone; Polymorphism; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL        1     25
FT   CHAIN        26    115       Promotilin.
FT                                /FTId=PRO_0000342171.
FT   PEPTIDE      26     47       Motilin.
FT                                /FTId=PRO_0000019184.
FT   PEPTIDE      50    115       Motilin-associated peptide.
FT                                /FTId=PRO_0000019185.
FT   VARIANT      15     15       V -> A (in dbSNP:rs2281820).
FT                                /FTId=VAR_020372.
FT   HELIX        32     46
SQ   SEQUENCE   115 AA;  12920 MW;  30D4BB59B2F42783 CRC64;
     MVSRKAVAAL LVVHVAAMLA SQTEAFVPIF TYGELQRMQE KERNKGQKKS LSVWQRSGEE
     GPVDPAEPIR EEENEMIKLT APLEIGMRMN SRQLEKYPAT LEGLLSEMLP QHAAK
//