Reviewed, UniProtKB/Swiss-Prot P12872 (MOTI_HUMAN)

Names and origin

Protein names

Recommended name:
    Promotilin
Cleaved into the following 2 chains:
    1- Recommended name:
            Motilin
    2- Recommended name:
            Motilin-associated peptide
                Short name=MAP

Gene names

Name:

MLN

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	115 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays an important role in the regulation of interdigestive gastrointestinal motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle.
Subcellular location	Secreted.
Sequence similarities	Belongs to the motilin family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hormone
PTM	Cleavage on pair of basic residues
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	G-protein coupled receptor protein signaling pathway Traceable author statement. Source: ProtInc cell-cell signaling Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Traceable author statement. Source: ProtInc
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.8

Chain

26 – 115

90

Promotilin

PRO_0000342171

Peptide

26 – 47

22

Motilin

PRO_0000019184

Peptide

50 – 115

66

Motilin-associated peptide

PRO_0000019185

Natural variations

Natural variant

15

1

V → A: dbSNP rs2281820. Ref.7

VAR_020372

Secondary structure

1

.

.

.

115

Helix Strand Turn

Details...

Helix

32 – 46

15

Sequences

	Sequence		Length	Mass (Da)
	P12872-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 30D4BB59B2F42783	FASTA	115	12,920
	10 20 30 40 50 60 MVSRKAVAAL LVVHVAAMLA SQTEAFVPIF TYGELQRMQE KERNKGQKKS LSVWQRSGEE 70 80 90 100 110 GPVDPAEPIR EEENEMIKLT APLEIGMRMN SRQLEKYPAT LEGLLSEMLP QHAAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of an intestinal cDNA encoding human motilin precursor." Seino Y., Tanaka K., Takeda J., Takahashi H., Mitani T., Kurono M., Kayano T., Koh G., Fukumoto H., Yano H., Fujita J., Inagaki N., Yamada Y., Imura H. FEBS Lett. 223:74-76(1987) [PubMed: 3666144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Exon-intron organization, expression, and chromosomal localization of the human motilin gene." Yano H., Seino Y., Fujita J., Yamada Y., Inagaki N., Takeda J., Bell G.I., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Imura H. FEBS Lett. 249:248-252(1989) [PubMed: 2737284] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Structure and expression of the human motilin gene." Daikh D.I., Douglass J.O., Adelman J.P. DNA 8:615-621(1989) [PubMed: 2574660] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Molecular heterogeneity of human motilin-like immunoreactivity explained by the processing of prepromotilin." Dea D., Boileau G., Poitras P., Lahaie R.G. Gastroenterology 96:695-703(1989) [PubMed: 2914635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-15. Tissue: Brain.
[8]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-40.
[9]	"NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution." Andersson A., Maler L. J. Biomol. NMR 24:103-112(2002) [PubMed: 12495026] [Abstract] Cited for: STRUCTURE BY NMR OF 26-47.
+	Additional computationally mapped references.

Web resources

Wikipedia

Motilin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00695 mRNA. Translation: CAA68690.1.
X15393 , X15396, X15395, X15394 Genomic DNA. Translation: CAA33448.1.
M30281 , M30278, M30279, M30280 Genomic DNA. Translation: AAA59860.1.
AL138889, AL158049 Genomic DNA. Translation: CAI21441.2.
AL158049, AL138889 Genomic DNA. Translation: CAI21526.2.
CH471081 Genomic DNA. Translation: EAX03753.1.
BC069675 mRNA. Translation: AAH69675.1.
BC112314 mRNA. Translation: AAI12315.1.

IPI

IPI00025878.

PIR

A33323.

RefSeq

NP_001035198.1.
NP_002409.1.

UniGene

Hs.2813

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LBJ	NMR	-	A	26-47	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P12872.

Proteomic databases

PRIDE

P12872.

Genome annotation databases

Ensembl

ENST00000266003; ENSP00000266003; ENSG00000096395; Homo sapiens. [Genome view]

GeneID

4295.

KEGG

hsa:4295.

UCSC

uc003off.1. human.

Organism-specific databases

CTD

4295.

GeneCards

GC06M033870.

H-InvDB

HIX0032938.

HGNC

HGNC:7141. MLN.

MIM

158270. gene.

PharmGKB

PA30402.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20517.

HOGENOM

HBG100930.

HOVERGEN

P12872.

InParanoid

P12872.

OMA

ERNKGQK.

OrthoDB

EOG9D299F.

PhylomeDB

P12872.

Gene expression databases

ArrayExpress

P12872.

Bgee

P12872.

CleanEx

HS_MLN.

Genevestigator

P12872.

GermOnline

ENSG00000096395. Homo sapiens.

Family and domain databases

InterPro

IPR015662. Motilin.
IPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
[Graphical view]

PANTHER

PTHR14156. Motilin. 1 hit.

Pfam

PF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16905.

SOURCE

Search...

Entry information

Entry name

MOTI_HUMAN

Accession

Primary (citable) accession number: P12872
Secondary accession number(s): Q2M1L2, Q5T975, Q6NSY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	February 9, 2010
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.