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UniProtKB/Swiss-Prot entry P12872


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MOTI_HUMAN
Primary accession number P12872
Secondary accession number Q6NSY7
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 79)
Name and origin of the protein
Protein name Promotilin [Precursor]
Synonyms None
Contains Motilin
Motilin-associated peptide
     (MAP)
Gene name
Name: MLN
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0014-5793(87)80512-4; PubMed=3666144 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence of an intestinal cDNA encoding human motilin precursor.";
FEBS Lett. 223:74-76(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0014-5793(89)80633-7; PubMed=2737284 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Exon-intron organization, expression, and chromosomal localization of the human motilin gene.";
FEBS Lett. 249:248-252(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2574660 [NCBI, ExPASy, EBI, Israel, Japan]
Daikh D.I., Douglass J.O., Adelman J.P.;
"Structure and expression of the human motilin gene.";
DNA 8:615-621(1989).
[4]
NUCLEOTIDE SEQUENCE.
PubMed=2914635 [NCBI, ExPASy, EBI, Israel, Japan]
Dea D., Boileau G., Poitras P., Lahaie R.G.;
"Molecular heterogeneity of human motilin-like immunoreactivity explained by the processing of prepromotilin.";
Gastroenterology 96:695-703(1989).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-15.
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 26-40.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00695; CAA68690.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15393; CAA33448.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15396; CAA33448.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15395; CAA33448.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15394; CAA33448.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30281; AAA59860.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30278; AAA59860.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30279; AAA59860.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30280; AAA59860.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069675; AAH69675.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A33323; A33323.
RefSeq NP_001035198.1; -.
NP_002409.1; -.
UniGene Hs.2813
3D structure databases
PDB
1LBJ; NMR; -; A=26-47.[ExPASy / RCSB / EBI]
PDBsum 1LBJ; -.
ModBase P12872.
Organism-specific databases
H-InvDB HIX0032938; -.
HGNC HGNC:7141; MLN.
GeneLynx MLN; Homo sapiens.
GenAtlas MLN.
MIM 158270; gene. [NCBI / EBI]
PharmGKB PA30402; -.
GeneCards P12872.
Gene expression databases
ArrayExpress P12872; -.
CleanEx HS_MLN; -.
GermOnline ENSG00000096395; Homo sapiens.
Ontologies
GO
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005102; Molecular function: receptor binding (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR015662; Motilin.
IPR006737; Motilin_assoc.
IPR006738; Motilin_ghrelin.
Graphical view of domain structure.
PANTHER PTHR14156; Motilin; 1.
Pfam PF04643; Motilin_assoc; 1.
PF04644; Motilin_ghrelin; 1.
Pfam graphical view of domain structure.
BLOCKS P12872.
Genome annotation databases
Ensembl ENSG00000096395; Homo sapiens. [Contig view]
GeneID 4295; -.
KEGG hsa:4295; -.
Phylogenomic databases
HOGENOM P12872; -.
HOVERGEN P12872; -.
Other
SOURCE MLN; Homo sapiens.
ProtoNet P12872.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cleavage on pair of basic residues; Direct protein sequencing; Hormone; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
SIGNAL   1    25  25      
CHAIN   26   115  90     Promotilin. PRO_0000342171
PEPTIDE   26    47  22     Motilin. PRO_0000019184
PEPTIDE   50   115  66     Motilin-associated peptide. PRO_0000019185
VARIANT   15    15  1     V -> A (in dbSNP:rs2281820 [NCBI]). VAR_020372 
HELIX   32    46  15      
Sequence information
Length: 115 AA [This is the length of the unprocessed precursor] Molecular weight: 12920 Da [This is the MW of the unprocessed precursor] CRC64: 30D4BB59B2F42783 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVSRKAVAAL LVVHVAAMLA SQTEAFVPIF TYGELQRMQE KERNKGQKKS LSVWQRSGEE 

        70         80         90        100        110 
GPVDPAEPIR EEENEMIKLT APLEIGMRMN SRQLEKYPAT LEGLLSEMLP QHAAK 

P12872 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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