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Protein

Promotilin

Gene

MLN

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the regulation of interdigestive gastrointestinal motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle.1 Publication

Keywords - Molecular functioni

Hormone

Names & Taxonomyi

Protein namesi
Recommended name:
Promotilin
Cleaved into the following 2 chains:
Gene namesi
Name:MLN
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 11994PromotilinPRO_0000342173Add
BLAST
Peptidei26 – 4722MotilinPRO_0000019188Add
BLAST
Peptidei50 – 11970Motilin-associated peptidePRO_0000019189Add
BLAST

Keywords - PTMi

Cleavage on pair of basic residues

Proteomic databases

PaxDbiP01307.

Expressioni

Gene expression databases

GenevisibleiP01307. SS.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000001650.

Family & Domainsi

Sequence similaritiesi

Belongs to the motilin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J17F. Eukaryota.
ENOG411197B. LUCA.
HOGENOMiHOG000108883.
HOVERGENiHBG003618.
InParanoidiP01307.
KOiK05265.
OrthoDBiEOG7RRF9Q.
TreeFamiTF336217.

Family and domain databases

InterProiIPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR015662. Promotilin.
[Graphical view]
PANTHERiPTHR14156. PTHR14156. 1 hit.
PfamiPF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01307-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSRKAVVVL LVVHAAAMLA SHTEAFVPIF TYGELQRMQE KERNKGQKKS
60 70 80 90 100
LSVQQASEEL GPLDPSEPTK EEERVVIKLL APVDIGIRMD SRQLEKYRAT
110
LERLLGQAPQ STQNQNAAK
Length:119
Mass (Da):13,296
Last modified:August 1, 1992 - v2
Checksum:i6E31A1038E142671
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291I → S in AAA31088 (PubMed:2456453).Curated
Sequence conflicti29 – 291I → S in ABG23101 (Ref. 3) Curated
Sequence conflicti103 – 1031R → G in ABC94729 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31219 mRNA. Translation: AAA31088.1.
DQ355970 mRNA. Translation: ABC94729.1.
DQ663494 Genomic DNA. Translation: ABG23101.1.
PIRiA40932. MSPG.
RefSeqiNP_999400.1. NM_214235.1.
XP_013833249.1. XM_013977795.1.
XP_013833250.1. XM_013977796.1.
UniGeneiSsc.714.

Genome annotation databases

GeneIDi397466.
KEGGissc:397466.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31219 mRNA. Translation: AAA31088.1.
DQ355970 mRNA. Translation: ABC94729.1.
DQ663494 Genomic DNA. Translation: ABG23101.1.
PIRiA40932. MSPG.
RefSeqiNP_999400.1. NM_214235.1.
XP_013833249.1. XM_013977795.1.
XP_013833250.1. XM_013977796.1.
UniGeneiSsc.714.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000001650.

Proteomic databases

PaxDbiP01307.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397466.
KEGGissc:397466.

Organism-specific databases

CTDi4295.

Phylogenomic databases

eggNOGiENOG410J17F. Eukaryota.
ENOG411197B. LUCA.
HOGENOMiHOG000108883.
HOVERGENiHBG003618.
InParanoidiP01307.
KOiK05265.
OrthoDBiEOG7RRF9Q.
TreeFamiTF336217.

Gene expression databases

GenevisibleiP01307. SS.

Family and domain databases

InterProiIPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR015662. Promotilin.
[Graphical view]
PANTHERiPTHR14156. PTHR14156. 1 hit.
PfamiPF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of complementary deoxyribonucleic acid for precursor of porcine motilin."
    Bond C.T., Nilaver G., Godfrey B., Zimmerman E.A., Adelman J.P.
    Mol. Endocrinol. 2:175-180(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Two SNP found in motilin in China Meishan pig."
    Ying M., Yang Z.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequencing and chromosome mapping of pig ghrelin and motilin genes."
    Ying M., Yang Z.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Motilin, a gastric motor activity stimulating polypeptide: the complete amino acid sequence."
    Brown J.C., Cook M.A., Dryburgh J.R.
    Can. J. Biochem. 51:533-537(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-47.
  5. "Correction to the amino acid sequence of porcine motilin."
    Schubert H., Brown J.C.
    Can. J. Biochem. 52:7-8(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. Yajima H., Kai Y., Kawatani H.
    J. Chem. Soc. Chem. Commun. 1975:159-160(1975)
    Cited for: SYNTHESIS.
  7. "The further purification of motilin, a gastric motor activity stimulating polypeptide from the mucosa of the small intestine of hogs."
    Brown J.C., Mutt V., Dryburgh J.R.
    Can. J. Physiol. Pharmacol. 49:399-405(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Sequence-specific 1H NMR assignments and secondary structure of porcine motilin."
    Khan N., Graslund A., Ehrenberg A., Shriver J.
    Biochemistry 29:5743-5751(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 26-47.
  9. "The solution structure of motilin from NMR distance constraints, distance geometry, molecular dynamics, and an iterative full relaxation matrix refinement."
    Edmondson S., Khan N., Shriver J., Zdunek J., Graslund A.
    Biochemistry 30:11271-11279(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 26-47.

Entry informationi

Entry nameiMOTI_PIG
AccessioniPrimary (citable) accession number: P01307
Secondary accession number(s): A5X8W5, Q2I0F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1992
Last modified: June 8, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.