ID   MOTI_CAVPO              Reviewed;         127 AA.
AC   Q99MP5;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 56.
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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Intestine;
RX   PubMed=11172801; DOI=10.1016/s0014-5793(01)02125-1;
RA   Xu L., Depoortere I., Tang M., Peeters T.L.;
RT   "Identification and expression of the motilin precursor in the guinea
RT   pig.";
RL   FEBS Lett. 490:7-10(2001).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Present in the gut mucosa with the exception of the
CC       gastric corpus. Also present in medulla oblongata, nucleus of the
CC       solitary tract, hypophysis, spinal cord, hypothalamus, and cerebellum
CC       but not in the cerebral cortex.
CC   -!- SIMILARITY: Belongs to the motilin family. {ECO:0000305}.
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DR   EMBL; AF323752; AAK07442.1; -; mRNA.
DR   RefSeq; NP_001166331.1; NM_001172860.1.
DR   AlphaFoldDB; Q99MP5; -.
DR   GeneID; 100379560; -.
DR   CTD; 4295; -.
DR   InParanoid; Q99MP5; -.
DR   OrthoDB; 1512819at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..127
FT                   /note="Promotilin"
FT                   /id="PRO_0000342168"
FT   PEPTIDE         26..47
FT                   /note="Motilin"
FT                   /id="PRO_0000019178"
FT   PEPTIDE         50..127
FT                   /note="Motilin-associated peptide"
FT                   /id="PRO_0000019179"
FT   REGION          41..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   127 AA;  14156 MW;  A46E90C0E7EFC220 CRC64;
     MLSRKAVAAL LLVHVTAMLA SQTEGFVPIF TYSELRRTQE REQNKRLRKS LRVQQRSKAA
     GRLEPQEVME EEENGVIKLT APVEIGVGLS SRQLEKHRAV LEALLSEALP PPSLVFGGQR
     PVTAAWE