COPA_CANLF
ID COPA_CANLF Reviewed; 35 AA.
AC P40765;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Coatomer subunit alpha;
DE AltName: Full=Alpha-coat protein;
DE Short=Alpha-COP;
DE AltName: Full=HEP-COP;
DE Short=HEPCOP;
DE Contains:
DE RecName: Full=Xenin;
DE AltName: Full=Xenopsin-related peptide;
DE Contains:
DE RecName: Full=Proxenin;
DE Flags: Fragment;
GN Name=COPA;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Pancreas;
RX PubMed=8899805; DOI=10.1016/0196-9781(96)00150-7;
RA Hamscher G., Meyer H.E., Feurle G.E.;
RT "Identification of proxenin as a precursor of the peptide xenin with
RT sequence homology to yeast and mammalian coat protein alpha.";
RL Peptides 17:889-893(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-25.
RX PubMed=2235681; DOI=10.1016/0196-9781(90)90190-g;
RA Carraway R.E., Mitra S.P.;
RT "Isolation and sequence of canine xenopsin and an extended fragment from
RT its precursor.";
RL Peptides 11:747-752(1990).
CC -!- FUNCTION: Xenin stimulates exocrine pancreatic secretion. It inhibits
CC pentagastrin-stimulated secretion of acid, to induce exocrine
CC pancreatic secretion and to affect small and large intestinal motility.
CC In the gut, xenin interacts with the neurotensin receptor.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Probably interacts with
CC PEX11A. Interacts with SCYL1. Interacts with JAGN1 (By similarity).
CC Interacts with TMEM41B (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P53621}.
CC -!- TISSUE SPECIFICITY: Gastric, duodenal and jejunal mucosa. Circulates in
CC the blood. Seems to be confined to specific endocrine cells.
CC -!- DEVELOPMENTAL STAGE: Released into the circulation after a meal.
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DR PIR; A60412; A60412.
DR AlphaFoldDB; P40765; -.
DR SMR; P40765; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hormone; Reference proteome.
FT CHAIN 1..>35
FT /note="Coatomer subunit alpha"
FT /id="PRO_0000223306"
FT PEPTIDE 1..35
FT /note="Proxenin"
FT /id="PRO_0000041402"
FT PEPTIDE 1..25
FT /note="Xenin"
FT /id="PRO_0000041403"
FT NON_TER 35
SQ SEQUENCE 35 AA; 4035 MW; C3B0A0EB307CF24E CRC64;
MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQL