SCRN1_BOVIN
ID SCRN1_BOVIN Reviewed; 414 AA.
AC P83939;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Secernin-1;
DE AltName: Full=p50;
GN Name=SCRN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 17-32; 65-72; 99-115; 198-206; 304-315; 337-365 AND
RP 370-377.
RC TISSUE=Brain {ECO:0000269|PubMed:12221138};
RX PubMed=12221138; DOI=10.1091/mbc.e01-10-0094;
RA Way G., Morrice N., Smythe C., O'Sullivan A.J.O.;
RT "Purification and identification of secernin, a novel cytosolic protein
RT that regulates exocytosis in mast cells.";
RL Mol. Biol. Cell 13:3344-3354(2002).
CC -!- FUNCTION: Regulates exocytosis in mast cells. Increases both the extent
CC of secretion and the sensitivity of mast cells to stimulation with
CC calcium. {ECO:0000269|PubMed:12221138}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: 'Secern' is an archaic English term meaning 'secrete'.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C69 family. Secernin subfamily.
CC {ECO:0000305}.
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DR RefSeq; XP_010802602.1; XM_010804300.2.
DR RefSeq; XP_010802603.1; XM_010804301.2.
DR AlphaFoldDB; P83939; -.
DR SMR; P83939; -.
DR STRING; 9913.ENSBTAP00000021588; -.
DR PaxDb; P83939; -.
DR PRIDE; P83939; -.
DR Ensembl; ENSBTAT00000021588; ENSBTAP00000021588; ENSBTAG00000016223.
DR GeneID; 534933; -.
DR CTD; 9805; -.
DR VEuPathDB; HostDB:ENSBTAG00000016223; -.
DR VGNC; VGNC:34366; SCRN1.
DR eggNOG; ENOG502QTSN; Eukaryota.
DR GeneTree; ENSGT00390000013474; -.
DR HOGENOM; CLU_046840_0_0_1; -.
DR InParanoid; P83939; -.
DR OMA; SSCHTFQ; -.
DR OrthoDB; 322959at2759; -.
DR TreeFam; TF323890; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000016223; Expressed in prefrontal cortex and 101 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0070004; F:cysteine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR005322; Peptidase_C69.
DR PANTHER; PTHR12994; PTHR12994; 1.
DR Pfam; PF03577; Peptidase_C69; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Exocytosis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q12765"
FT CHAIN 2..414
FT /note="Secernin-1"
FT /id="PRO_0000221435"
FT ACT_SITE 9
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q12765"
FT CONFLICT 70..71
FT /note="IS -> AE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 46202 MW; C7419065A5D3DA77 CRC64;
MAVAPPSYCF VAFPPRAKDG LVVFGKNSAR PRDEVQEVVY FSAADHEPES KVECTYISIN
QVPRTHAIVI SRPAWLWGAE MGANEHGVCI ANEAINAREP AAETEALLGM DLVRLGLERG
ATAKEALDVI VALLEEHGQG GNYYEDANSC HSFQSAFLIV DREEAWVLET VGKYWAAEKI
TEGVKCICNQ LSLTTKIDAE HPELRSYAQS QGWWMGEDEF NFSEVFSPAD DHLTCCSGRD
TLEKQEESIT VQTMIDVLRD KASGVCVDSE SFLTTASVVS VLPQNGSSPC IHYFTGTPDP
SRSIFKPFIF VDDVKLVPKA QSPCFGDDDP AKKEPRFQEK PDRRHELYKA HEWARAVLES
DEEQGQKLRK TMLELEKQGL EAMEEILTSS DPLDPTEVGD LFYDCVDTEI KFFK