ID   SCRN1_RAT               Reviewed;         414 AA.
AC   Q6AY84;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Secernin-1;
GN   Name=Scrn1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 303-315 AND 356-366, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: 'Secern' is an archaic English term meaning 'secrete'.
CC   -!- SIMILARITY: Belongs to the peptidase C69 family. Secernin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC079152; AAH79152.1; -; mRNA.
DR   RefSeq; NP_001020234.1; NM_001025063.1.
DR   RefSeq; XP_006236574.1; XM_006236512.3.
DR   AlphaFoldDB; Q6AY84; -.
DR   SMR; Q6AY84; -.
DR   STRING; 10116.ENSRNOP00000013088; -.
DR   iPTMnet; Q6AY84; -.
DR   PhosphoSitePlus; Q6AY84; -.
DR   SwissPalm; Q6AY84; -.
DR   PaxDb; Q6AY84; -.
DR   PRIDE; Q6AY84; -.
DR   Ensembl; ENSRNOT00000013088; ENSRNOP00000013088; ENSRNOG00000009636.
DR   GeneID; 502776; -.
DR   KEGG; rno:502776; -.
DR   UCSC; RGD:1560999; rat.
DR   CTD; 9805; -.
DR   RGD; 1560999; Scrn1.
DR   eggNOG; ENOG502QTSN; Eukaryota.
DR   GeneTree; ENSGT00390000013474; -.
DR   HOGENOM; CLU_046840_0_0_1; -.
DR   InParanoid; Q6AY84; -.
DR   OMA; SSCHTFQ; -.
DR   OrthoDB; 322959at2759; -.
DR   PhylomeDB; Q6AY84; -.
DR   TreeFam; TF323890; -.
DR   PRO; PR:Q6AY84; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000009636; Expressed in cerebellum and 20 other tissues.
DR   Genevisible; Q6AY84; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
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; IEA:UniProtKB-KW.
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   Cytoplasm; Direct protein sequencing; Exocytosis; Reference proteome.
FT   CHAIN           1..414
FT                   /note="Secernin-1"
FT                   /id="PRO_0000271394"
SQ   SEQUENCE   414 AA;  46396 MW;  A636EA15FD189CA3 CRC64;
     MSGAPPSYSF VALPPRAKDG LVVFGKNSAR PRDEVQEVVY FPAVDHEAES KVECTYISID
     QVPRTHAIVI SRPAWLWGAE MGANEHGVCI ANEAINAREP AAETEALLGM DLVRLGLERG
     TTAKEALDII VSLLDEHGQG GNYYEDAHSC HSFQSAYLLV DRDEAWVLET VGKYWAAERI
     TEGVRCICNH LSLTTKMDEE HPELRTYAQS QGWWTGEDEF NFAQVFSPAD DHLDCCAGKD
     SLEKQEESIT VQTMINILRD KASGVCIDSE SFLTTASIVS VLPQNRSSPC IHYFTGTPDP
     SRSIFKPFIF VDDVKLVPKA QSPCFGDDDP AKKEPRFQEK PDRRHELYKA HEWARAVIES
     DQEQGRTLRK TMLELEKQGL EAMEEILSSP EPPDPAEVGD LFYDCVDTEM KFFK