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SYCN_RAT
ID   SYCN_RAT                Reviewed;         134 AA.
AC   O35775;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Syncollin;
DE   AltName: Full=Proximal small intestine-specific protein 9;
DE   Flags: Precursor;
GN   Name=Sycn; Synonyms=Sip9;
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 [MRNA], PROTEIN SEQUENCE OF 102-124, INTERACTION WITH
RP   SYNTAXIN-1 AND STX2, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Pancreas;
RX   PubMed=9244306; DOI=10.1016/s0092-8674(00)80340-2;
RA   Edwardson J.M., An S., Jahn R.;
RT   "The secretory granule protein syncollin binds to syntaxin in a Ca2(+)-
RT   sensitive manner.";
RL   Cell 90:325-333(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley; TISSUE=Duodenum;
RX   PubMed=10666056; DOI=10.1152/ajpgi.2000.278.2.g308;
RA   Tan S., Hooi S.C.;
RT   "Syncollin is differentially expressed in rat proximal small intestine and
RT   regulated by feeding behavior.";
RL   Am. J. Physiol. 278:G308-G320(2000).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BONDS,
RP   AND OLIGOMERIZATION.
RX   PubMed=10753942; DOI=10.1074/jbc.275.15.11306;
RA   An S.J., Hansen N.J., Hodel A., Jahn R., Edwardson J.M.;
RT   "Analysis of the association of syncollin with the membrane of the
RT   pancreatic zymogen granule.";
RL   J. Biol. Chem. 275:11306-11311(2000).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=11389693; DOI=10.1042/0264-6021:3560843;
RA   Hodel A., An S.J., Hansen N.J., Lawrence J., Waesle B., Schrader M.,
RA   Edwardson J.M.;
RT   "Cholesterol-dependent interaction of syncollin with the membrane of the
RT   pancreatic zymogen granule.";
RL   Biochem. J. 356:843-850(2001).
RN   [5]
RP   SUBCELLULAR LOCATION, TOPOLOGY, OLIGOMERIZATION, AND INTERACTION WITH GP2.
RX   PubMed=11853552; DOI=10.1042/0264-6021:3620433;
RA   Kalus I., Hodel A., Koch A., Kleene R., Edwardson J.M., Schrader M.;
RT   "Interaction of syncollin with GP-2, the major membrane protein of
RT   pancreatic zymogen granules, and association with lipid microdomains.";
RL   Biochem. J. 362:433-442(2002).
RN   [6]
RP   FUNCTION, AND OLIGOMERIZATION.
RX   PubMed=12235484; DOI=10.1007/s00232-002-1005-9;
RA   Geisse N.A., Waesle B., Saslowsky D.E., Henderson R.M., Edwardson J.M.;
RT   "Syncollin homo-oligomers associate with lipid bilayers in the form of
RT   doughnut-shaped structures.";
RL   J. Membr. Biol. 189:83-92(2002).
RN   [7]
RP   FUNCTION.
RX   PubMed=15766266; DOI=10.1021/bi048894d;
RA   Li J., Luo R., Hooi S.C., Ruga P., Zhang J., Meda P., Li G.;
RT   "Ectopic expression of syncollin in INS-1 beta-cells sorts it into granules
RT   and impairs regulated secretion.";
RL   Biochemistry 44:4365-4374(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=15817827; DOI=10.1677/joe.1.05934;
RA   Hays L.B., Wicksteed B., Wang Y., McCuaig J.F., Philipson L.H.,
RA   Edwardson J.M., Rhodes C.J.;
RT   "Intragranular targeting of syncollin, but not a syncollinGFP chimera,
RT   inhibits regulated insulin exocytosis in pancreatic beta-cells.";
RL   J. Endocrinol. 185:57-67(2005).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=16517980; DOI=10.1369/jhc.5a6792.2006;
RA   Bach J.-P., Borta H., Ackermann W., Faust F., Borchers O., Schrader M.;
RT   "The secretory granule protein syncollin localizes to HL-60 cells and
RT   neutrophils.";
RL   J. Histochem. Cytochem. 54:877-888(2006).
CC   -!- FUNCTION: Functions in exocytosis in pancreatic acinar cells regulating
CC       the fusion of zymogen granules with each other. May have a pore-forming
CC       activity on membranes and regulate exocytosis in other exocrine
CC       tissues. {ECO:0000269|PubMed:12235484, ECO:0000269|PubMed:15766266,
CC       ECO:0000269|PubMed:15817827}.
CC   -!- SUBUNIT: Monomer and homooligomer; most probably hexameric. Interacts
CC       with GP2. According to PubMed:10753942 interaction with syntaxins shown
CC       in PubMed:9244306 is physiologically questionable.
CC       {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:9244306}.
CC   -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC       {ECO:0000269|PubMed:10753942, ECO:0000269|PubMed:11389693,
CC       ECO:0000269|PubMed:11853552}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:10753942, ECO:0000269|PubMed:11389693,
CC       ECO:0000269|PubMed:11853552}; Lumenal side
CC       {ECO:0000269|PubMed:10753942, ECO:0000269|PubMed:11389693,
CC       ECO:0000269|PubMed:11853552}. Zymogen granule lumen
CC       {ECO:0000269|PubMed:11389693}. Note=Associated in a cholesterol-
CC       dependent manner with lipid rafts of zymogen granule membranes.
CC       {ECO:0000269|PubMed:11389693}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in pancreas and also
CC       detected in secretory granules of parotid gland (at protein level).
CC       Expressed in pancreas, spleen, small intestine, lung and neutrophilic
CC       granulocytes (at protein level). Expressed by epithelial cells in
CC       duodenum and colon. {ECO:0000269|PubMed:10666056,
CC       ECO:0000269|PubMed:16517980, ECO:0000269|PubMed:9244306}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in gut after birth.
CC       {ECO:0000269|PubMed:10666056}.
CC   -!- INDUCTION: Down-regulated in small intestine upon fasting.
CC       {ECO:0000269|PubMed:10666056}.
CC   -!- PTM: Contains intrachain disulfide bonds.
CC   -!- MISCELLANEOUS: Syncollin comes from the Greek word meaning to glue
CC       together.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC53314.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR   EMBL; AF008197; AAC53314.1; ALT_SEQ; mRNA.
DR   EMBL; AF012887; AAC27983.1; -; mRNA.
DR   RefSeq; NP_620786.1; NM_139086.1.
DR   AlphaFoldDB; O35775; -.
DR   SMR; O35775; -.
DR   STRING; 10116.ENSRNOP00000026907; -.
DR   PaxDb; O35775; -.
DR   Ensembl; ENSRNOT00000026907; ENSRNOP00000026907; ENSRNOG00000019879.
DR   GeneID; 245917; -.
DR   UCSC; RGD:620862; rat.
DR   CTD; 342898; -.
DR   RGD; 620862; Sycn.
DR   eggNOG; ENOG502S3UP; Eukaryota.
DR   GeneTree; ENSGT00390000014835; -.
DR   HOGENOM; CLU_1890586_0_0_1; -.
DR   InParanoid; O35775; -.
DR   OMA; PYLPSNW; -.
DR   OrthoDB; 1433772at2759; -.
DR   PhylomeDB; O35775; -.
DR   TreeFam; TF338021; -.
DR   PRO; PR:O35775; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019879; Expressed in pancreas and 14 other tissues.
DR   Genevisible; O35775; RN.
DR   GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; TAS:RGD.
DR   InterPro; IPR028137; Syncollin.
DR   PANTHER; PTHR17503; PTHR17503; 1.
DR   Pfam; PF15138; Syncollin; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Exocytosis;
KW   Membrane; Reference proteome; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..134
FT                   /note="Syncollin"
FT                   /id="PRO_0000072358"
SQ   SEQUENCE   134 AA;  14635 MW;  98CD4576850CAD94 CRC64;
     MSPLCLLLLA LALVAVPGAR GACPVPADLK KSDGTRTCAR LYENSDPYYD NCCQGPELSV
     DPGTDLPYLP SDWSNSASSL VVAQRCELTV WSLPGKRGKT RKFSTGSYPR LEEYRKGIFG
     TWAKSISGLY CKCY
 
 
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