SNG2_RAT
ID SNG2_RAT Reviewed; 224 AA.
AC O54980;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Synaptogyrin-2 {ECO:0000305};
DE AltName: Full=Cellugyrin {ECO:0000303|PubMed:9446595};
GN Name=Syngr2 {ECO:0000312|RGD:621334};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RX PubMed=9446595; DOI=10.1074/jbc.273.5.2851;
RA Janz R., Suedhof T.C.;
RT "Cellugyrin, a novel ubiquitous form of synaptogyrin that is phosphorylated
RT by pp60(c-src).";
RL J. Biol. Chem. 273:2851-2857(1998).
RN [2]
RP FUNCTION.
RX PubMed=10383386; DOI=10.1074/jbc.274.27.18893;
RA Sugita S., Janz R., Suedhof T.C.;
RT "Synaptogyrins regulate Ca2+-dependent exocytosis in PC12 cells.";
RL J. Biol. Chem. 274:18893-18901(1999).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=10967091; DOI=10.1074/jbc.m002797200;
RA Kupriyanova T.A., Kandror K.V.;
RT "Cellugyrin is a marker for a distinct population of intracellular Glut4-
RT containing vesicles.";
RL J. Biol. Chem. 275:36263-36268(2000).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12928441; DOI=10.1074/jbc.m304174200;
RA Belfort G.M., Kandror K.V.;
RT "Cellugyrin and synaptogyrin facilitate targeting of synaptophysin to a
RT ubiquitous synaptic vesicle-sized compartment in PC12 cells.";
RL J. Biol. Chem. 278:47971-47978(2003).
RN [5]
RP FUNCTION.
RX PubMed=15590695; DOI=10.1074/jbc.m404851200;
RA Belfort G.M., Bakirtzi K., Kandror K.V.;
RT "Cellugyrin induces biogenesis of synaptic-like microvesicles in PC12
RT cells.";
RL J. Biol. Chem. 280:7262-7272(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 15-PHE--LEU-17.
RX PubMed=26071524; DOI=10.1242/jcs.166561;
RA Kioumourtzoglou D., Pryor P.R., Gould G.W., Bryant N.J.;
RT "Alternative routes to the cell surface underpin insulin-regulated membrane
RT trafficking of GLUT4.";
RL J. Cell Sci. 128:2423-2429(2015).
CC -!- FUNCTION: May play a role in regulated exocytosis (PubMed:10383386). In
CC neuronal cells, modulates the localization of synaptophysin/SYP into
CC synaptic-like microvesicles and may therefore play a role in the
CC formation and/or the maturation of this vesicles (PubMed:12928441,
CC PubMed:15590695). May also play a role in GLUT4 storage and transport
CC to the plasma membrane (PubMed:26071524). {ECO:0000269|PubMed:10383386,
CC ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:15590695,
CC ECO:0000269|PubMed:26071524}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:26071524}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:12928441,
CC ECO:0000269|PubMed:9446595}; Multi-pass membrane protein {ECO:0000255}.
CC Note=Localizes to cytoplasmic vesicles associated with the recycling
CC endosomes. {ECO:0000269|PubMed:10967091}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with lower expression in
CC brain (at protein level). {ECO:0000269|PubMed:9446595}.
CC -!- PTM: May be tyrosine phosphorylated by Src.
CC {ECO:0000269|PubMed:9446595}.
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB96666.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF039085; AAB96666.1; ALT_INIT; mRNA.
DR RefSeq; NP_446005.1; NM_053553.1.
DR AlphaFoldDB; O54980; -.
DR IntAct; O54980; 1.
DR STRING; 10116.ENSRNOP00000064123; -.
DR PhosphoSitePlus; O54980; -.
DR PaxDb; O54980; -.
DR PRIDE; O54980; -.
DR GeneID; 89815; -.
DR KEGG; rno:89815; -.
DR CTD; 9144; -.
DR RGD; 621334; Syngr2.
DR eggNOG; KOG4016; Eukaryota.
DR InParanoid; O54980; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; O54980; -.
DR PRO; PR:O54980; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; IMP:UniProtKB.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR016579; Synaptogyrin.
DR PANTHER; PTHR10838; PTHR10838; 1.
DR Pfam; PF01284; MARVEL; 1.
DR PIRSF; PIRSF011282; Synaptogyrin; 1.
DR PROSITE; PS51225; MARVEL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasmic vesicle; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..224
FT /note="Synaptogyrin-2"
FT /id="PRO_0000183995"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 20..171
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43760"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43760"
FT MUTAGEN 15..17
FT /note="FDL->AAA: Increased localization to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:26071524"
SQ SEQUENCE 224 AA; 24711 MW; 5F21F25B44652FDA CRC64;
MESGAYGAAN AGGSFDLRRY VSQPQVVTRL VSMVLALIVF SCIFGEGYIN LHSSDQLHCV
FNRNEDACRY GSAIGVLAFL ASAFFLVVDA FFSQISNATD RKYLVIGDLL FSALWTFLWF
VGFCFLTNQW AATKPDDVLV GADSARAAIT FSFFSIFSWG VLASLAYQRY KAGVDAFIQN
YVDPTPDPTT AYASYPSASV ENYQQPPFTQ NVETTEGYQP PPVY
