SNG1_RAT
ID SNG1_RAT Reviewed; 234 AA.
AC Q62876;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Synaptogyrin-1 {ECO:0000305};
DE AltName: Full=p29 {ECO:0000303|PubMed:8557746};
GN Name=Syngr1 {ECO:0000312|RGD:3801};
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, AND TOPOLOGY.
RX PubMed=8557746; DOI=10.1083/jcb.131.6.1801;
RA Stenius K., Janz R., Suedhof T.C., Jahn R.;
RT "Structure of synaptogyrin (p29) defines novel synaptic vesicle protein.";
RL J. Cell Biol. 131:1801-1809(1995).
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 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 [4]
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).
CC -!- FUNCTION: May play a role in regulated exocytosis (PubMed:10383386).
CC Modulates the localization of synaptophysin/SYP into synaptic-like
CC microvesicles and may therefore play a role in synaptic-like
CC microvesicle formation and/or maturation (PubMed:15590695,
CC PubMed:12928441). Involved in the regulation of short-term and long-
CC term synaptic plasticity (By similarity).
CC {ECO:0000250|UniProtKB:O55100, ECO:0000269|PubMed:10383386,
CC ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:15590695}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:12928441,
CC ECO:0000269|PubMed:8557746}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8557746}. Melanosome
CC {ECO:0000250|UniProtKB:O43759}.
CC -!- TISSUE SPECIFICITY: Nervous system (at protein level).
CC {ECO:0000269|PubMed:8557746}.
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
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DR EMBL; U39549; AAB17890.1; -; mRNA.
DR RefSeq; NP_062039.1; NM_019166.2.
DR AlphaFoldDB; Q62876; -.
DR BioGRID; 247883; 2.
DR IntAct; Q62876; 1.
DR MINT; Q62876; -.
DR STRING; 10116.ENSRNOP00000023066; -.
DR PhosphoSitePlus; Q62876; -.
DR PaxDb; Q62876; -.
DR PRIDE; Q62876; -.
DR Ensembl; ENSRNOT00000023066; ENSRNOP00000023066; ENSRNOG00000017108.
DR GeneID; 29205; -.
DR KEGG; rno:29205; -.
DR UCSC; RGD:3801; rat.
DR CTD; 9145; -.
DR RGD; 3801; Syngr1.
DR eggNOG; KOG4016; Eukaryota.
DR GeneTree; ENSGT00950000182935; -.
DR HOGENOM; CLU_079186_0_1_1; -.
DR InParanoid; Q62876; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; Q62876; -.
DR TreeFam; TF320995; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q62876; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000017108; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; Q62876; baseline and differential.
DR Genevisible; Q62876; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISO:RGD.
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; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..234
FT /note="Synaptogyrin-1"
FT /id="PRO_0000183992"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8557746"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..71
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8557746"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8557746"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..148
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8557746"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8557746"
FT DOMAIN 20..173
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 201..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43759"
SQ SEQUENCE 234 AA; 25669 MW; B3038B64C49F31E1 CRC64;
MEGGAYGAGK AGGAFDPYTL VRQPHTILRV VSWVFSIVVF GSIVNEGYLN NPEEEEEFCI
YNRNPNACSY GVTVGVLAFL TCLVYLALDV YFPQISSVKD RKKAVLSDIG VSAFWAFFWF
VGFCFLANQW QVSKPKDNPL NEGTDAARAA IAFSFFSIFT WAGQAVLAFQ RYQIGADSAL
FSQDYMDPSQ DSSMPYAPYV EPSAGSDPTG MGGTYQHPAN AFDAEPQGYQ SQGY
