SNG1_MOUSE
ID SNG1_MOUSE Reviewed; 234 AA.
AC O55100; B9EI16; Q543Y5; Q9DCB0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Synaptogyrin-1 {ECO:0000305};
GN Name=Syngr1 {ECO:0000312|MGI:MGI:1328323};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1B).
RX PubMed=9760194; DOI=10.1007/s004390050795;
RA Kedra D., Pan H.-Q., Seroussi E., Fransson I., Guilbaud C., Collins J.E.,
RA Dunham I., Blennow E., Roe B.A., Piehl F., Dumanski J.P.;
RT "Characterization of the human synaptogyrin gene family.";
RL Hum. Genet. 103:131-141(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
RC TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 11-22 AND 137-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10595519; DOI=10.1016/s0896-6273(00)81122-8;
RA Janz R., Suedhof T.C., Hammer R.E., Unni V., Siegelbaum S.A.,
RA Bolshakov V.Y.;
RT "Essential roles in synaptic plasticity for synaptogyrin I and
RT synaptophysin I.";
RL Neuron 24:687-700(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in regulated exocytosis. Modulates the
CC localization of synaptophysin/SYP into synaptic-like microvesicles and
CC may therefore play a role in synaptic-like microvesicle formation
CC and/or maturation (By similarity). Involved in the regulation of short-
CC term and long-term synaptic plasticity (PubMed:10595519).
CC {ECO:0000250|UniProtKB:Q62876, ECO:0000269|PubMed:10595519}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q62876}. Melanosome
CC {ECO:0000250|UniProtKB:O43759}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1A;
CC IsoId=O55100-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=O55100-2; Sequence=VSP_006333;
CC -!- DISRUPTION PHENOTYPE: Mice lacking both Syngr1 and Syp show normal
CC brain structure and composition, but impaired short-term and long-term
CC synaptic plasticity. {ECO:0000269|PubMed:10595519}.
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ002306; CAA05323.1; -; mRNA.
DR EMBL; AK002972; BAB22487.1; -; mRNA.
DR EMBL; AK010442; BAB26943.1; -; mRNA.
DR EMBL; AK044007; BAC31736.1; -; mRNA.
DR EMBL; BC138728; AAI38729.1; -; mRNA.
DR EMBL; BC138729; AAI38730.1; -; mRNA.
DR CCDS; CCDS27657.1; -. [O55100-1]
DR CCDS; CCDS27658.1; -. [O55100-2]
DR RefSeq; NP_033329.1; NM_009303.2. [O55100-2]
DR RefSeq; NP_997591.1; NM_207708.1. [O55100-1]
DR AlphaFoldDB; O55100; -.
DR BioGRID; 203605; 2.
DR STRING; 10090.ENSMUSP00000009727; -.
DR TCDB; 9.B.130.2.5; the tetraspan vesicle membrane protein (tvp) family.
DR iPTMnet; O55100; -.
DR PhosphoSitePlus; O55100; -.
DR MaxQB; O55100; -.
DR PaxDb; O55100; -.
DR PeptideAtlas; O55100; -.
DR PRIDE; O55100; -.
DR ProteomicsDB; 257535; -. [O55100-1]
DR ProteomicsDB; 257536; -. [O55100-2]
DR Antibodypedia; 26612; 184 antibodies from 31 providers.
DR DNASU; 20972; -.
DR Ensembl; ENSMUST00000009727; ENSMUSP00000009727; ENSMUSG00000022415. [O55100-1]
DR Ensembl; ENSMUST00000009728; ENSMUSP00000009728; ENSMUSG00000022415. [O55100-2]
DR GeneID; 20972; -.
DR KEGG; mmu:20972; -.
DR UCSC; uc007wvd.1; mouse. [O55100-1]
DR CTD; 9145; -.
DR MGI; MGI:1328323; Syngr1.
DR VEuPathDB; HostDB:ENSMUSG00000022415; -.
DR eggNOG; KOG4016; Eukaryota.
DR GeneTree; ENSGT00950000182935; -.
DR HOGENOM; CLU_079186_1_0_1; -.
DR InParanoid; O55100; -.
DR OMA; WSQWSSA; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; O55100; -.
DR TreeFam; TF320995; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 20972; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Syngr1; mouse.
DR PRO; PR:O55100; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O55100; protein.
DR Bgee; ENSMUSG00000022415; Expressed in dentate gyrus of hippocampal formation granule cell and 204 other tissues.
DR ExpressionAtlas; O55100; baseline and differential.
DR Genevisible; O55100; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006605; P:protein targeting; ISO:MGI.
DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; ISS: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; Alternative splicing; Cytoplasmic vesicle;
KW Direct protein sequencing; Membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..234
FT /note="Synaptogyrin-1"
FT /id="PRO_0000183991"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..71
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..148
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q62876"
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"
FT VAR_SEQ 162..234
FT /note="AGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPSAGSDPAGMGG
FT TYQHPANAFDAEPQGYQSQGY -> SLTAALAVRRFKELTFQEEYNTLFPASAQP (in
FT isoform 1B)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9760194"
FT /id="VSP_006333"
SQ SEQUENCE 234 AA; 25653 MW; 09566021DF3E809A CRC64;
MEGGAYGAGK AGGAFDPYTL VRQPHTILRV VSWVFSIVVF GSIVNEGYLN NPEEEEEFCI
YNRNPNACSY GVTVGVLAFL TCLLYLALDV YFPQISSVKD RKKAVLSDIG VSAFWAFFWF
VGFCFLANQW QVSKPKDNPL NEGTDAARAA IAFSFFSIFT WAGQAVLAFQ RYQIGADSAL
FSQDYMDPSQ DSSMPYAPYV EPSAGSDPAG MGGTYQHPAN AFDAEPQGYQ SQGY
