SNG2_MOUSE
ID SNG2_MOUSE Reviewed; 224 AA.
AC O55101; Q3TCK2; Q8C225; Q99K83;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Synaptogyrin-2 {ECO:0000305};
DE AltName: Full=Cellugyrin {ECO:0000303|PubMed:12928441};
GN Name=Syngr2 {ECO:0000312|MGI:MGI:1328324};
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].
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 [MRNA].
RA Sun M.Y., Reay P.A.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA O-Wang J.;
RT "Isolation of a CD40-activated gene from murine splenic B cells.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Dendritic cell;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-215.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [6]
RP 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).
CC -!- FUNCTION: May play a role in regulated exocytosis. In neuronal cells,
CC modulates the localization of synaptophysin/SYP into synaptic-like
CC microvesicles and may therefore play a role in the formation and/or the
CC maturation of this vesicles. May also play a role in GLUT4 storage and
CC transport to the plasma membrane. {ECO:0000250|UniProtKB:O54980}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:12928441}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:12928441}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to cytoplasmic vesicles associated with
CC the recycling endosomes. {ECO:0000250|UniProtKB:O54980}.
CC -!- PTM: May be tyrosine phosphorylated by Src.
CC {ECO:0000250|UniProtKB:O54980}.
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
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DR EMBL; AJ002307; CAA05324.1; -; mRNA.
DR EMBL; AF151985; AAD38046.1; -; mRNA.
DR EMBL; AF364049; AAK50857.1; -; mRNA.
DR EMBL; AK089424; BAC40876.1; -; mRNA.
DR EMBL; AK150234; BAE29399.1; -; mRNA.
DR EMBL; AK170681; BAE41954.1; -; mRNA.
DR EMBL; BC004829; AAH04829.1; -; mRNA.
DR CCDS; CCDS25691.1; -.
DR RefSeq; NP_033330.1; NM_009304.2.
DR AlphaFoldDB; O55101; -.
DR STRING; 10090.ENSMUSP00000026649; -.
DR PhosphoSitePlus; O55101; -.
DR MaxQB; O55101; -.
DR PaxDb; O55101; -.
DR PRIDE; O55101; -.
DR ProteomicsDB; 261091; -.
DR Antibodypedia; 32546; 260 antibodies from 31 providers.
DR DNASU; 20973; -.
DR Ensembl; ENSMUST00000026649; ENSMUSP00000026649; ENSMUSG00000048277.
DR GeneID; 20973; -.
DR KEGG; mmu:20973; -.
DR UCSC; uc007mnx.2; mouse.
DR CTD; 9144; -.
DR MGI; MGI:1328324; Syngr2.
DR VEuPathDB; HostDB:ENSMUSG00000048277; -.
DR eggNOG; KOG4016; Eukaryota.
DR GeneTree; ENSGT00950000182935; -.
DR InParanoid; O55101; -.
DR OMA; NQWAATR; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; O55101; -.
DR TreeFam; TF320995; -.
DR BioGRID-ORCS; 20973; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Syngr2; mouse.
DR PRO; PR:O55101; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O55101; protein.
DR Bgee; ENSMUSG00000048277; Expressed in peripheral lymph node and 249 other tissues.
DR ExpressionAtlas; O55101; baseline and differential.
DR Genevisible; O55101; MM.
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; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISO:MGI.
DR GO; GO:0045055; P:regulated exocytosis; ISS: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 2: Evidence at transcript 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_0000183994"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
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 VARIANT 215
FT /note="T -> I"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 69
FT /note="R -> H (in Ref. 4; BAC40876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24778 MW; 951FE014C9C3EEB6 CRC64;
MESGAYGAAN AGGSFDLRRF LSQPQVVTRL VSMVLALIVF SCIFGEGYTN IHTSDQLYCV
FNQNEDACRY GSAIGVLAFL ASAFFLVVDA FFSQISNATD RKYLVIGDLL FSALWTFLWF
VGFCFLTNQW AATKPQDVRV GADSARAAIT FSFFSIFSWG VLASLAYQRY KAGVDAFIQN
YVDPTPDPNT AYASYPSASV ENYQQPPFTQ NVETTEGYQP PPVY
