SNG3_MOUSE
ID SNG3_MOUSE Reviewed; 229 AA.
AC Q8R191; Q9WVG8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Synaptogyrin-3 {ECO:0000305};
GN Name=Syngr3 {ECO:0000312|MGI:MGI:1341881};
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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].
RC TISSUE=Eye;
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; 92-99 AND 133-147, 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 SUBCELLULAR LOCATION.
RX PubMed=14755516; DOI=10.1002/cne.20008;
RA Belizaire R., Komanduri C., Wooten K., Chen M., Thaller C., Janz R.;
RT "Characterization of synaptogyrin 3 as a new synaptic vesicle protein.";
RL J. Comp. Neurol. 470:266-281(2004).
RN [6]
RP FUNCTION, INTERACTION WITH SLC6A3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19357284; DOI=10.1523/jneurosci.4559-08.2009;
RA Egana L.A., Cuevas R.A., Baust T.B., Parra L.A., Leak R.K., Hochendoner S.,
RA Pena K., Quiroz M., Hong W.C., Dorostkar M.M., Janz R., Sitte H.H.,
RA Torres G.E.;
RT "Physical and functional interaction between the dopamine transporter and
RT the synaptic vesicle protein synaptogyrin-3.";
RL J. Neurosci. 29:4592-4604(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 (PubMed:10383386).
CC May indirectly regulate the activity of the plasma membrane dopamine
CC transporter SLC6A3 and thereby regulate dopamine transport back from
CC the synaptic cleft into the presynaptic terminal (PubMed:19357284).
CC {ECO:0000269|PubMed:10383386, ECO:0000269|PubMed:19357284}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SLC6A3 (via N-terminus)
CC (PubMed:19357284). May interact with VMAT2 (PubMed:19357284).
CC {ECO:0000269|PubMed:19357284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:14755516,
CC ECO:0000269|PubMed:19357284}; Multi-pass membrane protein
CC {ECO:0000255}. Synapse {ECO:0000269|PubMed:14755516}. Note=Found at the
CC neuromuscular synapses. {ECO:0000269|PubMed:14755516}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain. Found in the brain
CC across the dorsal and ventral corpus striatum as well as in the cortex.
CC {ECO:0000269|PubMed:10383386, ECO:0000269|PubMed:19357284}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during brain development from
CC P2 to adult (at protein level). {ECO:0000269|PubMed:10383386}.
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
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DR EMBL; AF117207; AAD28556.1; -; mRNA.
DR EMBL; AK048753; BAC33444.1; -; mRNA.
DR EMBL; AK081164; BAC38151.1; -; mRNA.
DR EMBL; AK082167; BAC38430.1; -; mRNA.
DR EMBL; BC025022; AAH25022.1; -; mRNA.
DR CCDS; CCDS28491.1; -.
DR RefSeq; NP_035652.2; NM_011522.3.
DR AlphaFoldDB; Q8R191; -.
DR BioGRID; 203607; 3.
DR IntAct; Q8R191; 1.
DR STRING; 10090.ENSMUSP00000007236; -.
DR iPTMnet; Q8R191; -.
DR PhosphoSitePlus; Q8R191; -.
DR MaxQB; Q8R191; -.
DR PaxDb; Q8R191; -.
DR PeptideAtlas; Q8R191; -.
DR PRIDE; Q8R191; -.
DR ProteomicsDB; 261290; -.
DR DNASU; 20974; -.
DR Ensembl; ENSMUST00000007236; ENSMUSP00000007236; ENSMUSG00000007021.
DR GeneID; 20974; -.
DR KEGG; mmu:20974; -.
DR UCSC; uc008axq.1; mouse.
DR CTD; 9143; -.
DR MGI; MGI:1341881; Syngr3.
DR VEuPathDB; HostDB:ENSMUSG00000007021; -.
DR eggNOG; KOG4016; Eukaryota.
DR GeneTree; ENSGT00950000182935; -.
DR HOGENOM; CLU_079186_0_1_1; -.
DR InParanoid; Q8R191; -.
DR OMA; ACRFGVV; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; Q8R191; -.
DR TreeFam; TF320995; -.
DR BioGRID-ORCS; 20974; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Syngr3; mouse.
DR PRO; PR:Q8R191; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R191; protein.
DR Bgee; ENSMUSG00000007021; Expressed in primary visual cortex and 152 other tissues.
DR Genevisible; Q8R191; 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:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
DR GO; GO:0001504; P:neurotransmitter uptake; ISO:MGI.
DR GO; GO:0032411; P:positive regulation of transporter activity; IMP:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; 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; Direct protein sequencing; Membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..229
FT /note="Synaptogyrin-3"
FT /id="PRO_0000183997"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 20..172
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 209..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43761"
FT CONFLICT 171
FT /note="F -> L (in Ref. 1; AAD28556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 24561 MW; E04C00555B8A3C08 CRC64;
MEGASFGAGR AGAAFDPVSF ARRPQTLLRV VSWVFSIAVF GPIVNEGYVN SDSGPELRCV
FNGNAGACRF GVVLGLGAFI ACVAFLLLDV RFQQISSVRD RRRAVLLDLG FSGVWSFLWF
VGFCFLTNQW QRTTPGPGTA QAGDAARAAI AFSFFSILSW VALTVKALQR FRLGTDMSLF
ATDQLGTGAA QAYPGYPVGS GVEGTETYQS PPFTETLDTS SKGYQVPAY
