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Synaptic vesicle glycoprotein 2A (Synaptic vesicle protein 2) (Synaptic vesicle protein 2A) (Calcium regulator SV2A)

 SV2A_MOUSE              Reviewed;         742 AA.
Q9JIS5; Q80TT0; Q8R0R5;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-JUL-2017, entry version 138.
RecName: Full=Synaptic vesicle glycoprotein 2A;
Short=Synaptic vesicle protein 2;
Short=Synaptic vesicle protein 2A;
AltName: Full=Calcium regulator SV2A;
Name=Sv2a; Synonyms=Kiaa0736, Sv2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=129/Sv;
PubMed=10624962; DOI=10.1016/S0896-6273(00)81046-6;
Janz R., Goda Y., Geppert M., Missler M., Suedhof T.C.;
"SV2A and SV2B function as redundant Ca2+ regulators in
neurotransmitter release.";
Neuron 24:1003-1016(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[3]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10611374; DOI=10.1073/pnas.96.26.15268;
Crowder K.M., Gunther J.M., Jones T.A., Hale B.D., Zhang H.Z.,
Peterson M.R., Scheller R.H., Chavkin C., Bajjalieh S.M.;
"Abnormal neurotransmission in mice lacking synaptic vesicle protein
2A (SV2A).";
Proc. Natl. Acad. Sci. U.S.A. 96:15268-15273(1999).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11483953; DOI=10.1038/35087000;
Xu T., Bajjalieh S.M.;
"SV2 modulates the size of the readily releasable pool of secretory
vesicles.";
Nat. Cell Biol. 3:691-698(2001).
[8]
SUBCELLULAR LOCATION.
PubMed=12209837; DOI=10.1002/cne.10281;
Krizaj D., Demarco S.J., Johnson J., Strehler E.E., Copenhagen D.R.;
"Cell-specific expression of plasma membrane calcium ATPase isoforms
in retinal neurons.";
J. Comp. Neurol. 451:1-21(2002).
[9]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12687700; DOI=10.1002/cne.10636;
Wang M.M., Janz R., Belizaire R., Frishman L.J., Sherry D.M.;
"Differential distribution and developmental expression of synaptic
vesicle protein 2 isoforms in the mouse retina.";
J. Comp. Neurol. 460:106-122(2003).
[10]
FUNCTION.
PubMed=16436618; DOI=10.1523/JNEUROSCI.2699-05.2006;
Custer K.L., Austin N.S., Sullivan J.M., Bajjalieh S.M.;
"Synaptic vesicle protein 2 enhances release probability at quiescent
synapses.";
J. Neurosci. 26:1303-1313(2006).
[11]
FUNCTION AS A BOTA RECEPTOR, AND DISRUPTION PHENOTYPE.
PubMed=16543415; DOI=10.1126/science.1123654;
Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R.,
Chapman E.R.;
"SV2 is the protein receptor for botulinum neurotoxin A.";
Science 312:592-596(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-81; THR-84 AND
SER-127, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays a role in the control of regulated secretion in
neural and endocrine cells, enhancing selectively low-frequency
neurotransmission. Positively regulates vesicle fusion by
maintaining the readily releasable pool of secretory vesicles.
-!- FUNCTION: Receptor for the botulinium neurotoxin type A/BOTA.
-!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-
dependent manner. Binds the adapter protein complex AP-2 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse
{ECO:0000269|PubMed:12209837}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q02563};
Multi-pass membrane protein {ECO:0000250|UniProtKB:Q02563}.
Note=Enriched in chromaffin granules, not present in adrenal
microsomes. Associated with both insulin granules and synaptic-
like microvesicles in insulin-secreting cells of the pancreas (By
similarity). Colocalizes with ATP2B1 at photoreceptor synaptic
terminals. {ECO:0000250|UniProtKB:Q02563,
ECO:0000269|PubMed:12209837}.
-!- TISSUE SPECIFICITY: Expressed in conventional synapses and cone
ribbon synapses in the retina (at protein level).
{ECO:0000269|PubMed:12687700}.
-!- DEVELOPMENTAL STAGE: Expressed during synaptogenesis in the retina
(at protein level). {ECO:0000269|PubMed:12687700}.
-!- PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain
regulates interaction with SYT1. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice fail to grow, experience severe
epileptic seizures and die immediately or shortly after birth
probably due to multiple neural and endocrine deficits. Mice
lacking both Sv2a and Sv2b display a similar phenotype.
{ECO:0000269|PubMed:10611374, ECO:0000269|PubMed:11483953,
ECO:0000269|PubMed:16543415}.
-!- SIMILARITY: Belongs to the major facilitator superfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC65642.3; Type=Frameshift; Positions=72; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF196781; AAF87321.1; -; Genomic_DNA.
EMBL; AF196780; AAF87321.1; JOINED; Genomic_DNA.
EMBL; AK122360; BAC65642.3; ALT_SEQ; Transcribed_RNA.
EMBL; AK028318; BAC25876.1; -; mRNA.
EMBL; BC026494; AAH26494.1; -; mRNA.
EMBL; BC046587; AAH46587.1; -; mRNA.
CCDS; CCDS17631.1; -.
RefSeq; NP_071313.1; NM_022030.3.
UniGene; Mm.491135; -.
ProteinModelPortal; Q9JIS5; -.
SMR; Q9JIS5; -.
BioGrid; 211019; 1.
IntAct; Q9JIS5; 5.
MINT; MINT-4129805; -.
STRING; 10090.ENSMUSP00000037576; -.
iPTMnet; Q9JIS5; -.
PhosphoSitePlus; Q9JIS5; -.
SwissPalm; Q9JIS5; -.
MaxQB; Q9JIS5; -.
PaxDb; Q9JIS5; -.
PeptideAtlas; Q9JIS5; -.
PRIDE; Q9JIS5; -.
Ensembl; ENSMUST00000035371; ENSMUSP00000037576; ENSMUSG00000038486.
GeneID; 64051; -.
KEGG; mmu:64051; -.
UCSC; uc008qmf.1; mouse.
CTD; 9900; -.
MGI; MGI:1927139; Sv2a.
eggNOG; ENOG410IRID; Eukaryota.
eggNOG; ENOG410YQME; LUCA.
GeneTree; ENSGT00550000074384; -.
HOGENOM; HOG000065727; -.
HOVERGEN; HBG053967; -.
InParanoid; Q9JIS5; -.
KO; K06258; -.
OMA; MMMAVWF; -.
OrthoDB; EOG091G02NC; -.
PhylomeDB; Q9JIS5; -.
TreeFam; TF324824; -.
PRO; PR:Q9JIS5; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000038486; -.
CleanEx; MM_SV2A; -.
Genevisible; Q9JIS5; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0048786; C:presynaptic active zone; IDA:BHF-UCL.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004872; F:receptor activity; IDA:MGI.
GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
GO; GO:0007268; P:chemical synaptic transmission; TAS:MGI.
GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
GO; GO:0014052; P:regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
CDD; cd06174; MFS; 2.
InterPro; IPR001646; 5peptide_repeat.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005828; MFS_sugar_transport-like.
InterPro; IPR005829; Sugar_transporter_CS.
InterPro; IPR022308; SV2.
Pfam; PF07690; MFS_1; 1.
Pfam; PF13599; Pentapeptide_4; 1.
Pfam; PF00083; Sugar_tr; 1.
SUPFAM; SSF103473; SSF103473; 3.
TIGRFAMs; TIGR01299; synapt_SV2; 1.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Cell junction; Complete proteome; Cytoplasmic vesicle; Glycoprotein;
Membrane; Neurotransmitter transport; Phosphoprotein; Receptor;
Reference proteome; Synapse; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 742 Synaptic vesicle glycoprotein 2A.
/FTId=PRO_0000239766.
TOPO_DOM 1 169 Cytoplasmic. {ECO:0000255}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TOPO_DOM 191 205 Extracellular. {ECO:0000255}.
TRANSMEM 206 226 Helical. {ECO:0000255}.
TOPO_DOM 227 233 Cytoplasmic. {ECO:0000255}.
TRANSMEM 234 254 Helical. {ECO:0000255}.
TOPO_DOM 255 262 Extracellular. {ECO:0000255}.
TRANSMEM 263 283 Helical. {ECO:0000255}.
TOPO_DOM 284 294 Cytoplasmic. {ECO:0000255}.
TRANSMEM 295 315 Helical. {ECO:0000255}.
TOPO_DOM 316 334 Extracellular. {ECO:0000255}.
TRANSMEM 335 355 Helical. {ECO:0000255}.
TOPO_DOM 356 447 Cytoplasmic. {ECO:0000255}.
TRANSMEM 448 468 Helical. {ECO:0000255}.
TOPO_DOM 469 598 Extracellular. {ECO:0000255}.
TRANSMEM 599 619 Helical. {ECO:0000255}.
TOPO_DOM 620 626 Cytoplasmic. {ECO:0000255}.
TRANSMEM 627 647 Helical. {ECO:0000255}.
TOPO_DOM 648 651 Extracellular. {ECO:0000255}.
TRANSMEM 652 672 Helical. {ECO:0000255}.
TOPO_DOM 673 685 Cytoplasmic. {ECO:0000255}.
TRANSMEM 686 708 Helical. {ECO:0000255}.
TOPO_DOM 709 712 Extracellular. {ECO:0000255}.
TRANSMEM 713 731 Helical. {ECO:0000255}.
TOPO_DOM 732 742 Cytoplasmic. {ECO:0000255}.
REGION 1 57 Interaction with SYT1. {ECO:0000250}.
REGION 543 580 BOTA-binding. {ECO:0000250}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 84 84 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000250|UniProtKB:Q02563}.
MOD_RES 480 480 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 742 AA; 82647 MW; 1074857FD13ED894 CRC64;
MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE EEDDDDDFPA
PADGYYRGEG AQDEEEGGAS SDATEGHDED DEIYEGEYQG IPRAESGGKG ERMADGAPLA
GVRGGLSDGE GPPGGRGEAQ RRKDREELAQ QYETILRECG HGRFQWTLYF VLGLALMADG
VEVFVVGFVL PSAEKDMCLS DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS
VNSVFAFFSS FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW
MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA LTTQPESPRF
FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI HQEDELIEIQ SDTGTWYQRW
GVRALSLGGQ VWGNFLSCFS PEYRRITLMM MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY
AARTKVFPGE RVEHVTFNFT LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT
SSNTFFRNCT FINTVFYNTD LFEYKFVNSR LVNSTFLHNK EGCPLDVTGT GEGAYMVYFV
SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVLSCVSCF FLSFGNSESA MIALLCLFGG
VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG ISIFTSFVGI TKAAPILFAS
AALALGSSLA LKLPETRGQV LQ


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