SV2A_MOUSE
ID SV2A_MOUSE Reviewed; 742 AA.
AC Q9JIS5; Q80TT0; Q8R0R5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Synaptic vesicle glycoprotein 2A;
DE Short=Synaptic vesicle protein 2;
DE Short=Synaptic vesicle protein 2A;
DE AltName: Full=Calcium regulator SV2A;
GN Name=Sv2a; Synonyms=Kiaa0736, Sv2;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=129/Sv;
RX PubMed=10624962; DOI=10.1016/s0896-6273(00)81046-6;
RA Janz R., Goda Y., Geppert M., Missler M., Suedhof T.C.;
RT "SV2A and SV2B function as redundant Ca2+ regulators in neurotransmitter
RT release.";
RL Neuron 24:1003-1016(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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].
RC STRAIN=C57BL/6J; 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10611374; DOI=10.1073/pnas.96.26.15268;
RA Crowder K.M., Gunther J.M., Jones T.A., Hale B.D., Zhang H.Z.,
RA Peterson M.R., Scheller R.H., Chavkin C., Bajjalieh S.M.;
RT "Abnormal neurotransmission in mice lacking synaptic vesicle protein 2A
RT (SV2A).";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15268-15273(1999).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11483953; DOI=10.1038/35087000;
RA Xu T., Bajjalieh S.M.;
RT "SV2 modulates the size of the readily releasable pool of secretory
RT vesicles.";
RL Nat. Cell Biol. 3:691-698(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12209837; DOI=10.1002/cne.10281;
RA Krizaj D., Demarco S.J., Johnson J., Strehler E.E., Copenhagen D.R.;
RT "Cell-specific expression of plasma membrane calcium ATPase isoforms in
RT retinal neurons.";
RL J. Comp. Neurol. 451:1-21(2002).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12687700; DOI=10.1002/cne.10636;
RA Wang M.M., Janz R., Belizaire R., Frishman L.J., Sherry D.M.;
RT "Differential distribution and developmental expression of synaptic vesicle
RT protein 2 isoforms in the mouse retina.";
RL J. Comp. Neurol. 460:106-122(2003).
RN [10]
RP FUNCTION.
RX PubMed=16436618; DOI=10.1523/jneurosci.2699-05.2006;
RA Custer K.L., Austin N.S., Sullivan J.M., Bajjalieh S.M.;
RT "Synaptic vesicle protein 2 enhances release probability at quiescent
RT synapses.";
RL J. Neurosci. 26:1303-1313(2006).
RN [11]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A RECEPTOR (MICROBIAL INFECTION),
RP SUBUNIT (MICROBIAL INFECTION), TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16543415; DOI=10.1126/science.1123654;
RA Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R., Chapman E.R.;
RT "SV2 is the protein receptor for botulinum neurotoxin A.";
RL Science 312:592-596(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [13]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE E RECEPTOR (MICROBIAL INFECTION),
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18815274; DOI=10.1091/mbc.e08-07-0765;
RA Dong M., Liu H., Tepp W.H., Johnson E.A., Janz R., Chapman E.R.;
RT "Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E
RT into neurons.";
RL Mol. Biol. Cell 19:5226-5237(2008).
RN [14]
RP POSSIBLE FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE D RECEPTOR (MICROBIAL
RP INFECTION), AND DISRUPTION PHENOTYPE.
RX PubMed=21483489; DOI=10.1371/journal.ppat.1002008;
RA Peng L., Tepp W.H., Johnson E.A., Dong M.;
RT "Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides
RT as receptors.";
RL PLoS Pathog. 7:E1002008-E1002008(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-81; THR-84 AND
RP SER-127, AND 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: Plays a role in the control of regulated secretion in neural
CC and endocrine cells, enhancing selectively low-frequency
CC neurotransmission. Positively regulates vesicle fusion by maintaining
CC the readily releasable pool of secretory vesicles.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type A (BoNT/A, botA); the toxin probably binds via extracellular loop
CC 4 (PubMed:16543415). {ECO:0000269|PubMed:16543415}.
CC -!- FUNCTION: (Microbial infection) Possible receptor for C.botulinum
CC neurotoxin type D (BoNT/D, botD); BoNT/D does not bind to extracellular
CC loop 4 as do BoNT/A and BoNT/E (PubMed:21483489).
CC {ECO:0000269|PubMed:21483489}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type E (BoNT/E); the toxin probably binds via extracellular loop 4
CC (PubMed:18815274). It probably requires glycosylation of Asn-573
CC (PubMed:18815274). {ECO:0000269|PubMed:18815274,
CC ECO:0000305|PubMed:18815274}.
CC -!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-dependent
CC manner. Binds the adapter protein complex AP-2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type A (BoNT/A, botA). {ECO:0000269|PubMed:18815274,
CC ECO:0000305|PubMed:16543415}.
CC -!- SUBCELLULAR LOCATION: Presynapse {ECO:0000269|PubMed:12209837}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules,
CC not present in adrenal microsomes. Associated with both insulin
CC granules and synaptic-like microvesicles in insulin-secreting cells of
CC the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor
CC synaptic terminals. {ECO:0000250|UniProtKB:Q02563,
CC ECO:0000269|PubMed:12209837}.
CC -!- TISSUE SPECIFICITY: Expressed in conventional synapses and cone ribbon
CC synapses in the retina (at protein level) (PubMed:12687700). Expressed
CC in diaphragm motor nerve terminals (at protein level)
CC (PubMed:16543415). Expressed in hippocampus neurons (at protein level)
CC (PubMed:18815274). {ECO:0000269|PubMed:12687700,
CC ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:18815274}.
CC -!- DEVELOPMENTAL STAGE: Expressed during synaptogenesis in the retina (at
CC protein level). {ECO:0000269|PubMed:12687700}.
CC -!- PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain
CC regulates interaction with SYT1. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:18815274}.
CC -!- DISRUPTION PHENOTYPE: Mice fail to grow, experience severe epileptic
CC seizures and die immediately or shortly after birth probably due to
CC multiple neural and endocrine deficits (PubMed:10624962). Mice lacking
CC both Sv2a and Sv2b display a similar phenotype (PubMed:10624962).
CC Diaphragm motor nerve terminals from mice with only a single copy of
CC this gene and no Sv2b have decreased binding of C.botulinum neurotoxin
CC type A (BoNT/A, botA) and are less sensitive to the toxin
CC (PubMed:16543415). Hippocampal neurons from young mice lacking both
CC Sv2a and Sv2b do not bind BoNT/A, nor do they take it up
CC (PubMed:16543415, PubMed:18815274). Hippocampal neurons from young mice
CC lacking both Sv2a and Sv2b do not bind C.botulinum neurotoxin type E
CC (BoNT/E), nor do they take it up (PubMed:18815274). Hippocampal neurons
CC from young mice lacking both Sv2a and Sv2b do not bind C.botulinum
CC neurotoxin type BoNT/D (BoNT/D, botD), nor do they take it up
CC (PubMed:21483489). Hippocampal neurons from young mice lacking both
CC Sv2a and Sv2b take up C.botulinum neurotoxin type C (BoNT/C) and
CC C.botulinum neurotoxin type F (BonT/F, botF) normally
CC (PubMed:21483489). {ECO:0000269|PubMed:10611374,
CC ECO:0000269|PubMed:10624962, ECO:0000269|PubMed:11483953,
CC ECO:0000269|PubMed:16543415, ECO:0000269|PubMed:18815274,
CC ECO:0000269|PubMed:21483489}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65642.3; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF196781; AAF87321.1; -; Genomic_DNA.
DR EMBL; AF196780; AAF87321.1; JOINED; Genomic_DNA.
DR EMBL; AK122360; BAC65642.3; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK028318; BAC25876.1; -; mRNA.
DR EMBL; BC026494; AAH26494.1; -; mRNA.
DR EMBL; BC046587; AAH46587.1; -; mRNA.
DR CCDS; CCDS17631.1; -.
DR RefSeq; NP_071313.1; NM_022030.3.
DR AlphaFoldDB; Q9JIS5; -.
DR BioGRID; 211019; 4.
DR IntAct; Q9JIS5; 6.
DR MINT; Q9JIS5; -.
DR STRING; 10090.ENSMUSP00000037576; -.
DR GlyConnect; 2746; 8 N-Linked glycans (2 sites).
DR GlyGen; Q9JIS5; 3 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; Q9JIS5; -.
DR PhosphoSitePlus; Q9JIS5; -.
DR SwissPalm; Q9JIS5; -.
DR MaxQB; Q9JIS5; -.
DR PaxDb; Q9JIS5; -.
DR PeptideAtlas; Q9JIS5; -.
DR PRIDE; Q9JIS5; -.
DR ProteomicsDB; 258675; -.
DR Antibodypedia; 2184; 185 antibodies from 35 providers.
DR DNASU; 64051; -.
DR Ensembl; ENSMUST00000035371; ENSMUSP00000037576; ENSMUSG00000038486.
DR GeneID; 64051; -.
DR KEGG; mmu:64051; -.
DR UCSC; uc008qmf.1; mouse.
DR CTD; 9900; -.
DR MGI; MGI:1927139; Sv2a.
DR VEuPathDB; HostDB:ENSMUSG00000038486; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00950000182940; -.
DR HOGENOM; CLU_001265_46_15_1; -.
DR InParanoid; Q9JIS5; -.
DR OMA; FNDKSMV; -.
DR OrthoDB; 724235at2759; -.
DR PhylomeDB; Q9JIS5; -.
DR TreeFam; TF324824; -.
DR BioGRID-ORCS; 64051; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Sv2a; mouse.
DR PRO; PR:Q9JIS5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JIS5; protein.
DR Bgee; ENSMUSG00000038486; Expressed in lateral geniculate body and 176 other tissues.
DR Genevisible; Q9JIS5; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:MGI.
DR GO; GO:0014052; P:regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR InterPro; IPR022308; SV2.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR01299; synapt_SV2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Receptor; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..742
FT /note="Synaptic vesicle glycoprotein 2A"
FT /id="PRO_0000239766"
FT TOPO_DOM 1..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..598
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16543415"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Interaction with SYT1"
FT /evidence="ECO:0000250"
FT REGION 40..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02563"
FT MOD_RES 480
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
