SYPH_MOUSE
ID SYPH_MOUSE Reviewed; 314 AA.
AC Q62277; Q8BRQ0; Q91WI8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Synaptophysin;
DE AltName: Full=BM89 antigen;
DE AltName: Full=Major synaptic vesicle protein p38;
GN Name=Syp;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-314.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9210520;
RX DOI=10.1002/(sici)1097-4547(19970615)48:6<507::aid-jnr3>3.0.co;2-e;
RA Gaitanou M., Mamalaki A., Merkouri E., Matsas R.;
RT "Purification and cDNA cloning of mouse BM89 antigen shows that it is
RT identical with the synaptic vesicle protein synaptophysin.";
RL J. Neurosci. Res. 48:507-514(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-314.
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 77-89; 170-179 AND 226-235, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, 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 [7]
RP INTERACTION WITH VAMP2.
RX PubMed=19196426; DOI=10.1111/j.1471-4159.2008.05849.x;
RA Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I.,
RA Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.;
RT "Sept8 controls the binding of vesicle-associated membrane protein 2 to
RT synaptophysin.";
RL J. Neurochem. 108:867-880(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, AND IDENTIFICATION BY
RP 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).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=24995978; DOI=10.1016/j.cell.2014.06.007;
RA Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.;
RT "Glucose regulates mitochondrial motility via Milton modification by O-
RT GlcNAc transferase.";
RL Cell 158:54-68(2014).
CC -!- FUNCTION: Possibly involved in structural functions as organizing other
CC membrane components or in targeting the vesicles to the plasma membrane
CC (By similarity). Involved in the regulation of short-term and long-term
CC synaptic plasticity. {ECO:0000250, ECO:0000269|PubMed:10595519}.
CC -!- SUBUNIT: Homohexamer or homotetramer. Interacts with SRCIN1 (By
CC similarity). Interacts with VAMP2; the interaction is inhibit by
CC interaction of VAPM2 with SEPT8 (PubMed:19196426).
CC {ECO:0000250|UniProtKB:P08247, ECO:0000269|PubMed:19196426}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:24995978}; Multi-pass membrane
CC protein {ECO:0000255}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P08247}.
CC -!- DOMAIN: The calcium-binding activity is thought to be localized in the
CC cytoplasmic tail of the protein.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000250}.
CC -!- PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:P07825}.
CC -!- DISRUPTION PHENOTYPE: Mice lackin both SYNGR1 and SYP show normal brain
CC structure and composition, but impaired short-term and long-term
CC synaptic plasticity. {ECO:0000269|PubMed:10595519}.
CC -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.
CC {ECO:0000305}.
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DR EMBL; AK043756; BAC31642.1; -; mRNA.
DR EMBL; X95818; CAA65084.1; -; mRNA.
DR EMBL; BC014823; AAH14823.1; -; mRNA.
DR CCDS; CCDS29967.2; -.
DR RefSeq; NP_033331.2; NM_009305.2.
DR AlphaFoldDB; Q62277; -.
DR BioGRID; 203609; 33.
DR IntAct; Q62277; 18.
DR MINT; Q62277; -.
DR STRING; 10090.ENSMUSP00000069429; -.
DR GlyGen; Q62277; 1 site.
DR iPTMnet; Q62277; -.
DR PhosphoSitePlus; Q62277; -.
DR MaxQB; Q62277; -.
DR PaxDb; Q62277; -.
DR PeptideAtlas; Q62277; -.
DR PRIDE; Q62277; -.
DR ProteomicsDB; 253441; -.
DR Antibodypedia; 501; 1336 antibodies from 53 providers.
DR DNASU; 20977; -.
DR Ensembl; ENSMUST00000069520; ENSMUSP00000069429; ENSMUSG00000031144.
DR GeneID; 20977; -.
DR KEGG; mmu:20977; -.
DR UCSC; uc009slr.2; mouse.
DR CTD; 6855; -.
DR MGI; MGI:98467; Syp.
DR VEuPathDB; HostDB:ENSMUSG00000031144; -.
DR eggNOG; ENOG502QT4W; Eukaryota.
DR GeneTree; ENSGT01030000234637; -.
DR HOGENOM; CLU_064642_0_0_1; -.
DR InParanoid; Q62277; -.
DR OMA; APTCRGD; -.
DR OrthoDB; 1446480at2759; -.
DR PhylomeDB; Q62277; -.
DR TreeFam; TF315804; -.
DR BioGRID-ORCS; 20977; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Syp; mouse.
DR PRO; PR:Q62277; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q62277; protein.
DR Bgee; ENSMUSG00000031144; Expressed in retinal neural layer and 178 other tissues.
DR ExpressionAtlas; Q62277; baseline and differential.
DR Genevisible; Q62277; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
DR GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR GO; GO:0044309; C:neuron spine; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IDA:BHF-UCL.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:MGI.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:SynGO.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR001285; Synaptophysin/porin.
DR InterPro; IPR028714; SYP.
DR PANTHER; PTHR10306; PTHR10306; 1.
DR PANTHER; PTHR10306:SF10; PTHR10306:SF10; 1.
DR Pfam; PF01284; MARVEL; 1.
DR PRINTS; PR00220; SYNAPTOPHYSN.
DR PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS00604; SYNAPTOP; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..314
FT /note="Synaptophysin"
FT /id="PRO_0000179162"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..107
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..200
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..228
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 239..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..305
FT /note="Repeats, Gly-rich"
FT COMPBIAS 297..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 279
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 296
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 105
FT /note="A -> G (in Ref. 2; CAA65084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34025 MW; F6AC6E30AECE10CE CRC64;
MLLLADMDVV NQLVAGGQFR VVKEPLGFVK VLQWVFAIFA FATCGSYTGE LRLSVECANK
TESALNIEVE FEYPFRLHQV YFDAPSCVKG GTTKIFLVGD YSSSAEFFVT VAVFAFLYSM
GALATYIFLQ NKYRENNKGP MMDFLATAVF AFMWLVSSSA WAKGLSDVKM ATDPENIIKE
MPMCRQTGNT CKELRDPVTS GLNTSVVFGF LNLVLWVGNL WFVFKETGWA APFMRAPPGA
PEKQPAPGDA YGDAGYGQGP GGYGPQDSYG PQGGYQPDYG QPASGGGGGY GPQGDYGQQG
YGQQGAPTSF SNQM
