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   27-MAR-2024, entry version 175.
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>3.3.co;2-2;
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; 38.
DR   IntAct; Q62277; 18.
DR   MINT; Q62277; -.
DR   STRING; 10090.ENSMUSP00000069429; -.
DR   GlyCosmos; Q62277; 1 site, No reported glycans.
DR   GlyGen; Q62277; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q62277; -.
DR   PhosphoSitePlus; Q62277; -.
DR   SwissPalm; Q62277; -.
DR   MaxQB; Q62277; -.
DR   PaxDb; 10090-ENSMUSP00000069429; -.
DR   PeptideAtlas; Q62277; -.
DR   ProteomicsDB; 253441; -.
DR   Antibodypedia; 501; 1545 antibodies from 53 providers.
DR   DNASU; 20977; -.
DR   Ensembl; ENSMUST00000069520.11; ENSMUSP00000069429.5; ENSMUSG00000031144.16.
DR   GeneID; 20977; -.
DR   KEGG; mmu:20977; -.
DR   UCSC; uc009slr.2; mouse.
DR   AGR; MGI:98467; -.
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; FIWKEVV; -.
DR   OrthoDB; 2881347at2759; -.
DR   PhylomeDB; Q62277; -.
DR   TreeFam; TF315804; -.
DR   BioGRID-ORCS; 20977; 1 hit in 79 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 181 other cell types or tissues.
DR   ExpressionAtlas; Q62277; baseline and differential.
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: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:0098793; C:presynapse; IDA: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   PANTHER; PTHR10306; SYNAPTOPHYSIN; 1.
DR   PANTHER; PTHR10306:SF10; SYNAPTOPHYSIN; 1.
DR   Pfam; PF01284; MARVEL; 1.
DR   PRINTS; PR00220; SYNAPTOPHYSN.
DR   PROSITE; PS51225; MARVEL; 1.
DR   PROSITE; PS00604; SYNAPTOP; 1.
DR   Genevisible; Q62277; MM.
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
//