ID SYPH_HUMAN Reviewed; 313 AA. AC P08247; B2R7L6; B7Z359; Q6P2F7; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 3. DT 27-MAR-2024, entry version 201. DE RecName: Full=Synaptophysin; DE AltName: Full=Major synaptic vesicle protein p38; GN Name=SYP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3120152; DOI=10.1093/nar/15.22.9607; RA Suedhof T.C., Lottspeich F., Greengard P., Mehl E., Jahn R.; RT "The cDNA and derived amino acid sequences for rat and human RT synaptophysin."; RL Nucleic Acids Res. 15:9607-9607(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1975480; RA Oezcelik T., Lafreniere R.G., Archer B.T. III, Johnston P.A., Willard H.F., RA Francke U., Suedhof T.C.; RT "Synaptophysin: structure of the human gene and assignment to the X RT chromosome in man and mouse."; RL Am. J. Hum. Genet. 47:551-561(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9344658; DOI=10.1006/geno.1997.4941; RA Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S., D'Urso M., RA Craig I.W.; RT "Sequence-based exon prediction around the synaptophysin locus reveals a RT gene-rich area containing novel genes in human proximal Xp."; RL Genomics 45:340-347(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [8] RP TISSUE SPECIFICITY. RX PubMed=8838578; DOI=10.1002/jnr.490430111; RA Harigaya Y., Shoji M., Shirao T., Hirai S.; RT "Disappearance of actin-binding protein, drebrin, from hippocampal synapses RT in Alzheimer's disease."; RL J. Neurosci. Res. 43:87-92(1996). RN [9] RP TISSUE SPECIFICITY. RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019; RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R., RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T., RA Kinoshita M.; RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required RT for the suppression of alpha-synuclein neurotoxicity."; RL Neuron 53:519-533(2007). RN [10] RP INTERACTION WITH SRCIN1, AND SUBCELLULAR LOCATION. RX PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x; RA Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R., RA Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.; RT "Characterization of a multidomain adaptor protein, p140Cap, as part of a RT pre-synaptic complex."; RL J. Neurochem. 107:61-72(2008). RN [11] RP VARIANTS XLID96 ARG-217; GLU-277 AND SER-293, AND VARIANTS [LARGE SCALE RP ANALYSIS] GLN-2; LEU-158; ASN-166 AND ASN-248. RX PubMed=19377476; DOI=10.1038/ng.367; RA Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C., RA O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M., RA Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J., RA Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M., RA Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P., RA Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R., RA Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R., RA de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M., RA Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U., RA Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M., RA Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T., RA Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C., RA Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L., RA Futreal P.A., Stratton M.R.; RT "A systematic, large-scale resequencing screen of X-chromosome coding exons RT in mental retardation."; RL Nat. Genet. 41:535-543(2009). RN [12] RP VARIANT GLN-72. RX PubMed=28669405; DOI=10.1016/j.ajhg.2017.05.016; RG CAUSES Study; RG EPGEN Study; RA Lehman A., Thouta S., Mancini G.M.S., Naidu S., van Slegtenhorst M., RA McWalter K., Person R., Mwenifumbo J., Salvarinova R., Guella I., RA McKenzie M.B., Datta A., Connolly M.B., Kalkhoran S.M., Poburko D., RA Friedman J.M., Farrer M.J., Demos M., Desai S., Claydon T.; RT "Loss-of-function and gain-of-function mutations in KCNQ5 cause RT intellectual disability or epileptic encephalopathy."; RL Am. J. Hum. Genet. 101:65-74(2017). CC -!- FUNCTION: Possibly involved in structural functions as organizing other CC membrane components or in targeting the vesicles to the plasma CC membrane. Involved in the regulation of short-term and long-term CC synaptic plasticity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer or homotetramer. Interacts with SRCIN1 CC (PubMed:18662323). Interacts with VAMP2; the interaction is inhibit by CC interaction of VAPM2 with SEPT8 (By similarity). CC {ECO:0000250|UniProtKB:P07825, ECO:0000269|PubMed:18662323}. CC -!- INTERACTION: CC P08247; P05067: APP; NbExp=3; IntAct=EBI-9071725, EBI-77613; CC P08247; P53365: ARFIP2; NbExp=3; IntAct=EBI-9071725, EBI-638194; CC P08247; O75155: CAND2; NbExp=3; IntAct=EBI-9071725, EBI-5656182; CC P08247; O95971: CD160; NbExp=3; IntAct=EBI-9071725, EBI-4314390; CC P08247; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-9071725, EBI-517508; CC P08247; O95363: FARS2; NbExp=3; IntAct=EBI-9071725, EBI-2513774; CC P08247; P39905-3: GDNF; NbExp=3; IntAct=EBI-9071725, EBI-12702062; CC P08247; Q9UBD0: HSFX2; NbExp=3; IntAct=EBI-9071725, EBI-947253; CC P08247; P42858: HTT; NbExp=13; IntAct=EBI-9071725, EBI-466029; CC P08247; Q8TAC2: JOSD2; NbExp=3; IntAct=EBI-9071725, EBI-12205593; CC P08247; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9071725, EBI-21591415; CC P08247; Q9C0E8-2: LNPK; NbExp=3; IntAct=EBI-9071725, EBI-11024283; CC P08247; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-9071725, EBI-740987; CC P08247; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-9071725, EBI-11988931; CC P08247; Q6IN84: MRM1; NbExp=3; IntAct=EBI-9071725, EBI-5454865; CC P08247; Q96E11: MRRF; NbExp=3; IntAct=EBI-9071725, EBI-2855755; CC P08247; Q96E29: MTERF3; NbExp=3; IntAct=EBI-9071725, EBI-7825321; CC P08247; Q9HB07: MYG1; NbExp=3; IntAct=EBI-9071725, EBI-709754; CC P08247; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-9071725, EBI-11978907; CC P08247; Q96AL5: PBX3; NbExp=5; IntAct=EBI-9071725, EBI-741171; CC P08247; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-9071725, EBI-14223623; CC P08247; O60664: PLIN3; NbExp=3; IntAct=EBI-9071725, EBI-725795; CC P08247; Q96T60: PNKP; NbExp=3; IntAct=EBI-9071725, EBI-1045072; CC P08247; P30405: PPIF; NbExp=5; IntAct=EBI-9071725, EBI-5544229; CC P08247; O75127: PTCD1; NbExp=3; IntAct=EBI-9071725, EBI-2560233; CC P08247; P43378: PTPN9; NbExp=3; IntAct=EBI-9071725, EBI-742898; CC P08247; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-9071725, EBI-3232108; CC P08247; Q9Y371: SH3GLB1; NbExp=6; IntAct=EBI-9071725, EBI-2623095; CC P08247; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-9071725, EBI-2872322; CC P08247; Q13596: SNX1; NbExp=3; IntAct=EBI-9071725, EBI-2822329; CC P08247; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-9071725, EBI-742688; CC P08247; O60225-2: SSX5; NbExp=3; IntAct=EBI-9071725, EBI-12033476; CC P08247; Q96DR4: STARD4; NbExp=3; IntAct=EBI-9071725, EBI-17217258; CC P08247; Q8WY91: THAP4; NbExp=3; IntAct=EBI-9071725, EBI-726691; CC P08247; Q13885: TUBB2A; NbExp=3; IntAct=EBI-9071725, EBI-711595; CC P08247; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-9071725, EBI-12261790; CC P08247; Q96P53: WDFY2; NbExp=3; IntAct=EBI-9071725, EBI-9478589; CC P08247; Q9Y4P8-4: WIPI2; NbExp=3; IntAct=EBI-9071725, EBI-12205107; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic CC vesicle membrane {ECO:0000269|PubMed:18662323}; Multi-pass membrane CC protein {ECO:0000255}. Synapse, synaptosome CC {ECO:0000269|PubMed:18662323}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P08247-1; Sequence=Displayed; CC Name=2; CC IsoId=P08247-2; Sequence=VSP_056897; CC -!- TISSUE SPECIFICITY: Expressed in the brain, with expression in the CC hippocampus, the neuropil in the dentate gyrus, where expression is CC higher in the outer half of the molecular layer than in the inner half, CC and in the neuropil of CA4 and CA3 (PubMed:8838578). Expressed in the CC putamen (at protein level) (PubMed:17296554). CC {ECO:0000269|PubMed:17296554, ECO:0000269|PubMed:8838578}. 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 -!- DISEASE: Intellectual developmental disorder, X-linked 96 (XLID96) CC [MIM:300802]: A disorder characterized by significantly below average CC general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. CC {ECO:0000269|PubMed:19377476}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Synaptophysin entry; CC URL="https://en.wikipedia.org/wiki/Synaptophysin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X06389; CAA29686.1; -; mRNA. DR EMBL; U93305; AAB92358.1; -; Genomic_DNA. DR EMBL; AK295524; BAH12095.1; -; mRNA. DR EMBL; AK313030; BAG35863.1; -; mRNA. DR EMBL; AK315953; BAH14324.1; -; mRNA. DR EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471224; EAW50685.1; -; Genomic_DNA. DR EMBL; BC064550; AAH64550.1; -; mRNA. DR CCDS; CCDS14321.1; -. [P08247-1] DR PIR; A35699; A35699. DR RefSeq; NP_003170.1; NM_003179.2. [P08247-1] DR AlphaFoldDB; P08247; -. DR BioGRID; 112721; 133. DR IntAct; P08247; 67. DR STRING; 9606.ENSP00000263233; -. DR TCDB; 9.B.130.1.4; the tetraspan vesicle membrane protein (tvp) family. DR GlyCosmos; P08247; 1 site, No reported glycans. DR GlyGen; P08247; 1 site. DR iPTMnet; P08247; -. DR PhosphoSitePlus; P08247; -. DR BioMuta; SYP; -. DR DMDM; 135162; -. DR jPOST; P08247; -. DR MassIVE; P08247; -. DR MaxQB; P08247; -. DR PaxDb; 9606-ENSP00000263233; -. DR PeptideAtlas; P08247; -. DR ProteomicsDB; 52100; -. [P08247-1] DR ProteomicsDB; 6493; -. DR Pumba; P08247; -. DR ABCD; P08247; 1 sequenced antibody. DR Antibodypedia; 501; 1545 antibodies from 53 providers. DR DNASU; 6855; -. DR Ensembl; ENST00000263233.9; ENSP00000263233.4; ENSG00000102003.12. [P08247-1] DR Ensembl; ENST00000479808.5; ENSP00000418169.1; ENSG00000102003.12. [P08247-1] DR GeneID; 6855; -. DR KEGG; hsa:6855; -. DR MANE-Select; ENST00000263233.9; ENSP00000263233.4; NM_003179.3; NP_003170.1. DR UCSC; uc004dmz.2; human. [P08247-1] DR AGR; HGNC:11506; -. DR CTD; 6855; -. DR DisGeNET; 6855; -. DR GeneCards; SYP; -. DR HGNC; HGNC:11506; SYP. DR HPA; ENSG00000102003; Tissue enhanced (brain, retina). DR MalaCards; SYP; -. DR MIM; 300802; phenotype. DR MIM; 313475; gene. DR neXtProt; NX_P08247; -. DR OpenTargets; ENSG00000102003; -. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA36288; -. DR VEuPathDB; HostDB:ENSG00000102003; -. DR eggNOG; ENOG502QT4W; Eukaryota. DR GeneTree; ENSGT01030000234637; -. DR HOGENOM; CLU_064642_0_0_1; -. DR InParanoid; P08247; -. DR OMA; FIWKEVV; -. DR OrthoDB; 2881347at2759; -. DR PhylomeDB; P08247; -. DR TreeFam; TF315804; -. DR PathwayCommons; P08247; -. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR SignaLink; P08247; -. DR SIGNOR; P08247; -. DR BioGRID-ORCS; 6855; 15 hits in 787 CRISPR screens. DR ChiTaRS; SYP; human. DR GeneWiki; Synaptophysin; -. DR GenomeRNAi; 6855; -. DR Pharos; P08247; Tbio. DR PRO; PR:P08247; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P08247; Protein. DR Bgee; ENSG00000102003; Expressed in right hemisphere of cerebellum and 148 other cell types or tissues. DR ExpressionAtlas; P08247; baseline and differential. DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL. DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl. DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISS: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; ISS:UniProtKB. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl. DR GO; GO:0016188; P:synaptic vesicle maturation; NAS:UniProtKB. DR GO; GO:0048499; P:synaptic vesicle membrane organization; NAS:UniProtKB. 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; P08247; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cytoplasmic vesicle; Disease variant; KW Glycoprotein; Intellectual disability; Membrane; Phosphoprotein; KW Reference proteome; Repeat; Synapse; Synaptosome; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1..313 FT /note="Synaptophysin" FT /id="PRO_0000179161" 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..106 FT /note="Vesicular" FT /evidence="ECO:0000255" FT TRANSMEM 107..130 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 131..137 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 138..161 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 162..199 FT /note="Vesicular" FT /evidence="ECO:0000255" FT TRANSMEM 200..223 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 224..313 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 21..227 FT /note="MARVEL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581" FT REGION 238..313 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 254..305 FT /note="Repeats, Gly-rich" FT MOD_RES 81 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q62277" FT CARBOHYD 59 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..118 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056897" FT VARIANT 2 FT /note="L -> Q (in dbSNP:rs200470034)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062983" FT VARIANT 72 FT /note="E -> Q" FT /evidence="ECO:0000269|PubMed:28669405" FT /id="VAR_079223" FT VARIANT 158 FT /note="S -> L" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062984" FT VARIANT 166 FT /note="D -> N" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062985" FT VARIANT 217 FT /note="G -> R (in XLID96; dbSNP:rs137852561)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062986" FT VARIANT 248 FT /note="D -> N (in dbSNP:rs782086106)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062987" FT VARIANT 277 FT /note="D -> E (in XLID96; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062988" FT VARIANT 293 FT /note="G -> S (in XLID96; uncertain significance; FT dbSNP:rs139475570)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062989" FT CONFLICT 196 FT /note="P -> L (in Ref. 7; AAH64550)" FT /evidence="ECO:0000305" SQ SEQUENCE 313 AA; 33845 MW; 592289C43B12EFA7 CRC64; MLLLADMDVV NQLVAGGQFR VVKEPLGFVK VLQWVFAIFA FATCGSYSGE LQLSVDCANK TESDLSIEVE FEYPFRLHQV YFDAPTCRGG TTKVFLVGDY SSSAEFFVTV AVFAFLYSMG ALATYIFLQN KYRENNKGPM LDFLATAVFA FMWLVSSSAW AKGLSDVKMA TDPENIIKEM PVCRQTGNTC KELRDPVTSG LNTSVVFGFL NLVLWVGNLW FVFKETGWAA PFLRAPPGAP EKQPAPGDAY GDAGYGQGPG GYGPQDSYGP QGGYQPDYGQ PAGSGGSGYG PQGDYGQQGY GPQGAPTSFS NQM //