ID   SYPH_SPECI              Reviewed;         307 AA.
AC   Q5YJC1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Synaptophysin;
GN   Name=SYP;
OS   Spermophilus citellus (European suslik) (Citellus citellus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Spermophilus.
OX   NCBI_TaxID=9997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Stieler J.T., Strijkstra A.M.;
RT   "Molecular cloning of Spermophilus citellus synaptophysin (Syp) mRNA.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P07825, ECO:0000250|UniProtKB:P08247}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:Q62277}; 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. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.
CC       {ECO:0000305}.
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DR   EMBL; AY392022; AAS59775.1; -; mRNA.
DR   AlphaFoldDB; Q5YJC1; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Calcium; Cytoplasmic vesicle; Glycoprotein; Membrane; Phosphoprotein;
KW   Repeat; Synapse; Synaptosome; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   CHAIN           1..307
FT                   /note="Synaptophysin"
FT                   /id="PRO_0000250500"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..100
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..193
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          15..221
FT                   /note="MARVEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT   REGION          232..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..298
FT                   /note="Repeats, Gly-rich"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         75
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62277"
FT   MOD_RES         220
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         272
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         289
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   307 AA;  33275 MW;  2E5087F714C5A586 CRC64;
     MDVVNQLVAG GQFRVIKEPL GFVKVLQWVF AIFAFATCGS YNGELRLSVE CANKTESDLS
     IEVEFEYPFR LHQVYFDAPN CRGGTTKVFL LGDYSSSAEF FVTVAVFAFL YSMGALATYI
     FLQNKYRENN KGPMMDFLAT AVFAFMWLVS SSAWAKGLSD VKMATDPENI IKEMDVCRQT
     GNTCKELRDP VTSGLNTSVV FGFLNLVLWV GNLWFVFKET GWAAPFLRAP PGAPEKQPAP
     GDAYGDAGYG QGPGGYGPQD SYGPQGGYQP DYGQPAGGGG GGYGPQGDYG QQGYGPQGAP
     TSFSNQM