SYPH_RAT
ID SYPH_RAT Reviewed; 307 AA.
AC P07825; Q499R3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Synaptophysin;
DE AltName: Full=Major synaptic vesicle protein p38;
GN Name=Syp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=3123215; DOI=10.1002/j.1460-2075.1987.tb02644.x;
RA Leube R.E., Kaiser P., Seiter A., Zimbelmann R., Franke W.W., Rehm H.,
RA Knaus P., Prior P., Betz H., Reinke H., Beyreuther K., Wiedenmann B.;
RT "Synaptophysin: molecular organization and mRNA expression as determined
RT from cloned cDNA.";
RL EMBO J. 6:3261-3268(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3120313; DOI=10.1126/science.3120313;
RA Suedhof T.C., Lottspeich F., Greengard P., Mehl E., Jahn R.;
RT "A synaptic vesicle protein with a novel cytoplasmic domain and four
RT transmembrane regions.";
RL Science 238:1142-1144(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1902431; DOI=10.1016/0378-1119(91)90127-w;
RA Bargou R.C.E.F., Leube R.E.;
RT "The synaptophysin-encoding gene in rat and man is specifically transcribed
RT in neuroendocrine cells.";
RL Gene 99:197-204(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 13-307.
RC TISSUE=Brain;
RX PubMed=3121632; DOI=10.1083/jcb.105.6.2447;
RA Buckley K.M., Floor E., Kelly R.B.;
RT "Cloning and sequence analysis of cDNA encoding p38, a major synaptic
RT vesicle protein.";
RL J. Cell Biol. 105:2447-2456(1987).
RN [7]
RP INTERACTION WITH SIAH1 AND SIAH2, AND DEGRADATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=11786535; DOI=10.1074/jbc.m107857200;
RA Wheeler T.C., Chin L.-S., Li Y., Roudabush F.L., Li L.;
RT "Regulation of synaptophysin degradation by mammalian homologues of Seven
RT in Absentia.";
RL J. Biol. Chem. 277:10273-10282(2002).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP PHOSPHORYLATION.
RX PubMed=26026271; DOI=10.1016/j.febslet.2015.05.033;
RA Keenan S., Lewis P.A., Wetherill S.J., Dunning C.J., Evans G.J.;
RT "The N2-Src neuronal splice variant of C-Src has altered SH3 domain ligand
RT specificity and a higher constitutive activity than N1-Src.";
RL FEBS Lett. 589:1995-2000(2015).
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 (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 -!- INTERACTION:
CC P07825; Q5XIE8: Itm2b; NbExp=4; IntAct=EBI-976085, EBI-15348306;
CC P07825; P33535: Oprm1; NbExp=8; IntAct=EBI-976085, EBI-4392569;
CC P07825; Q9QWI6-2: Srcin1; Xeno; NbExp=2; IntAct=EBI-976085, EBI-775607;
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 -!- TISSUE SPECIFICITY: Expressed in the brain with expression in the
CC cerebrum and the cerebellum. {ECO:0000269|PubMed:3123215}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the spinal cord of newborn animals.
CC {ECO:0000269|PubMed:3123215}.
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.
CC -!- PTM: Phosphorylated by SRC. {ECO:0000269|PubMed:26026271}.
CC -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.
CC {ECO:0000305}.
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DR EMBL; X06177; CAA29543.1; -; mRNA.
DR EMBL; X06388; CAA29685.1; -; mRNA.
DR EMBL; M58396; AAA42196.1; -; Genomic_DNA.
DR EMBL; M58402; AAA42196.1; JOINED; Genomic_DNA.
DR EMBL; M58401; AAA42196.1; JOINED; Genomic_DNA.
DR EMBL; M58399; AAA42196.1; JOINED; Genomic_DNA.
DR EMBL; BC099798; AAH99798.1; -; mRNA.
DR EMBL; X06655; CAA29854.1; -; mRNA.
DR PIR; JU0464; B27287.
DR RefSeq; NP_036796.1; NM_012664.3.
DR AlphaFoldDB; P07825; -.
DR BioGRID; 246927; 7.
DR IntAct; P07825; 14.
DR MINT; P07825; -.
DR STRING; 10116.ENSRNOP00000013724; -.
DR GlyGen; P07825; 1 site.
DR iPTMnet; P07825; -.
DR PhosphoSitePlus; P07825; -.
DR jPOST; P07825; -.
DR PaxDb; P07825; -.
DR PRIDE; P07825; -.
DR GeneID; 24804; -.
DR KEGG; rno:24804; -.
DR UCSC; RGD:3802; rat.
DR CTD; 6855; -.
DR RGD; 3802; Syp.
DR eggNOG; ENOG502QT4W; Eukaryota.
DR InParanoid; P07825; -.
DR OrthoDB; 1446480at2759; -.
DR PhylomeDB; P07825; -.
DR PRO; PR:P07825; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043229; C:intracellular organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR GO; GO:0044309; C:neuron spine; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:CAFA.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:1904645; P:response to amyloid-beta; IEP:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
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..307
FT /note="Synaptophysin"
FT /id="PRO_0000179163"
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..101
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..194
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 15..222
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 233..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..298
FT /note="Repeats, Gly-rich"
FT COMPBIAS 290..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 273
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; 33311 MW; A245E4F70BF0EAF0 CRC64;
MDVVNQLVAG GQFRVVKEPL GFVKVLQWVF AIFAFATCGS YTGELRLSVE CANKTESALN
IEVEFEYPFR LHQVYFDAPS CVKGGTTKIF LVGDYSSSAE FFVTVAVFAF LYSMGALATY
IFLQNKYREN NKGPMMDFLA TAVFAFMWLV SSSAWAKGLS DVKMATDPEN IIKEMPMCRQ
TGNTCKELRD PVTSGLNTSV VFGFLNLVLW VGNLWFVFKE TGWAAPFMRA PPGAPEKQPA
PGDAYGDAGY GQGPGGYGPQ DSYGPQGGYQ PDYGQPASGG GGYGPQGDYG QQGYGQQGAP
TSFSNQM
