SYPH_BOVIN
ID SYPH_BOVIN Reviewed; 313 AA.
AC P20488;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Synaptophysin;
DE AltName: Full=Major synaptic vesicle protein p38;
GN Name=SYP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2492017; DOI=10.1016/s0021-9258(19)85081-0;
RA Johnston P.A., Jahn R., Suedhof T.C.;
RT "Transmembrane topography and evolutionary conservation of synaptophysin.";
RL J. Biol. Chem. 264:1268-1273(1989).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P07825, ECO:0000250|UniProtKB:P08247}.
CC -!- INTERACTION:
CC P20488; P20488: SYP; NbExp=3; IntAct=EBI-15641786, EBI-15641786;
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: Characteristic of a type of small (30-80 nm)
CC neurosecretory vesicles, including presynaptic vesicles, but also
CC vesicles of various neuroendocrine cells of both neuronal and
CC epithelial phenotype.
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 -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30767.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M22967; AAA30767.1; ALT_INIT; mRNA.
DR PIR; A32208; A32208.
DR RefSeq; NP_776388.1; NM_173963.1.
DR AlphaFoldDB; P20488; -.
DR DIP; DIP-29431N; -.
DR STRING; 9913.ENSBTAP00000021428; -.
DR PaxDb; P20488; -.
DR GeneID; 280937; -.
DR KEGG; bta:280937; -.
DR CTD; 6855; -.
DR eggNOG; ENOG502QT4W; Eukaryota.
DR InParanoid; P20488; -.
DR OrthoDB; 1446480at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042584; C:chromaffin granule membrane; IDA:AgBase.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:AgBase.
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:0051020; F:GTPase binding; IPI:AgBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0045920; P:negative regulation of exocytosis; IDA:AgBase.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:InterPro.
DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; ISS:UniProtKB.
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; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..313
FT /note="Synaptophysin"
FT /id="PRO_0000179160"
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..304
FT /note="Repeats, Gly/Tyr-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 CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 313 AA; 33910 MW; 3D787D4288304587 CRC64;
MLLLADMDVV NQLVAGGQFR VVKEPLGFVK VLQWVFAIFA FATCGSYSGE LQLSVDCANK
TKSDLNIEVE FEYPFRLHEV YFEAPTCQGD PKKIFLVGNY SSSAEFFVTV AVFAFLYSMG
ALATYIFLQN KYRENNKGPM LDFLATAVFA FMWLVSSSAW AKGLSDVKMA TDPENIIKGM
HVCHQPGNTC KELRDPVTSG LNTSVVFGFL NLVLWVGNLW FVFKETGWAA PFLRAPPGAP
EKQPAPGDAY GQAGYGQGPG GYGPQDSYGP QGGYQPDYGQ PASSGGGGYG PQGDYGQQGY
GPQGAPTSFS NQM
