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Protein

Synaptosomal-associated protein 23

Gene

Snap23

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.By similarity

GO - Molecular functioni

  • SNAP receptor activity Source: FlyBase
  • syntaxin binding Source: RGD

GO - Biological processi

  • membrane fusion Source: RGD
  • protein complex assembly Source: RGD
  • protein transport Source: RGD
  • regulation of exocytosis Source: RGD
  • synaptic vesicle fusion to presynaptic active zone membrane Source: GO_Central
  • synaptic vesicle priming Source: GO_Central
  • vesicle-mediated transport Source: RGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptosomal-associated protein 23
Short name:
SNAP-23
Alternative name(s):
Vesicle-membrane fusion protein SNAP-23
Gene namesi
Name:Snap23
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620221. Snap23.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • plasma membrane Source: RGD
  • SNARE complex Source: UniProtKB
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Synaptosomal-associated protein 23PRO_0000213600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Lipidationi79 – 791S-palmitoyl cysteineBy similarity
Lipidationi80 – 801S-palmitoyl cysteineBy similarity
Lipidationi83 – 831S-palmitoyl cysteineBy similarity
Lipidationi85 – 851S-palmitoyl cysteineBy similarity
Lipidationi87 – 871S-palmitoyl cysteineBy similarity
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei160 – 1601PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PRIDEiO70377.

PTM databases

iPTMnetiO70377.
PhosphoSiteiO70377.

Interactioni

Subunit structurei

Homotetramer (via coiled-coil domain), also forms heterotetramers with STX4 and VAMP3 (By similarity). Found in a complex with VAMP8 and STX1A (By similarity). Found in a complex with VAMP8 and STX4 in pancreas (By similarity). Interacts simultaneously with SNAPIN and SYN4 (By similarity). Interacts with STX1A (By similarity). Interacts with STX12 (By similarity). Interacts tightly to multiple syntaxins and synaptobrevins/VAMPs (PubMed:14993220). Interacts with ZDHHC13 (via ANK repeats) (By similarity). Interacts with ZDHHC17 (via ANK repeats) (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
IkbkbQ9QY782EBI-1573765,EBI-1812464

GO - Molecular functioni

  • SNAP receptor activity Source: FlyBase
  • syntaxin binding Source: RGD

Protein-protein interaction databases

BioGridi249168. 2 interactions.
IntActiO70377. 7 interactions.
MINTiMINT-96124.

Structurei

3D structure databases

ProteinModelPortaliO70377.
SMRiO70377. Positions 23-76, 136-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 7663t-SNARE coiled-coil homology 1PROSITE-ProRule annotationAdd
BLAST
Domaini145 – 20763t-SNARE coiled-coil homology 2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili23 – 7654By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the SNAP-25 family.Curated
Contains 2 t-SNARE coiled-coil homology domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

HOVERGENiHBG056971.
InParanoidiO70377.
KOiK08508.
PhylomeDBiO70377.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O70377-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDLSPEEIQ LRAHQVTDES LESTRRILGL AIESQDAGIK TITMLDEQGE
60 70 80 90 100
QLNRIEEGMD QINKDMREAE KTLTELNKCC GLCVCPCNRT KNFESGKNYK
110 120 130 140 150
ATWGDGGDSS PSNVVSKQPS RITNGQPQQT TGAASGGYIK RITNDAREDE
160 170 180 190 200
MEENLTQVGS ILGNLKNMAL DMGNEIDAQN QQIQKITEKA DTNKNRIDIA
210
NTRAKKLIDS
Length:210
Mass (Da):23,235
Last modified:August 1, 1998 - v1
Checksum:i0D63E3A6F9FE3BA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052596 mRNA. Translation: AAC06031.1.
BC127494 mRNA. Translation: AAI27495.1.
RefSeqiNP_073180.1. NM_022689.2.
UniGeneiRn.14789.

Genome annotation databases

GeneIDi64630.
KEGGirno:64630.
UCSCiRGD:620221. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052596 mRNA. Translation: AAC06031.1.
BC127494 mRNA. Translation: AAI27495.1.
RefSeqiNP_073180.1. NM_022689.2.
UniGeneiRn.14789.

3D structure databases

ProteinModelPortaliO70377.
SMRiO70377. Positions 23-76, 136-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249168. 2 interactions.
IntActiO70377. 7 interactions.
MINTiMINT-96124.

PTM databases

iPTMnetiO70377.
PhosphoSiteiO70377.

Proteomic databases

PRIDEiO70377.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64630.
KEGGirno:64630.
UCSCiRGD:620221. rat.

Organism-specific databases

CTDi8773.
RGDi620221. Snap23.

Phylogenomic databases

HOVERGENiHBG056971.
InParanoidiO70377.
KOiK08508.
PhylomeDBiO70377.

Miscellaneous databases

PROiO70377.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SNAP-23 participates in SNARE complex assembly in rat adipose cells."
    St Denis J.-F., Cabaniols J.-P., Cushman S.W., Roche P.A.
    Biochem. J. 338:709-715(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis."
    Rao S.K., Huynh C., Proux-Gillardeaux V., Galli T., Andrews N.W.
    J. Biol. Chem. 279:20471-20479(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SNARE COMPLEX CHARACTERIZATION.
  4. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 55-64, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiSNP23_RAT
AccessioniPrimary (citable) accession number: O70377
Secondary accession number(s): A0JPL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.