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Protein

SNARE-associated protein Snapin

Gene

Snapin

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

Functioni

Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Exocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
SNARE-associated protein Snapin
Alternative name(s):
Biogenesis of lysosome-related organelles complex 1 subunit 7
Short name:
BLOC-1 subunit 7
Synaptosomal-associated protein 25-binding protein
Short name:
SNAP-associated protein
Gene namesi
Name:Snapin
Synonyms:Bloc1s7, Snap25bp, Snapap
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1560377. Snapin.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 136135SNARE-associated protein SnapinPRO_0000097558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei10 – 101PhosphoserineBy similarity
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei50 – 501Phosphoserine; by PKABy similarity
Modified residuei126 – 1261PhosphoserineBy similarity
Modified residuei129 – 1291PhosphotyrosineBy similarity
Modified residuei133 – 1331PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CSNK1D/CK1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP60192.
PRIDEiP60192.

PTM databases

iPTMnetiP60192.

Expressioni

Tissue specificityi

Strongly expressed in testis, spleen, kidney, liver and brain; lower expression in heart, fat and skeletal muscle.2 Publications

Gene expression databases

GenevisibleiP60192. RN.

Interactioni

Subunit structurei

Interacts with CSNK1D, SNAP23 and STX4A but not with STX1A, VAMP2 and SYT1. Interacts with SNAP25; the interaction with SNAP25 is increased by its phosphorylation. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Associates with the SNARE complex. Interacts with CNTRL, NANOS1, PUM2 and RGS7. Interacts with TOR1A; the interaction is direct and associates SNAPIN with the CSN complex (By similarity).By similarity

Protein-protein interaction databases

BioGridi254916. 1 interaction.
IntActiP60192. 5 interactions.
MINTiMINT-3389957.
STRINGi10116.ENSRNOP00000018830.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 13654Interaction with TOR1ABy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili37 – 12690Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SNAPIN family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410J16C. Eukaryota.
ENOG4111JM9. LUCA.
GeneTreeiENSGT00390000008274.
HOGENOMiHOG000253926.
HOVERGENiHBG056744.
InParanoidiP60192.
KOiK20002.
OMAiINEHQKV.
OrthoDBiEOG7SXW5D.
PhylomeDBiP60192.
TreeFamiTF319577.

Family and domain databases

InterProiIPR017246. Snapin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view]
PANTHERiPTHR31305. PTHR31305. 1 hit.
PfamiPF14712. Snapin_Pallidin. 1 hit.
[Graphical view]
PIRSFiPIRSF037631. Snapin. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES
60 70 80 90 100
QVELREQIDN LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ
110 120 130
NAQERLRRLN HSVAKETARR RAMLDSGVYP PGSPSK
Length:136
Mass (Da):14,904
Last modified:January 16, 2004 - v1
Checksum:iC81AC2ABCDCA21FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012141 Genomic DNA. No translation available.
CB613900 mRNA. No translation available.
RefSeqiNP_001164047.1. NM_001170576.1.
UniGeneiRn.3815.

Genome annotation databases

EnsembliENSRNOT00000018830; ENSRNOP00000018830; ENSRNOG00000013356.
GeneIDi295217.
KEGGirno:295217.
UCSCiRGD:1560377. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012141 Genomic DNA. No translation available.
CB613900 mRNA. No translation available.
RefSeqiNP_001164047.1. NM_001170576.1.
UniGeneiRn.3815.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi254916. 1 interaction.
IntActiP60192. 5 interactions.
MINTiMINT-3389957.
STRINGi10116.ENSRNOP00000018830.

PTM databases

iPTMnetiP60192.

Proteomic databases

PaxDbiP60192.
PRIDEiP60192.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018830; ENSRNOP00000018830; ENSRNOG00000013356.
GeneIDi295217.
KEGGirno:295217.
UCSCiRGD:1560377. rat.

Organism-specific databases

CTDi23557.
RGDi1560377. Snapin.

Phylogenomic databases

eggNOGiENOG410J16C. Eukaryota.
ENOG4111JM9. LUCA.
GeneTreeiENSGT00390000008274.
HOGENOMiHOG000253926.
HOVERGENiHBG056744.
InParanoidiP60192.
KOiK20002.
OMAiINEHQKV.
OrthoDBiEOG7SXW5D.
PhylomeDBiP60192.
TreeFamiTF319577.

Miscellaneous databases

PROiP60192.

Gene expression databases

GenevisibleiP60192. RN.

Family and domain databases

InterProiIPR017246. Snapin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view]
PANTHERiPTHR31305. PTHR31305. 1 hit.
PfamiPF14712. Snapin_Pallidin. 1 hit.
[Graphical view]
PIRSFiPIRSF037631. Snapin. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Snapin: a SNARE-associated protein implicated in synaptic transmission."
    Ilardi J.M., Mochida S., Sheng Z.-H.
    Nat. Neurosci. 2:119-124(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex."
    Chheda M.G., Ashery U., Thakur P., Rettig J., Sheng Z.-H.
    Nat. Cell Biol. 3:331-338(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  4. "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells."
    Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I., Manickam E., Rowe T.
    Biochem. J. 375:433-440(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "The dystonia-associated protein torsinA modulates synaptic vesicle recycling."
    Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.
    J. Biol. Chem. 283:7568-7579(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSNAPN_RAT
AccessioniPrimary (citable) accession number: P60192
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: July 6, 2016
This is version 101 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, 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.