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Q9Z266

- SNAPN_MOUSE

UniProt

Q9Z266 - SNAPN_MOUSE

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Protein

SNARE-associated protein Snapin

Gene

Snapin

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.3 Publications

GO - Molecular functioni

  1. SNARE binding Source: MGI

GO - Biological processi

  1. anterograde axon cargo transport Source: UniProtKB
  2. anterograde synaptic vesicle transport Source: UniProtKB
  3. autophagic vacuole maturation Source: MGI
  4. calcium ion-dependent exocytosis Source: ParkinsonsUK-UCL
  5. intracellular protein transport Source: InterPro
  6. negative regulation of neuron projection development Source: ParkinsonsUK-UCL
  7. neuron projection development Source: UniProtKB
  8. regulation of protein binding Source: Ensembl
  9. synaptic transmission Source: MGI
  10. synaptic vesicle exocytosis Source: MGI
  11. synaptic vesicle fusion to presynaptic membrane Source: MGI
  12. synaptic vesicle maturation Source: MGI
  13. synaptic vesicle transport Source: UniProtKB
  14. terminal button organization Source: MGI
Complete GO annotation...

Keywords - Biological processi

Exocytosis

Enzyme and pathway databases

ReactomeiREACT_232671. Golgi Associated Vesicle Biogenesis.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1333745. Snapin.

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmperinuclear region. Golgi apparatus membrane. Cytoplasmic vesiclesecretory vesicle By similarity
Note: Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells (By similarity). According to PubMed:12877659 it may be cytoplasmic and peripheral membrane bound. According to PubMed:11283605 it is anchored to the vesicular membrane through an N-terminal signal anchor.By similarity

GO - Cellular componenti

  1. BLOC-1 complex Source: MGI
  2. cell junction Source: UniProtKB-KW
  3. cytosol Source: MGI
  4. Golgi apparatus Source: UniProtKB-KW
  5. membrane Source: UniProtKB-KW
  6. nucleolus Source: Ensembl
  7. perinuclear region of cytoplasm Source: UniProtKB
  8. secretory granule Source: UniProtKB
  9. synapse Source: MGI
  10. synaptic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421S → A: No effect. 1 Publication
Mutagenesisi50 – 501S → A: Inhibition of phosphorylation. 1 Publication
Mutagenesisi50 – 501S → D: 3.5-fold increase in SNAP25 binding. 1 Publication
Mutagenesisi63 – 631T → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 136135SNARE-associated protein SnapinPRO_0000097557Add
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 PKA; in vitro1 Publication
Modified residuei129 – 1291PhosphotyrosineBy similarity
Modified residuei133 – 1331PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by PKD, phosphorylation controls SNAPIN protein stability (By similarity). Phosphorylated by CSNK1D/CK1.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Z266.
PaxDbiQ9Z266.
PRIDEiQ9Z266.

PTM databases

PhosphoSiteiQ9Z266.

Expressioni

Tissue specificityi

Strongly expressed in heart, brain, testis, kidney and liver; low expression in spleen, lung and skeletal muscle. In the testis, expressed in the seminiferous tubules.2 Publications

Gene expression databases

BgeeiQ9Z266.
CleanExiMM_SNAPIN.
ExpressionAtlasiQ9Z266. baseline and differential.
GenevestigatoriQ9Z266.

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Csnk1dQ06486-24EBI-6170320,EBI-7088890From a different organism.

Protein-protein interaction databases

BioGridi203363. 1 interaction.
IntActiQ9Z266. 5 interactions.
MINTiMINT-3389684.

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

eggNOGiNOG83669.
GeneTreeiENSGT00390000008274.
HOGENOMiHOG000253926.
HOVERGENiHBG056744.
InParanoidiQ9Z266.
OMAiHVHSVRE.
OrthoDBiEOG7SXW5D.
PhylomeDBiQ9Z266.
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.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Z266-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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:May 1, 1999 - v1
Checksum:iC81AC2ABCDCA21FA
GO
Isoform 2 (identifier: Q9Z266-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     55-63: REQIDNLAT → MLVAHFLFP

Show »
Length:82
Mass (Da):9,451
Checksum:i234286EC5C2B94D4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5454Missing in isoform 2. 1 PublicationVSP_009165Add
BLAST
Alternative sequencei55 – 639REQIDNLAT → MLVAHFLFP in isoform 2. 1 PublicationVSP_009166

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086838 mRNA. Translation: AAD11418.1.
AK007458 mRNA. Translation: BAB25049.1.
AK048007 mRNA. Translation: BAC33212.1.
AK050151 mRNA. Translation: BAC34095.1.
AK077840 mRNA. Translation: BAC37029.1.
AK080718 mRNA. Translation: BAC37991.1.
AK152057 mRNA. Translation: BAE30913.1.
BC006744 mRNA. Translation: AAH06744.1.
BC048691 mRNA. Translation: AAH48691.1.
CCDSiCCDS17531.1. [Q9Z266-1]
RefSeqiNP_598615.1. NM_133854.3. [Q9Z266-1]
UniGeneiMm.331182.

Genome annotation databases

EnsembliENSMUST00000149884; ENSMUSP00000122090; ENSMUSG00000001018. [Q9Z266-1]
GeneIDi20615.
KEGGimmu:20615.
UCSCiuc008qck.2. mouse. [Q9Z266-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086838 mRNA. Translation: AAD11418.1 .
AK007458 mRNA. Translation: BAB25049.1 .
AK048007 mRNA. Translation: BAC33212.1 .
AK050151 mRNA. Translation: BAC34095.1 .
AK077840 mRNA. Translation: BAC37029.1 .
AK080718 mRNA. Translation: BAC37991.1 .
AK152057 mRNA. Translation: BAE30913.1 .
BC006744 mRNA. Translation: AAH06744.1 .
BC048691 mRNA. Translation: AAH48691.1 .
CCDSi CCDS17531.1. [Q9Z266-1 ]
RefSeqi NP_598615.1. NM_133854.3. [Q9Z266-1 ]
UniGenei Mm.331182.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203363. 1 interaction.
IntActi Q9Z266. 5 interactions.
MINTi MINT-3389684.

PTM databases

PhosphoSitei Q9Z266.

Proteomic databases

MaxQBi Q9Z266.
PaxDbi Q9Z266.
PRIDEi Q9Z266.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000149884 ; ENSMUSP00000122090 ; ENSMUSG00000001018 . [Q9Z266-1 ]
GeneIDi 20615.
KEGGi mmu:20615.
UCSCi uc008qck.2. mouse. [Q9Z266-1 ]

Organism-specific databases

CTDi 23557.
MGIi MGI:1333745. Snapin.

Phylogenomic databases

eggNOGi NOG83669.
GeneTreei ENSGT00390000008274.
HOGENOMi HOG000253926.
HOVERGENi HBG056744.
InParanoidi Q9Z266.
OMAi HVHSVRE.
OrthoDBi EOG7SXW5D.
PhylomeDBi Q9Z266.
TreeFami TF319577.

Enzyme and pathway databases

Reactomei REACT_232671. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

NextBioi 298987.
PROi Q9Z266.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z266.
CleanExi MM_SNAPIN.
ExpressionAtlasi Q9Z266. baseline and differential.
Genevestigatori Q9Z266.

Family and domain databases

InterProi IPR017246. Snapin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view ]
PANTHERi PTHR31305. PTHR31305. 1 hit.
Pfami PF14712. Snapin_Pallidin. 1 hit.
[Graphical view ]
PIRSFi PIRSF037631. Snapin. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SNAP25.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Forelimb, Head, Liver, Pancreas and Retina.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Limb and Mammary tumor.
  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, SUBCELLULAR LOCATION, INTERACTION WITH SNAP23 AND STX4A.
  5. "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: PHOSPHORYLATION AT SER-50, INTERACTION WITH SNAP25, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-42; SER-50 AND THR-63.
  6. "Regulation of the exocytotic machinery by cAMP-dependent protein kinase: implications for presynaptic plasticity."
    Evans G.J., Morgan A.
    Biochem. Soc. Trans. 31:824-827(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON PHOSPHORYLATION.
  7. "Casein kinase 1 delta (CK1delta) interacts with the SNARE associated protein snapin."
    Wolff S., Stoeter M., Giamas G., Piesche M., Henne-Bruns D., Banting G., Knippschild U.
    FEBS Lett. 580:6477-6484(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CSNK1D/CK1, SUBCELLULAR LOCATION, INTERACTION WITH CSNK1D.
  8. Cited for: FUNCTION.
  9. "The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells."
    Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C., Kupryjanczyk J., Jaruzelska J.
    Mol. Hum. Reprod. 15:173-179(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth."
    Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R., Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C., Dell'Angelica E.C.
    Mol. Psychiatry 15:204-215(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
    Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.
    Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE AP-3 COMPLEX.

Entry informationi

Entry nameiSNAPN_MOUSE
AccessioniPrimary (citable) accession number: Q9Z266
Secondary accession number(s): Q3U8V4, Q922V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 109 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3