Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Z266 (SNAPN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Snapin
Synonyms:Bloc1s7, Snap25bp, Snapap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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. Ref.8 Ref.10 Ref.11

Subunit structure

Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Associates with the SNARE complex. Interacts with CNTRL, NANOS1, PUM2, RGS7 By similarity. 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. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. 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. Ref.1 Ref.4 Ref.5 Ref.7

Subcellular location

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. Cell junctionsynapsesynaptosome. Cytoplasmperinuclear region. Golgi apparatus membrane. Note: Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells By similarity. According to Ref.4 it is may be cytoplasmic and peripheral membrane bound. According to Ref.5 it is anchored to the vesicular membrane through an N-terminal signal anchor. Ref.4 Ref.5 Ref.7

Tissue specificity

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. Ref.4 Ref.9

Post-translational modification

Phosphorylated by CSNK1D/CK1. Ref.5 Ref.7

Sequence similarities

Belongs to the SNAPIN family.

Ontologies

Keywords
   Biological processExocytosis
   Cellular componentCell junction
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterograde axon cargo transport

Inferred from mutant phenotype Ref.11. Source: UniProtKB

anterograde synaptic vesicle transport

Inferred from mutant phenotype Ref.11. Source: UniProtKB

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

neuron projection development

Non-traceable author statement Ref.10. Source: UniProtKB

synaptic transmission

Inferred from mutant phenotype PubMed 19217378. Source: MGI

synaptic vesicle exocytosis

Inferred from sequence orthology Ref.1. Source: MGI

synaptic vesicle fusion to presynaptic membrane

Inferred from mutant phenotype PubMed 19217378. Source: MGI

synaptic vesicle maturation

Inferred from mutant phenotype PubMed 19217378. Source: MGI

terminal button organization

Inferred from mutant phenotype PubMed 19217378. Source: MGI

   Cellular_componentBLOC-1 complex

Inferred from direct assay PubMed 15102850. Source: MGI

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Inferred from direct assay PubMed 15102850. Source: MGI

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from sequence orthology Ref.1. Source: MGI

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSNARE binding

Inferred from sequence orthology Ref.1. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Csnk1dQ06486-24EBI-6170320,EBI-7088890From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Z266-1)

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.
Isoform 2 (identifier: Q9Z266-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-54: Missing.
     55-63: REQIDNLAT → MLVAHFLFP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135SNARE-associated protein Snapin
PRO_0000097557

Regions

Coiled coil37 – 12690 Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue101Phosphoserine By similarity
Modified residue141Phosphothreonine By similarity
Modified residue501Phosphoserine; by PKA; in vitro
Modified residue1291Phosphotyrosine By similarity
Modified residue1331Phosphoserine By similarity

Natural variations

Alternative sequence2 – 5453Missing in isoform 2.
VSP_009165
Alternative sequence55 – 639REQIDNLAT → MLVAHFLFP in isoform 2.
VSP_009166

Experimental info

Mutagenesis421S → A: No effect. Ref.5
Mutagenesis501S → A: Inhibition of phosphorylation. Ref.5
Mutagenesis501S → D: 3.5-fold increase in SNAP25 binding. Ref.5
Mutagenesis631T → A: No effect. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C81AC2ABCDCA21FA

FASTA13614,904
        10         20         30         40         50         60 
MAAAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN 

        70         80         90        100        110        120 
LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR 

       130 
RAMLDSGVYP PGSPSK 

« Hide

Isoform 2 [UniParc].

Checksum: 0E42F823DD655B55
Show »

FASTA839,582

References

« Hide 'large scale' references
[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. expand/collapse author list , 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, 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]"BLOC-1 complex deficiency alters the targeting of adaptor protein complex-3 cargoes."
Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M., Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A., Werner E., Faundez V.
Mol. Biol. Cell 17:4014-4026(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_598615.1. NM_133854.3.
UniGeneMm.331182.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203363. 1 interaction.
IntActQ9Z266. 5 interactions.
MINTMINT-3389684.

PTM databases

PhosphoSiteQ9Z266.

Proteomic databases

PaxDbQ9Z266.
PRIDEQ9Z266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000149884; ENSMUSP00000122090; ENSMUSG00000001018. [Q9Z266-1]
GeneID20615.
KEGGmmu:20615.
UCSCuc008qck.2. mouse. [Q9Z266-1]

Organism-specific databases

CTD23557.
MGIMGI:1333745. Snapin.

Phylogenomic databases

eggNOGNOG83669.
GeneTreeENSGT00390000008274.
HOGENOMHOG000253926.
HOVERGENHBG056744.
InParanoidQ9Z266.
OMAENTENFC.
OrthoDBEOG7SXW5D.
PhylomeDBQ9Z266.
TreeFamTF319577.

Gene expression databases

BgeeQ9Z266.
CleanExMM_SNAPIN.
GenevestigatorQ9Z266.

Family and domain databases

InterProIPR017246. Snapin.
IPR028119. Snapin/Pallidin/Snn1.
[Graphical view]
PANTHERPTHR31305. PTHR31305. 1 hit.
PfamPF14712. Snapin_Pallidin. 1 hit.
[Graphical view]
PIRSFPIRSF037631. Snapin. 1 hit.
ProtoNetSearch...

Other

NextBio298987.
PROQ9Z266.
SOURCESearch...

Entry information

Entry nameSNAPN_MOUSE
AccessionPrimary (citable) accession number: Q9Z266
Secondary accession number(s): Q3U8V4, Q922V7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot