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Protein

Alpha-soluble NSF attachment protein

Gene

Napa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.By similarity

GO - Molecular functioni

  • SNARE binding Source: MGI
  • soluble NSF attachment protein activity Source: GO_Central
  • syntaxin binding Source: MGI

GO - Biological processi

  • apical protein localization Source: MGI
  • brain development Source: MGI
  • intracellular protein transport Source: MGI
  • membrane fusion Source: GO_Central
  • neuron differentiation Source: MGI
  • regulation of synaptic vesicle priming Source: MGI
  • SNARE complex disassembly Source: MGI
  • synaptic transmission, glutamatergic Source: MGI
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-MMU-6811438. Intra-Golgi traffic.
R-MMU-6811440. Retrograde transport at the Trans-Golgi-Network.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-soluble NSF attachment protein
Short name:
SNAP-alpha
Alternative name(s):
N-ethylmaleimide-sensitive factor attachment protein alpha
Gene namesi
Name:Napa
Synonyms:Snapa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:104563. Napa.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • myelin sheath Source: UniProtKB
  • synaptobrevin 2-SNAP-25-syntaxin-1a complex Source: MGI
  • terminal bouton Source: Ensembl
  • vacuolar membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Alpha-soluble NSF attachment proteinPRO_0000219057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei26 – 261PhosphoserineCombined sources
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei195 – 1951PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DB05.
MaxQBiQ9DB05.
PaxDbiQ9DB05.
PeptideAtlasiQ9DB05.
PRIDEiQ9DB05.

2D gel databases

REPRODUCTION-2DPAGEQ9DB05.

PTM databases

iPTMnetiQ9DB05.
PhosphoSiteiQ9DB05.
SwissPalmiQ9DB05.

Expressioni

Gene expression databases

BgeeiQ9DB05.
GenevisibleiQ9DB05. MM.

Interactioni

Subunit structurei

Interacts with PRKCABP, and disrupts the interaction between GRIA2 and PRKCABP, leading to the internalization of GRIA2. Found in a complex with VAMP8. Component of a SNARE-like complex that contains at least ZW10, USE1L, RINT1, STX18 and NAPA/SNAP-alpha. Interacts with STX12 (By similarity). Interacts with VTI1A.By similarity1 Publication

GO - Molecular functioni

  • SNARE binding Source: MGI
  • soluble NSF attachment protein activity Source: GO_Central
  • syntaxin binding Source: MGI

Protein-protein interaction databases

BioGridi223847. 3 interactions.
IntActiQ9DB05. 5 interactions.
MINTiMINT-1857852.
STRINGi10090.ENSMUSP00000006181.

Structurei

3D structure databases

ProteinModelPortaliQ9DB05.
SMRiQ9DB05. Positions 19-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SNAP family.Curated

Phylogenomic databases

eggNOGiKOG1586. Eukaryota.
ENOG410XPQ6. LUCA.
GeneTreeiENSGT00390000005826.
HOGENOMiHOG000165015.
HOVERGENiHBG001325.
InParanoidiQ9DB05.
KOiK15296.
OMAiATANACF.
OrthoDBiEOG7FNC80.
PhylomeDBiQ9DB05.
TreeFamiTF316547.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000744. NSF_attach.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13768. PTHR13768. 1 hit.
PRINTSiPR00448. NSFATTACHMNT.
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DB05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNSGKQAEA MALLAEAERK VKNSQSFFSG LFGGSSKIEE ACEIYARAAN
60 70 80 90 100
MFKMAKNWSA AGNAFCQAAQ LHLQLQSKHD AATCFVDAGN AFKKADPQEA
110 120 130 140 150
INCLMRAIEI YTDMGRFTIA AKHHISIAEI YETELVDVEK AIAHYEQSAD
160 170 180 190 200
YYKGEESNSS ANKCLLKVAG YAAQLEQYQK AIDIYEQVGT SAMDSPLLKY
210 220 230 240 250
SAKDYFFKAA LCHFCIDMLN AKLAVQKYEE LFPAFSDSRE CKLMKKLLEA
260 270 280 290
HEEQNVDSYT EAVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR
Length:295
Mass (Da):33,190
Last modified:June 1, 2001 - v1
Checksum:i30D099B598992AA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005372 mRNA. Translation: BAB23981.1.
AK050623 mRNA. Translation: BAC34348.1.
AK136689 mRNA. Translation: BAE23100.1.
AK171998 mRNA. Translation: BAE42767.1.
BC004804 mRNA. Translation: AAH04804.1.
CCDSiCCDS20843.1.
RefSeqiNP_080174.1. NM_025898.3.
UniGeneiMm.104540.

Genome annotation databases

EnsembliENSMUST00000006181; ENSMUSP00000006181; ENSMUSG00000006024.
GeneIDi108124.
KEGGimmu:108124.
UCSCiuc009fgw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005372 mRNA. Translation: BAB23981.1.
AK050623 mRNA. Translation: BAC34348.1.
AK136689 mRNA. Translation: BAE23100.1.
AK171998 mRNA. Translation: BAE42767.1.
BC004804 mRNA. Translation: AAH04804.1.
CCDSiCCDS20843.1.
RefSeqiNP_080174.1. NM_025898.3.
UniGeneiMm.104540.

3D structure databases

ProteinModelPortaliQ9DB05.
SMRiQ9DB05. Positions 19-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223847. 3 interactions.
IntActiQ9DB05. 5 interactions.
MINTiMINT-1857852.
STRINGi10090.ENSMUSP00000006181.

PTM databases

iPTMnetiQ9DB05.
PhosphoSiteiQ9DB05.
SwissPalmiQ9DB05.

2D gel databases

REPRODUCTION-2DPAGEQ9DB05.

Proteomic databases

EPDiQ9DB05.
MaxQBiQ9DB05.
PaxDbiQ9DB05.
PeptideAtlasiQ9DB05.
PRIDEiQ9DB05.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006181; ENSMUSP00000006181; ENSMUSG00000006024.
GeneIDi108124.
KEGGimmu:108124.
UCSCiuc009fgw.1. mouse.

Organism-specific databases

CTDi8775.
MGIiMGI:104563. Napa.

Phylogenomic databases

eggNOGiKOG1586. Eukaryota.
ENOG410XPQ6. LUCA.
GeneTreeiENSGT00390000005826.
HOGENOMiHOG000165015.
HOVERGENiHBG001325.
InParanoidiQ9DB05.
KOiK15296.
OMAiATANACF.
OrthoDBiEOG7FNC80.
PhylomeDBiQ9DB05.
TreeFamiTF316547.

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-MMU-6811438. Intra-Golgi traffic.
R-MMU-6811440. Retrograde transport at the Trans-Golgi-Network.

Miscellaneous databases

ChiTaRSiNapa. mouse.
PROiQ9DB05.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB05.
GenevisibleiQ9DB05. MM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000744. NSF_attach.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13768. PTHR13768. 1 hit.
PRINTSiPR00448. NSFATTACHMNT.
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum, Epididymis, Spleen and Thymus.
  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].
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 247-264 AND 272-282, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (Vti1-rp2) implicated in protein trafficking in the secretory pathway."
    Xu Y., Wong S.H., Tang B.L., Subramaniam V.N., Zhang T., Hong W.
    J. Biol. Chem. 273:21783-21789(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VTI1A.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSNAA_MOUSE
AccessioniPrimary (citable) accession number: Q9DB05
Secondary accession number(s): Q543I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 125 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.