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Q9ERB0 (SNP29_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptosomal-associated protein 29

Short name=SNAP-29
Alternative name(s):
Golgi SNARE of 32 kDa
Short name=Gs32
Soluble 29 kDa NSF attachment protein
Vesicle-membrane fusion protein SNAP-29
Gene names
Name:Snap29
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

SNAREs, Soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Probably involved in multiple membrane trafficking steps By similarity.

Subunit structure

Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17, involved in fusion of autophagosome with lysosome. Interacts with multiple syntaxins including STX6 By similarity.

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity. Note: Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic By similarity.

Sequence similarities

Belongs to the SNAP-25 family.

Contains 1 t-SNARE coiled-coil homology domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Synaptosomal-associated protein 29
PRO_0000213602

Regions

Domain198 – 26063t-SNARE coiled-coil homology
Coiled coil76 – 10732 Potential

Experimental info

Sequence conflict183 – 1842SS → FF in BAB23769. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9ERB0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: DD813A78C605576F

FASTA26029,572
        10         20         30         40         50         60 
MSGYPKSYNP FDDDVEEEDT RPAPWKDVRD LPDGPDAPID RQQYLRQEVL RRAEATAAST 

        70         80         90        100        110        120 
SRSLSLMYES EKIGVASSEE LVRQRGVLEH TEKMVDKMDQ DLKMSQKHIN SIKSVFGGFI 

       130        140        150        160        170        180 
NYFKSKPVEP PPEQNGSIVS QPNSRLKEAI NTSKDQENKY QASHPNLRRL QDAELDSVPK 

       190        200        210        220        230        240 
EPSSTVNTEV YPKNSTLRTY HQKIDSNLDE LSVGLGHLKD IALGMQTEIE EQDDILDRLT 

       250        260 
TKVDKLDVNI KSTEKKVRQL 

« Hide

References

« Hide 'large scale' references
[1]Bui T.D., Hong W.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Strain: C57BL/6J.
Tissue: Hypothalamus, Liver and Testis.
[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].
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY008722 mRNA. Translation: AAG32076.1.
AK005042 mRNA. Translation: BAB23769.1.
AK007065 mRNA. Translation: BAB24850.1.
AK039203 mRNA. Translation: BAC30277.1.
AK147845 mRNA. Translation: BAE28177.1.
BC030066 mRNA. Translation: AAH30066.1.
CCDSCCDS28001.1.
RefSeqNP_075837.3. NM_023348.4.
UniGeneMm.271992.

3D structure databases

ProteinModelPortalQ9ERB0.
SMRQ9ERB0. Positions 54-110, 204-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4998219.

PTM databases

PhosphoSiteQ9ERB0.

Proteomic databases

MaxQBQ9ERB0.
PaxDbQ9ERB0.
PRIDEQ9ERB0.

Protocols and materials databases

DNASU67474.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023449; ENSMUSP00000023449; ENSMUSG00000022765.
GeneID67474.
KEGGmmu:67474.
UCSCuc007yku.1. mouse.

Organism-specific databases

CTD9342.
MGIMGI:1914724. Snap29.

Phylogenomic databases

eggNOGNOG244202.
GeneTreeENSGT00510000048053.
HOGENOMHOG000046806.
HOVERGENHBG057045.
InParanoidQ9ERB0.
KOK08509.
OMAAYPRSYN.
OrthoDBEOG7FNC8G.
PhylomeDBQ9ERB0.
TreeFamTF320226.

Gene expression databases

BgeeQ9ERB0.
CleanExMM_SNAP29.
GenevestigatorQ9ERB0.

Family and domain databases

InterProIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEPS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNAP29. mouse.
NextBio324690.
PROQ9ERB0.
SOURCESearch...

Entry information

Entry nameSNP29_MOUSE
AccessionPrimary (citable) accession number: Q9ERB0
Secondary accession number(s): Q3UGN0, Q9DBC5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 97 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