Skip Header

Contribute Send feedback
Read comments (?) or add your own

O89116 (VTI1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Vesicle transport through interaction with t-SNAREs homolog 1A
Alternative name(s):
Vesicle transport v-SNARE protein Vti1-like 2
Vti1-rp2
Gene names
Name:Vti1a
Synonyms:Vti1, Vti1l2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be concerned with increased secretion of cytokines associated with cellular senescence. Ref.5

Subunit structure

Interacts with distinct SNARE complexes that contain either STX5 or STX6. Interacts with NAPA and, to a lesser extent, with NAPG. Also identified in a complex containing STX13 and VAMP4 By similarity. Ref.1

Subcellular location

Golgi apparatus membrane; Single-pass type IV membrane protein By similarity.

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Belongs to the VTI1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Vesicle transport through interaction with t-SNAREs homolog 1A
PRO_0000218226

Regions

Topological domain1 – 192192Cytoplasmic Potential
Transmembrane193 – 21321Helical; Anchor for type IV membrane protein; Potential
Topological domain214 – 2174Vesicular Potential
Coiled coil31 – 9262 Potential
Coiled coil112 – 17867 Potential

Secondary structure

............ 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O89116 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 3FD7B7A5A16E3522

FASTA21724,986
        10         20         30         40         50         60 
MSSDFEGYEQ DFAVLTAEIT SKIARVPRLP PDEKKQMVAN VEKQLEEARE LLEQMDLEVR 

        70         80         90        100        110        120 
EIPPQSRGMY SNRMRSYKQE MGKLETDFKR SRIAYSDEVR NELLGDAGNS SENQRAHLLD 

       130        140        150        160        170        180 
NTERLERSSR RLEAGYQIAV ETEQIGQEML ENLSHDREKI QRARDRLRDA DANLGKSSRI 

       190        200        210 
LTGMLRRIIQ NRILLVILGI IVVIAILTAI AFFVKGH 

« Hide

References

« Hide 'large scale' references
[1]"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: 9705316] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NAPA AND NAPG, IDENTIFICATION IN SNARE COMPLEXES WITH STX5 OR STX6, TISSUE SPECIFICITY.
[2]"Seven novel mammalian SNARE proteins localize to distinct membrane compartments."
Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R., Yoo J.-S., Scheller R.H.
J. Biol. Chem. 273:10317-10324(1998) [PubMed: 9553086] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung and Skin.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
[5]"A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KChIP1 and Kv4 potassium channels."
Flowerdew S.E., Burgoyne R.D.
Biochem. J. 418:529-540(2009) [PubMed: 19138172] [Abstract]
Cited for: FUNCTION.
[6]"Solution structure of RSGI RUH-009, an N-terminal domain of VTI1A [Mus musculus]."
RIKEN structural genomics initiative (RSGI)
Submitted (MAY-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 3-94.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035823 mRNA. Translation: AAC32049.1.
AF035209 mRNA. Translation: AAC23482.1.
AK004751 mRNA. Translation: BAB23532.1.
AK028646 mRNA. Translation: BAC26046.1.
BC019386 mRNA. Translation: AAH19386.1.
IPIIPI00131540.
RefSeqNP_058558.1. NM_016862.3.
UniGeneMm.258637.
Mm.451214.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VCSNMR-A6-94[»]
ProteinModelPortalO89116.
SMRO89116. Positions 8-94, 113-190.
ModBaseSearch...

Protein-protein interaction databases

IntActO89116. 1 interaction.
STRINGO89116.

PTM databases

PhosphoSiteO89116.

Proteomic databases

PRIDEO89116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000095950; ENSMUSP00000093644; ENSMUSG00000024983.
GeneID53611.
KEGGmmu:53611.
UCSCuc008hxx.1. mouse.

Organism-specific databases

CTD143187.
MGIMGI:1855699. Vti1a.

Phylogenomic databases

eggNOGroNOG15861.
GeneTreeENSGT00530000063466.
HOVERGENHBG104027.
OrthoDBEOG4V6ZHV.
PhylomeDBO89116.

Gene expression databases

ArrayExpressO89116.
BgeeO89116.
GenevestigatorO89116.
GermOnlineENSMUSG00000024983. Mus musculus.

Family and domain databases

InterProIPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
IPR007705. Vesicle_trsprt_v-SNARE_N.
[Graphical view]
KOK08493.
PfamPF05008. V-SNARE. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. t-snare. 1 hit.
ProtoNetSearch...

Other

NextBio310323.
SOURCESearch...

Entry information

Entry nameVTI1A_MOUSE
AccessionPrimary (citable) accession number: O89116
Secondary accession number(s): Q545P9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1998
Last modified: January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families