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Protein

Vesicle transport through interaction with t-SNAREs homolog 1B

Gene

Vti1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle transport through interaction with t-SNAREs homolog 1B
Alternative name(s):
Vesicle transport v-SNARE protein Vti1-like 1
Vti1-rp1
Gene namesi
Name:Vti1b
Synonyms:Vti1l1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2323682. Vti1b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 208207CytoplasmicSequence analysisAdd
BLAST
Transmembranei209 – 22921Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini230 – 2323VesicularSequence analysis

GO - Cellular componenti

  • Golgi apparatus Source: InterPro
  • integral component of membrane Source: UniProtKB-KW
  • late endosome membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • neuronal cell body Source: ParkinsonsUK-UCL
  • SNARE complex Source: UniProtKB
  • synaptic vesicle Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 232231Vesicle transport through interaction with t-SNAREs homolog 1BPRO_0000218230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei138 – 1381PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP58200.
PRIDEiP58200.

Interactioni

Subunit structurei

May interact with STX17 (By similarity). Forms a SNARE complex with STX7, STX8 and VAMP8 which functions in the homotypic fusion of late endosomes. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VIT1B that is required for heterotypic fusion of late endosomes with lysosomes.By similarity

Protein-protein interaction databases

IntActiP58200. 2 interactions.
STRINGi10116.ENSRNOP00000015814.

Structurei

3D structure databases

ProteinModelPortaliP58200.
SMRiP58200. Positions 1-96, 139-197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili36 – 9863Sequence analysisAdd
BLAST
Coiled coili160 – 20142Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the VTI1 family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1666. Eukaryota.
ENOG4111J90. LUCA.
HOGENOMiHOG000116573.
HOVERGENiHBG058837.
InParanoidiP58200.
PhylomeDBiP58200.

Family and domain databases

InterProiIPR027027. GOSR2/Membrin/Bos1.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
IPR007705. Vesicle_trsprt_v-SNARE_N.
[Graphical view]
PfamiPF05008. V-SNARE. 1 hit.
[Graphical view]
PIRSFiPIRSF028865. Membrin-2. 1 hit.
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P58200-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSAASSEH FEKLHEIFRG LLEDLQGVPE RLLGTAGTEE KKKLVRDFDE
60 70 80 90 100
KQQEANETLA EMEEELRYAP LTFRNSMMSK LRNYRKDLAK LHREVRSTPL
110 120 130 140 150
TATPGGRGDL KFGTYTLENE HLNRLQSQRA LLLQGTESLN RATQSIERSH
160 170 180 190 200
RIAAETDQIG SEIIEELGEQ RDQLERTKSR LVNTNENLSK SRKILRSMSR
210 220 230
KVITNKLLLS VIIVLELAIL VGLVYYKFFR HH
Length:232
Mass (Da):26,703
Last modified:October 23, 2007 - v2
Checksum:i017363526CE3B9EA
GO

Sequence cautioni

The sequence AC111403 differs from that shown. Reason: Frameshift at position 78. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311L → V in BF413866 (Ref. 2) Curated
Sequence conflicti155 – 1551E → K in BF413866 (Ref. 2) Curated
Sequence conflicti162 – 1621E → K in BF413866 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC111403 mRNA. No translation available.
BF413866 mRNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC111403 mRNA. No translation available.
BF413866 mRNA. No translation available.

3D structure databases

ProteinModelPortaliP58200.
SMRiP58200. Positions 1-96, 139-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP58200. 2 interactions.
STRINGi10116.ENSRNOP00000015814.

Proteomic databases

PaxDbiP58200.
PRIDEiP58200.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi2323682. Vti1b.

Phylogenomic databases

eggNOGiKOG1666. Eukaryota.
ENOG4111J90. LUCA.
HOGENOMiHOG000116573.
HOVERGENiHBG058837.
InParanoidiP58200.
PhylomeDBiP58200.

Miscellaneous databases

PROiP58200.

Family and domain databases

InterProiIPR027027. GOSR2/Membrin/Bos1.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
IPR007705. Vesicle_trsprt_v-SNARE_N.
[Graphical view]
PfamiPF05008. V-SNARE. 1 hit.
[Graphical view]
PIRSFiPIRSF028865. Membrin-2. 1 hit.
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Soares M.B.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-163.
    Strain: Sprague-Dawley.
  3. "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function."
    Antonin W., Holroyd C., Fasshauer D., Pabst S., Fischer von Mollard G., Jahn R.
    EMBO J. 19:6453-6464(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SNARE COMPLEX CHARACTERIZATION.
  4. "Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late endocytic fusion events."
    Pryor P.R., Mullock B.M., Bright N.A., Lindsay M.R., Gray S.R., Richardson S.C.W., Stewart A., James D.E., Piper R.C., Luzio J.P.
    EMBO Rep. 5:590-595(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SNARE COMPLEX CHARACTERIZATION.

Entry informationi

Entry nameiVTI1B_RAT
AccessioniPrimary (citable) accession number: P58200
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 23, 2007
Last modified: May 11, 2016
This is version 91 of the entry and version 2 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. 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.