VTI1B_RAT
ID VTI1B_RAT Reviewed; 232 AA.
AC P58200;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Vesicle transport through interaction with t-SNAREs homolog 1B;
DE AltName: Full=Vesicle transport v-SNARE protein Vti1-like 1;
DE AltName: Full=Vti1-rp1;
GN Name=Vti1b; Synonyms=Vti1l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-163.
RC STRAIN=Sprague-Dawley;
RA Soares M.B.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SNARE COMPLEX CHARACTERIZATION.
RX PubMed=11101518; DOI=10.1093/emboj/19.23.6453;
RA Antonin W., Holroyd C., Fasshauer D., Pabst S., Fischer von Mollard G.,
RA Jahn R.;
RT "A SNARE complex mediating fusion of late endosomes defines conserved
RT properties of SNARE structure and function.";
RL EMBO J. 19:6453-6464(2000).
RN [4]
RP SNARE COMPLEX CHARACTERIZATION.
RX PubMed=15133481; DOI=10.1038/sj.embor.7400150;
RA Pryor P.R., Mullock B.M., Bright N.A., Lindsay M.R., Gray S.R.,
RA Richardson S.C.W., Stewart A., James D.E., Piper R.C., Luzio J.P.;
RT "Combinatorial SNARE complexes with VAMP7 or VAMP8 define different late
RT endocytic fusion events.";
RL EMBO Rep. 5:590-595(2004).
CC -!- FUNCTION: V-SNARE that mediates vesicle transport pathways through
CC interactions with t-SNAREs on the target membrane. These interactions
CC are proposed to mediate aspects of the specificity of vesicle
CC trafficking and to promote fusion of the lipid bilayers.
CC {ECO:0000305|PubMed:11101518, ECO:0000305|PubMed:15133481}.
CC -!- SUBUNIT: Forms a SNARE complex with STX7, STX8 and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Component of the
CC SNARE complex composed of STX7, STX8, VAMP7 and VIT1B that is required
CC for heterotypic fusion of late endosomes with lysosomes (By
CC similarity). May interact with STX17. Interacts with CLINT1 (By
CC similarity). {ECO:0000250|UniProtKB:O88384,
CC ECO:0000250|UniProtKB:Q9UEU0}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q9UEU0};
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9UEU0}.
CC Lysosome membrane {ECO:0000250|UniProtKB:Q9UEU0}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q9UEU0}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9UEU0}; Single-pass type IV membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AC111403; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC111403; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BF413866; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P58200; -.
DR SMR; P58200; -.
DR CORUM; P58200; -.
DR IntAct; P58200; 3.
DR MINT; P58200; -.
DR STRING; 10116.ENSRNOP00000015814; -.
DR jPOST; P58200; -.
DR PaxDb; P58200; -.
DR PRIDE; P58200; -.
DR Ensembl; ENSRNOT00000090407; ENSRNOP00000070613; ENSRNOG00000060436.
DR RGD; 2323682; Vti1b.
DR eggNOG; KOG1666; Eukaryota.
DR GeneTree; ENSGT00950000183192; -.
DR InParanoid; P58200; -.
DR PhylomeDB; P58200; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:P58200; -.
DR Proteomes; UP000002494; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; ISO:RGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR Gene3D; 1.20.58.400; -; 1.
DR InterPro; IPR027027; GOSR2/Membrin/Bos1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR038407; v-SNARE_N_sf.
DR InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
DR Pfam; PF05008; V-SNARE; 1.
DR PIRSF; PIRSF028865; Membrin-2; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Endosome; Lysosome; Membrane; Methylation;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT CHAIN 2..232
FT /note="Vesicle transport through interaction with t-SNAREs
FT homolog 1B"
FT /id="PRO_0000218230"
FT TOPO_DOM 2..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..232
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT REGION 2..23
FT /note="Interaction with CLINT1"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT REGION 69..73
FT /note="Interaction with CLINT1"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT COILED 36..98
FT /evidence="ECO:0000255"
FT COILED 160..201
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT MOD_RES 107
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT CONFLICT 131
FT /note="L -> V (in Ref. 2; BF413866)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> K (in Ref. 2; BF413866)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="E -> K (in Ref. 2; BF413866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 26703 MW; 017363526CE3B9EA CRC64;
MATSAASSEH FEKLHEIFRG LLEDLQGVPE RLLGTAGTEE KKKLVRDFDE KQQEANETLA
EMEEELRYAP LTFRNSMMSK LRNYRKDLAK LHREVRSTPL TATPGGRGDL KFGTYTLENE
HLNRLQSQRA LLLQGTESLN RATQSIERSH RIAAETDQIG SEIIEELGEQ RDQLERTKSR
LVNTNENLSK SRKILRSMSR KVITNKLLLS VIIVLELAIL VGLVYYKFFR HH
