VTI1B_MOUSE
ID VTI1B_MOUSE Reviewed; 232 AA.
AC O88384;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 143.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9553086; DOI=10.1074/jbc.273.17.10317;
RA Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R.,
RA Yoo J.-S., Scheller R.H.;
RT "Seven novel mammalian SNARE proteins localize to distinct membrane
RT compartments.";
RL J. Biol. Chem. 273:10317-10324(1998).
RN [2]
RP IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX7.
RX PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.;
RT "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar
RT cells.";
RL Dev. Cell 7:359-371(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 140-200 IN COMPLEX WITH STX7; STX8
RP AND VAMP8.
RX PubMed=11786915; DOI=10.1038/nsb746;
RA Antonin W., Fasshauer D., Becker S., Jahn R., Schneider T.R.;
RT "Crystal structure of the endosomal SNARE complex reveals common structural
RT principles of all SNAREs.";
RL Nat. Struct. Biol. 9:107-111(2002).
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:15363411}.
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
CC (PubMed:11786915, PubMed:15363411). May interact with STX17. Interacts
CC with CLINT1 (By similarity). {ECO:0000250|UniProtKB:Q9UEU0,
CC ECO:0000269|PubMed:11786915, ECO:0000269|PubMed:15363411}.
CC -!- INTERACTION:
CC O88384; P70280: Vamp7; NbExp=9; IntAct=EBI-775853, EBI-6555653;
CC O88384; Q14677: CLINT1; Xeno; NbExp=6; IntAct=EBI-775853, EBI-1171113;
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 -!- TISSUE SPECIFICITY: Broadly expressed.
CC -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR EMBL; AF035208; AAC23483.1; -; mRNA.
DR CCDS; CCDS26008.1; -.
DR PDB; 1GL2; X-ray; 1.90 A; C=140-200.
DR PDB; 2QYW; X-ray; 2.00 A; A=1-96.
DR PDBsum; 1GL2; -.
DR PDBsum; 2QYW; -.
DR AlphaFoldDB; O88384; -.
DR SMR; O88384; -.
DR CORUM; O88384; -.
DR DIP; DIP-32212N; -.
DR IntAct; O88384; 12.
DR MINT; O88384; -.
DR STRING; 10090.ENSMUSP00000057462; -.
DR iPTMnet; O88384; -.
DR PhosphoSitePlus; O88384; -.
DR SwissPalm; O88384; -.
DR EPD; O88384; -.
DR jPOST; O88384; -.
DR MaxQB; O88384; -.
DR PaxDb; O88384; -.
DR PeptideAtlas; O88384; -.
DR PRIDE; O88384; -.
DR ProteomicsDB; 297616; -.
DR UCSC; uc007nzy.2; mouse.
DR MGI; MGI:1855688; Vti1b.
DR eggNOG; KOG1666; Eukaryota.
DR InParanoid; O88384; -.
DR PhylomeDB; O88384; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR ChiTaRS; Vti1b; mouse.
DR EvolutionaryTrace; O88384; -.
DR PRO; PR:O88384; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88384; protein.
DR GO; GO:0031225; C:anchored component of membrane; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
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:MGI.
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; 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 SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Endosome; Lysosome; Membrane;
KW Methylation; Phosphoprotein; Protein transport; Reference proteome;
KW Transmembrane; 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_0000218229"
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 107
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEU0"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT HELIX 2..33
FT /evidence="ECO:0007829|PDB:2QYW"
FT HELIX 39..67
FT /evidence="ECO:0007829|PDB:2QYW"
FT HELIX 71..95
FT /evidence="ECO:0007829|PDB:2QYW"
FT HELIX 141..196
FT /evidence="ECO:0007829|PDB:1GL2"
SQ SEQUENCE 232 AA; 26713 MW; 6827DCAF9650DFC6 CRC64;
MAASAASSEH FEKLHEIFRG LLEDLQGVPE RLLGTAGTEE KKKLVRDFDE NQQEANETLA
EMEEELRYAP LTFRNPMMSK LRNYRKDLAK LHREVRSTPL TAAPGGRGDL KYGTYTLENE
HLNRLQSQRA LLLQGTESLN RATQSIERSH RIATETDQIG TEIIEELGEQ RDQLERTKSR
LVNTNENLSK SRKILRSMSR KVITNKLLLS VIILLELAIL VGLVYYKFFR HH
