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Vesicle transport through interaction with t-SNAREs homolog 1B (Vesicle transport v-SNARE protein Vti1-like 1) (Vti1-rp1)

 VTI1B_HUMAN             Reviewed;         232 AA.
Q9UEU0; O43547; Q96J28;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 3.
25-OCT-2017, entry version 156.
RecName: Full=Vesicle transport through interaction with t-SNAREs homolog 1B;
AltName: Full=Vesicle transport v-SNARE protein Vti1-like 1;
AltName: Full=Vti1-rp1;
Name=VTI1B; Synonyms=VTI1, VTI1L, VTI1L1, VTI2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
TISSUE=Glioblastoma, and Hypothalamus;
PubMed=9446565; DOI=10.1074/jbc.273.5.2624;
Fischer von Mollard G., Stevens T.H.;
"A human homolog can functionally replace the yeast vesicle-associated
SNARE Vti1p in two vesicle transport pathways.";
J. Biol. Chem. 273:2624-2630(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Fibroblast;
PubMed=9636656; DOI=10.1006/bbrc.1998.8737;
Li H.-C., Tahara H., Tsuyama N., Ide T.;
"A hVti1 homologue: its expression depends on population doubling
levels in both normal and SV40-transformed human fibroblasts.";
Biochem. Biophys. Res. Commun. 247:70-74(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH STX17.
PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
Itakura E., Kishi-Itakura C., Mizushima N.;
"The hairpin-type tail-anchored SNARE syntaxin 17 targets to
autophagosomes for fusion with endosomes/lysosomes.";
Cell 151:1256-1269(2012).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND SER-138, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-107, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[16]
X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-96 IN COMPLEX WITH CLINT1,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-8; GLU-12; ILE-17;
GLU-23; GLU-65; PHE-73; PRO-76 AND MET-77.
PubMed=18033301; DOI=10.1038/nature06353;
Miller S.E., Collins B.M., McCoy A.J., Robinson M.S., Owen D.J.;
"A SNARE-adaptor interaction is a new mode of cargo recognition in
clathrin-coated vesicles.";
Nature 450:570-574(2007).
-!- 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.
May be concerned with increased secretion of cytokines associated
with cellular senescence. {ECO:0000269|PubMed:23217709}.
-!- SUBUNIT: 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). May interact with STX17 (PubMed:23217709).
Interacts with CLINT1 (PubMed:18033301).
{ECO:0000250|UniProtKB:O88384, ECO:0000269|PubMed:18033301,
ECO:0000269|PubMed:23217709}.
-!- INTERACTION:
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-723716, EBI-10172290;
Q5T700:LDLRAD1; NbExp=5; IntAct=EBI-723716, EBI-10173166;
P54829:PTPN5; NbExp=3; IntAct=EBI-723716, EBI-1220572;
Q12846:STX4; NbExp=5; IntAct=EBI-723716, EBI-744942;
Q9UNK0:STX8; NbExp=6; IntAct=EBI-723716, EBI-727240;
Q8N205:SYNE4; NbExp=3; IntAct=EBI-723716, EBI-7131783;
Q8IWR1:TRIM59; NbExp=5; IntAct=EBI-723716, EBI-10262539;
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:18033301}; Single-pass type IV membrane
protein {ECO:0000255}. Late endosome membrane
{ECO:0000269|PubMed:18033301, ECO:0000269|PubMed:23217709};
Single-pass type IV membrane protein
{ECO:0000269|PubMed:23217709}. Lysosome membrane
{ECO:0000269|PubMed:18033301, ECO:0000269|PubMed:23217709}.
Cytoplasmic granule {ECO:0000269|PubMed:23217709}. Recycling
endosome membrane {ECO:0000269|PubMed:18033301}; Single-pass type
IV membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q9UEU0-1; Sequence=Displayed;
Name=Short;
IsoId=Q9UEU0-2; Sequence=VSP_006753;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined.
-!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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EMBL; AF035824; AAC52016.1; -; mRNA.
EMBL; AF060902; AAC73059.1; -; mRNA.
EMBL; CR456757; CAG33038.1; -; mRNA.
EMBL; CR542095; CAG46892.1; -; mRNA.
EMBL; BT019348; AAV38155.1; -; mRNA.
EMBL; BC003142; AAH03142.1; -; mRNA.
CCDS; CCDS9786.1; -. [Q9UEU0-1]
RefSeq; NP_006361.1; NM_006370.2. [Q9UEU0-1]
UniGene; Hs.741177; -.
PDB; 2V8S; X-ray; 2.22 A; V=1-96.
PDBsum; 2V8S; -.
ProteinModelPortal; Q9UEU0; -.
SMR; Q9UEU0; -.
BioGrid; 115753; 97.
CORUM; Q9UEU0; -.
IntAct; Q9UEU0; 27.
MINT; MINT-1429590; -.
STRING; 9606.ENSP00000450731; -.
iPTMnet; Q9UEU0; -.
PhosphoSitePlus; Q9UEU0; -.
SwissPalm; Q9UEU0; -.
BioMuta; VTI1B; -.
DMDM; 126302613; -.
EPD; Q9UEU0; -.
PaxDb; Q9UEU0; -.
PeptideAtlas; Q9UEU0; -.
PRIDE; Q9UEU0; -.
TopDownProteomics; Q9UEU0-1; -. [Q9UEU0-1]
TopDownProteomics; Q9UEU0-2; -. [Q9UEU0-2]
DNASU; 10490; -.
Ensembl; ENST00000554659; ENSP00000450731; ENSG00000100568. [Q9UEU0-1]
GeneID; 10490; -.
KEGG; hsa:10490; -.
UCSC; uc001xjt.4; human. [Q9UEU0-1]
CTD; 10490; -.
DisGeNET; 10490; -.
EuPathDB; HostDB:ENSG00000100568.10; -.
GeneCards; VTI1B; -.
HGNC; HGNC:17793; VTI1B.
HPA; HPA044121; -.
HPA; HPA048150; -.
HPA; HPA060118; -.
MIM; 603207; gene.
neXtProt; NX_Q9UEU0; -.
OpenTargets; ENSG00000100568; -.
PharmGKB; PA134861090; -.
eggNOG; KOG1666; Eukaryota.
eggNOG; ENOG4111J90; LUCA.
GeneTree; ENSGT00530000063466; -.
HOGENOM; HOG000116573; -.
HOVERGEN; HBG058837; -.
InParanoid; Q9UEU0; -.
KO; K08493; -.
OMA; EELKYAP; -.
OrthoDB; EOG091G12XX; -.
PhylomeDB; Q9UEU0; -.
TreeFam; TF312874; -.
Reactome; R-HSA-114608; Platelet degranulation.
ChiTaRS; VTI1B; human.
EvolutionaryTrace; Q9UEU0; -.
GeneWiki; VTI1B; -.
GenomeRNAi; 10490; -.
PRO; PR:Q9UEU0; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100568; -.
ExpressionAtlas; Q9UEU0; baseline and differential.
Genevisible; Q9UEU0; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0019869; F:chloride channel inhibitor activity; IDA:UniProtKB.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0000149; F:SNARE binding; IDA:MGI.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
GO; GO:0006904; P:vesicle docking involved in exocytosis; TAS:ProtInc.
GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
InterPro; IPR010989; SNARE.
InterPro; IPR000727; T_SNARE_dom.
InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
Pfam; PF05008; V-SNARE; 1.
SMART; SM00397; t_SNARE; 1.
SUPFAM; SSF47661; SSF47661; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Endosome; Lysosome; Membrane; Methylation;
Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712}.
CHAIN 2 232 Vesicle transport through interaction
with t-SNAREs homolog 1B.
/FTId=PRO_0000218228.
TOPO_DOM 2 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 230 232 Vesicular. {ECO:0000255}.
REGION 2 23 Interaction with CLINT1.
{ECO:0000244|PDB:2V8S,
ECO:0000269|PubMed:18033301}.
REGION 69 73 Interaction with CLINT1.
{ECO:0000244|PDB:2V8S,
ECO:0000269|PubMed:18033301}.
COILED 35 98 {ECO:0000255}.
COILED 161 198 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712}.
MOD_RES 103 103 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 107 107 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 61 Missing (in isoform Short).
{ECO:0000303|PubMed:9446565}.
/FTId=VSP_006753.
MUTAGEN 8 8 S->W: Abolished binding to CLINT1.
{ECO:0000269|PubMed:18033301}.
MUTAGEN 12 12 E->A: Abolished binding to CLINT1.
Abnormal subcellular localization
restricted to late endosomes and
lysosomes. {ECO:0000269|PubMed:18033301}.
MUTAGEN 17 17 I->S: Normal binding to CLINT1.
{ECO:0000269|PubMed:18033301}.
MUTAGEN 23 23 E->R: Abolished binding to CLINT1.
Rescued binding to CLINT1 E-146 mutant.
{ECO:0000269|PubMed:18033301}.
MUTAGEN 65 65 E->W: Abolished binding to CLINT1.
{ECO:0000269|PubMed:18033301}.
MUTAGEN 73 73 F->S: Abolished binding to CLINT1.
Abnormal subcellular localization
restricted to late endosomes and
lysosomes. {ECO:0000269|PubMed:18033301}.
MUTAGEN 76 76 P->S: Reduced binding to CLINT1.
{ECO:0000269|PubMed:18033301}.
MUTAGEN 77 77 M->S: Normal binding to CLINT1.
{ECO:0000269|PubMed:18033301}.
CONFLICT 24 24 D -> N (in Ref. 1; AAC52016).
{ECO:0000305}.
TURN 4 6 {ECO:0000244|PDB:2V8S}.
HELIX 9 26 {ECO:0000244|PDB:2V8S}.
TURN 29 31 {ECO:0000244|PDB:2V8S}.
STRAND 32 34 {ECO:0000244|PDB:2V8S}.
HELIX 39 66 {ECO:0000244|PDB:2V8S}.
HELIX 71 93 {ECO:0000244|PDB:2V8S}.
SEQUENCE 232 AA; 26688 MW; B421C2863235B9B1 CRC64;
MASSAASSEH FEKLHEIFRG LHEDLQGVPE RLLGTAGTEE KKKLIRDFDE KQQEANETLA
EMEEELRYAP LSFRNPMMSK LRNYRKDLAK LHREVRSTPL TATPGGRGDM KYGIYAVENE
HMNRLQSQRA MLLQGTESLN RATQSIERSH RIATETDQIG SEIIEELGEQ RDQLERTKSR
LVNTSENLSK SRKILRSMSR KVTTNKLLLS IIILLELAIL GGLVYYKFFR SH


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