ID   VTI1B_HUMAN             Reviewed;         232 AA.
AC   Q9UEU0; O43547; Q96J28;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 3.
DT   27-MAR-2024, entry version 198.
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=VTI1, VTI1L, VTI1L1, VTI2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   TISSUE=Glioblastoma, and Hypothalamus;
RX   PubMed=9446565; DOI=10.1074/jbc.273.5.2624;
RA   Fischer von Mollard G., Stevens T.H.;
RT   "A human homolog can functionally replace the yeast vesicle-associated
RT   SNARE Vti1p in two vesicle transport pathways.";
RL   J. Biol. Chem. 273:2624-2630(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   TISSUE=Fibroblast;
RX   PubMed=9636656; DOI=10.1006/bbrc.1998.8737;
RA   Li H.-C., Tahara H., Tsuyama N., Ide T.;
RT   "A hVti1 homologue: its expression depends on population doubling levels in
RT   both normal and SV40-transformed human fibroblasts.";
RL   Biochem. Biophys. Res. Commun. 247:70-74(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH STX17.
RX   PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
RA   Itakura E., Kishi-Itakura C., Mizushima N.;
RT   "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes
RT   for fusion with endosomes/lysosomes.";
RL   Cell 151:1256-1269(2012).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND SER-138, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-107, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-96 IN COMPLEX WITH CLINT1,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-8; GLU-12; ILE-17; GLU-23;
RP   GLU-65; PHE-73; PRO-76 AND MET-77.
RX   PubMed=18033301; DOI=10.1038/nature06353;
RA   Miller S.E., Collins B.M., McCoy A.J., Robinson M.S., Owen D.J.;
RT   "A SNARE-adaptor interaction is a new mode of cargo recognition in
RT   clathrin-coated vesicles.";
RL   Nature 450:570-574(2007).
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. May be
CC       concerned with increased secretion of cytokines associated with
CC       cellular senescence. {ECO:0000269|PubMed:23217709}.
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 (PubMed:23217709). Interacts with
CC       CLINT1 (PubMed:18033301). {ECO:0000250|UniProtKB:O88384,
CC       ECO:0000269|PubMed:18033301, ECO:0000269|PubMed:23217709}.
CC   -!- INTERACTION:
CC       Q9UEU0; Q13520: AQP6; NbExp=3; IntAct=EBI-723716, EBI-13059134;
CC       Q9UEU0; P07307-3: ASGR2; NbExp=3; IntAct=EBI-723716, EBI-12808270;
CC       Q9UEU0; P15529-3: CD46; NbExp=3; IntAct=EBI-723716, EBI-13046140;
CC       Q9UEU0; P11912: CD79A; NbExp=3; IntAct=EBI-723716, EBI-7797864;
CC       Q9UEU0; P13569: CFTR; NbExp=10; IntAct=EBI-723716, EBI-349854;
CC       Q9UEU0; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-723716, EBI-17233035;
CC       Q9UEU0; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-723716, EBI-781551;
CC       Q9UEU0; P12314: FCGR1A; NbExp=3; IntAct=EBI-723716, EBI-2869867;
CC       Q9UEU0; Q8TED1: GPX8; NbExp=3; IntAct=EBI-723716, EBI-11721746;
CC       Q9UEU0; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-723716, EBI-10266796;
CC       Q9UEU0; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-723716, EBI-749265;
CC       Q9UEU0; P26715: KLRC1; NbExp=3; IntAct=EBI-723716, EBI-9018187;
CC       Q9UEU0; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-723716, EBI-10172290;
CC       Q9UEU0; Q5T700: LDLRAD1; NbExp=8; IntAct=EBI-723716, EBI-10173166;
CC       Q9UEU0; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-723716, EBI-3867271;
CC       Q9UEU0; P54829: PTPN5; NbExp=4; IntAct=EBI-723716, EBI-1220572;
CC       Q9UEU0; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-723716, EBI-7545592;
CC       Q9UEU0; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-723716, EBI-18397230;
CC       Q9UEU0; O60669: SLC16A7; NbExp=3; IntAct=EBI-723716, EBI-3921243;
CC       Q9UEU0; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-723716, EBI-17295964;
CC       Q9UEU0; Q16623: STX1A; NbExp=3; IntAct=EBI-723716, EBI-712466;
CC       Q9UEU0; P32856-2: STX2; NbExp=3; IntAct=EBI-723716, EBI-11956649;
CC       Q9UEU0; Q12846: STX4; NbExp=6; IntAct=EBI-723716, EBI-744942;
CC       Q9UEU0; Q9UNK0: STX8; NbExp=7; IntAct=EBI-723716, EBI-727240;
CC       Q9UEU0; Q8N205: SYNE4; NbExp=4; IntAct=EBI-723716, EBI-7131783;
CC       Q9UEU0; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-723716, EBI-8638294;
CC       Q9UEU0; Q8WY98: TMEM234; NbExp=3; IntAct=EBI-723716, EBI-8642211;
CC       Q9UEU0; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-723716, EBI-726044;
CC       Q9UEU0; Q8IWR1: TRIM59; NbExp=9; IntAct=EBI-723716, EBI-10262539;
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000269|PubMed:18033301}; Single-pass type IV membrane protein
CC       {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:18033301,
CC       ECO:0000269|PubMed:23217709}; Single-pass type IV membrane protein
CC       {ECO:0000269|PubMed:23217709}. Lysosome membrane
CC       {ECO:0000269|PubMed:18033301, ECO:0000269|PubMed:23217709}. Cytoplasmic
CC       granule {ECO:0000269|PubMed:23217709}. Recycling endosome membrane
CC       {ECO:0000269|PubMed:18033301}; Single-pass type IV membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q9UEU0-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q9UEU0-2; Sequence=VSP_006753;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC   -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR   EMBL; AF035824; AAC52016.1; -; mRNA.
DR   EMBL; AF060902; AAC73059.1; -; mRNA.
DR   EMBL; CR456757; CAG33038.1; -; mRNA.
DR   EMBL; CR542095; CAG46892.1; -; mRNA.
DR   EMBL; BT019348; AAV38155.1; -; mRNA.
DR   EMBL; BC003142; AAH03142.1; -; mRNA.
DR   CCDS; CCDS9786.1; -. [Q9UEU0-1]
DR   RefSeq; NP_006361.1; NM_006370.2. [Q9UEU0-1]
DR   PDB; 2V8S; X-ray; 2.22 A; V=1-96.
DR   PDBsum; 2V8S; -.
DR   AlphaFoldDB; Q9UEU0; -.
DR   SMR; Q9UEU0; -.
DR   BioGRID; 115753; 202.
DR   CORUM; Q9UEU0; -.
DR   IntAct; Q9UEU0; 121.
DR   MINT; Q9UEU0; -.
DR   STRING; 9606.ENSP00000450731; -.
DR   TCDB; 1.F.1.1.5; the synaptosomal vesicle fusion pore (svf-pore) family.
DR   GlyCosmos; Q9UEU0; 2 sites, 1 glycan.
DR   GlyGen; Q9UEU0; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9UEU0; -.
DR   PhosphoSitePlus; Q9UEU0; -.
DR   SwissPalm; Q9UEU0; -.
DR   BioMuta; VTI1B; -.
DR   DMDM; 126302613; -.
DR   EPD; Q9UEU0; -.
DR   jPOST; Q9UEU0; -.
DR   MassIVE; Q9UEU0; -.
DR   MaxQB; Q9UEU0; -.
DR   PaxDb; 9606-ENSP00000450731; -.
DR   PeptideAtlas; Q9UEU0; -.
DR   ProteomicsDB; 84155; -. [Q9UEU0-1]
DR   ProteomicsDB; 84156; -. [Q9UEU0-2]
DR   Pumba; Q9UEU0; -.
DR   TopDownProteomics; Q9UEU0-1; -. [Q9UEU0-1]
DR   TopDownProteomics; Q9UEU0-2; -. [Q9UEU0-2]
DR   Antibodypedia; 24876; 277 antibodies from 33 providers.
DR   DNASU; 10490; -.
DR   Ensembl; ENST00000554659.6; ENSP00000450731.1; ENSG00000100568.11. [Q9UEU0-1]
DR   GeneID; 10490; -.
DR   KEGG; hsa:10490; -.
DR   MANE-Select; ENST00000554659.6; ENSP00000450731.1; NM_006370.3; NP_006361.1.
DR   UCSC; uc001xjt.4; human. [Q9UEU0-1]
DR   AGR; HGNC:17793; -.
DR   CTD; 10490; -.
DR   DisGeNET; 10490; -.
DR   GeneCards; VTI1B; -.
DR   HGNC; HGNC:17793; VTI1B.
DR   HPA; ENSG00000100568; Low tissue specificity.
DR   MIM; 603207; gene.
DR   neXtProt; NX_Q9UEU0; -.
DR   OpenTargets; ENSG00000100568; -.
DR   PharmGKB; PA134861090; -.
DR   VEuPathDB; HostDB:ENSG00000100568; -.
DR   eggNOG; KOG1666; Eukaryota.
DR   GeneTree; ENSGT00950000183192; -.
DR   HOGENOM; CLU_075474_2_0_1; -.
DR   InParanoid; Q9UEU0; -.
DR   OMA; KLRMYRR; -.
DR   OrthoDB; 2908325at2759; -.
DR   PhylomeDB; Q9UEU0; -.
DR   TreeFam; TF312874; -.
DR   PathwayCommons; Q9UEU0; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   SignaLink; Q9UEU0; -.
DR   BioGRID-ORCS; 10490; 143 hits in 1158 CRISPR screens.
DR   ChiTaRS; VTI1B; human.
DR   EvolutionaryTrace; Q9UEU0; -.
DR   GeneWiki; VTI1B; -.
DR   GenomeRNAi; 10490; -.
DR   Pharos; Q9UEU0; Tbio.
DR   PRO; PR:Q9UEU0; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9UEU0; Protein.
DR   Bgee; ENSG00000100568; Expressed in C1 segment of cervical spinal cord and 205 other cell types or tissues.
DR   ExpressionAtlas; Q9UEU0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
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:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR   GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR   GO; GO:0019869; F:chloride channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IDA: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:0061025; P:membrane fusion; TAS:ProtInc.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; TAS:ProtInc.
DR   GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR   CDD; cd15890; SNARE_Vti1b; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 1.20.58.400; t-snare proteins; 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   PANTHER; PTHR21230:SF104; VESICLE TRANSPORT THROUGH INTERACTION WITH T-SNARES HOMOLOG 1B; 1.
DR   PANTHER; PTHR21230; VESICLE TRANSPORT V-SNARE PROTEIN VTI1-RELATED; 1.
DR   Pfam; PF05008; V-SNARE; 1.
DR   Pfam; PF12352; V-SNARE_C; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   Genevisible; Q9UEU0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil; Endosome;
KW   Lysosome; Membrane; Methylation; Phosphoprotein; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT   CHAIN           2..232
FT                   /note="Vesicle transport through interaction with t-SNAREs
FT                   homolog 1B"
FT                   /id="PRO_0000218228"
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:0000269|PubMed:18033301,
FT                   ECO:0007744|PDB:2V8S"
FT   REGION          69..73
FT                   /note="Interaction with CLINT1"
FT                   /evidence="ECO:0000269|PubMed:18033301,
FT                   ECO:0007744|PDB:2V8S"
FT   COILED          35..98
FT                   /evidence="ECO:0000255"
FT   COILED          161..198
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT   MOD_RES         103
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         107
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..61
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:9446565"
FT                   /id="VSP_006753"
FT   MUTAGEN         8
FT                   /note="S->W: Abolished binding to CLINT1."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   MUTAGEN         12
FT                   /note="E->A: Abolished binding to CLINT1. Abnormal
FT                   subcellular localization restricted to late endosomes and
FT                   lysosomes."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   MUTAGEN         17
FT                   /note="I->S: Normal binding to CLINT1."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   MUTAGEN         23
FT                   /note="E->R: Abolished binding to CLINT1. Rescued binding
FT                   to CLINT1 E-146 mutant."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   MUTAGEN         65
FT                   /note="E->W: Abolished binding to CLINT1."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   MUTAGEN         73
FT                   /note="F->S: Abolished binding to CLINT1. Abnormal
FT                   subcellular localization restricted to late endosomes and
FT                   lysosomes."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   MUTAGEN         76
FT                   /note="P->S: Reduced binding to CLINT1."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   MUTAGEN         77
FT                   /note="M->S: Normal binding to CLINT1."
FT                   /evidence="ECO:0000269|PubMed:18033301"
FT   CONFLICT        24
FT                   /note="D -> N (in Ref. 1; AAC52016)"
FT                   /evidence="ECO:0000305"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:2V8S"
FT   HELIX           9..26
FT                   /evidence="ECO:0007829|PDB:2V8S"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:2V8S"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:2V8S"
FT   HELIX           39..66
FT                   /evidence="ECO:0007829|PDB:2V8S"
FT   HELIX           71..93
FT                   /evidence="ECO:0007829|PDB:2V8S"
SQ   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
//