VTI1B_HUMAN
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 03-AUG-2022, entry version 189.
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; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 186.
DR CORUM; Q9UEU0; -.
DR IntAct; Q9UEU0; 118.
DR MINT; Q9UEU0; -.
DR STRING; 9606.ENSP00000450731; -.
DR TCDB; 1.F.1.1.5; the synaptosomal vesicle fusion pore (svf-pore) family.
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; Q9UEU0; -.
DR PeptideAtlas; Q9UEU0; -.
DR PRIDE; Q9UEU0; -.
DR ProteomicsDB; 84155; -. [Q9UEU0-1]
DR ProteomicsDB; 84156; -. [Q9UEU0-2]
DR TopDownProteomics; Q9UEU0-1; -. [Q9UEU0-1]
DR TopDownProteomics; Q9UEU0-2; -. [Q9UEU0-2]
DR Antibodypedia; 24876; 251 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 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; 1195966at2759; -.
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 1080 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 203 other tissues.
DR ExpressionAtlas; Q9UEU0; baseline and differential.
DR Genevisible; Q9UEU0; HS.
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:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
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; 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
