Full text data of VTI1B
VTI1B
(VTI1, VTI1L, VTI1L1, VTI2)
[Confidence: low (only semi-automatic identification from reviews)]
Vesicle transport through interaction with t-SNAREs homolog 1B (Vesicle transport v-SNARE protein Vti1-like 1; Vti1-rp1)
Vesicle transport through interaction with t-SNAREs homolog 1B (Vesicle transport v-SNARE protein Vti1-like 1; Vti1-rp1)
UniProt
Q9UEU0
ID VTI1B_HUMAN Reviewed; 232 AA.
AC Q9UEU0; O43547; Q96J28;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-FEB-2007, sequence version 3.
DT 22-JAN-2014, entry version 122.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT levels in 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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
RT 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
RT project: 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT autophagosomes for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
CC -!- FUNCTION: V-SNARE that mediates vesicle transport pathways through
CC interactions with t-SNAREs on the target membrane. These
CC interactions are proposed to mediate aspects of the specificity of
CC vesicle trafficking and to promote fusion of the lipid bilayers.
CC May be concerned with increased secretion of cytokines associated
CC with cellular senescence.
CC -!- SUBUNIT: Forms a SNARE complex with STX7, STX8 and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Component of
CC the SNARE complex composed of STX7, STX8, VAMP7 and VIT1B that is
CC required for heterotypic fusion of late endosomes with lysosomes
CC (By similarity). May interact with STX17.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Single-pass type IV
CC membrane protein. Lysosome membrane. Cytoplasmic granule.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_006361.1; NM_006370.2.
DR RefSeq; XP_005267323.1; XM_005267266.1.
DR UniGene; Hs.741177; -.
DR PDB; 2V8S; X-ray; 2.22 A; V=1-96.
DR PDBsum; 2V8S; -.
DR ProteinModelPortal; Q9UEU0; -.
DR SMR; Q9UEU0; 2-94, 139-197.
DR IntAct; Q9UEU0; 5.
DR MINT; MINT-1429590; -.
DR STRING; 9606.ENSP00000216456; -.
DR PhosphoSite; Q9UEU0; -.
DR DMDM; 126302613; -.
DR PaxDb; Q9UEU0; -.
DR PRIDE; Q9UEU0; -.
DR DNASU; 10490; -.
DR Ensembl; ENST00000554659; ENSP00000450731; ENSG00000100568.
DR GeneID; 10490; -.
DR KEGG; hsa:10490; -.
DR UCSC; uc001xjt.3; human.
DR CTD; 10490; -.
DR GeneCards; GC14M068117; -.
DR HGNC; HGNC:17793; VTI1B.
DR MIM; 603207; gene.
DR neXtProt; NX_Q9UEU0; -.
DR PharmGKB; PA134861090; -.
DR eggNOG; NOG291765; -.
DR HOGENOM; HOG000116573; -.
DR HOVERGEN; HBG058837; -.
DR InParanoid; Q9UEU0; -.
DR KO; K08493; -.
DR OMA; MMSKLRT; -.
DR OrthoDB; EOG70KGQQ; -.
DR PhylomeDB; Q9UEU0; -.
DR ChiTaRS; VTI1B; human.
DR EvolutionaryTrace; Q9UEU0; -.
DR GeneWiki; VTI1B; -.
DR GenomeRNAi; 10490; -.
DR NextBio; 39804; -.
DR PRO; PR:Q9UEU0; -.
DR ArrayExpress; Q9UEU0; -.
DR Bgee; Q9UEU0; -.
DR Genevestigator; Q9UEU0; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; TAS:ProtInc.
DR InterPro; IPR010989; t-SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
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;
KW Complete proteome; Endosome; Lysosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 232 Vesicle transport through interaction
FT with t-SNAREs homolog 1B.
FT /FTId=PRO_0000218228.
FT TOPO_DOM 2 208 Cytoplasmic (Potential).
FT TRANSMEM 209 229 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 230 232 Vesicular (Potential).
FT COILED 35 98 Potential.
FT COILED 161 198 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 138 138 Phosphoserine (By similarity).
FT VAR_SEQ 1 61 Missing (in isoform Short).
FT /FTId=VSP_006753.
FT CONFLICT 24 24 D -> N (in Ref. 1; AAC52016).
FT TURN 4 6
FT HELIX 9 26
FT TURN 29 31
FT STRAND 32 34
FT HELIX 39 66
FT HELIX 71 93
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
//
ID VTI1B_HUMAN Reviewed; 232 AA.
AC Q9UEU0; O43547; Q96J28;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-FEB-2007, sequence version 3.
DT 22-JAN-2014, entry version 122.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT levels in 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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
RT 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
RT project: 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT autophagosomes for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
CC -!- FUNCTION: V-SNARE that mediates vesicle transport pathways through
CC interactions with t-SNAREs on the target membrane. These
CC interactions are proposed to mediate aspects of the specificity of
CC vesicle trafficking and to promote fusion of the lipid bilayers.
CC May be concerned with increased secretion of cytokines associated
CC with cellular senescence.
CC -!- SUBUNIT: Forms a SNARE complex with STX7, STX8 and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Component of
CC the SNARE complex composed of STX7, STX8, VAMP7 and VIT1B that is
CC required for heterotypic fusion of late endosomes with lysosomes
CC (By similarity). May interact with STX17.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Single-pass type IV
CC membrane protein. Lysosome membrane. Cytoplasmic granule.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_006361.1; NM_006370.2.
DR RefSeq; XP_005267323.1; XM_005267266.1.
DR UniGene; Hs.741177; -.
DR PDB; 2V8S; X-ray; 2.22 A; V=1-96.
DR PDBsum; 2V8S; -.
DR ProteinModelPortal; Q9UEU0; -.
DR SMR; Q9UEU0; 2-94, 139-197.
DR IntAct; Q9UEU0; 5.
DR MINT; MINT-1429590; -.
DR STRING; 9606.ENSP00000216456; -.
DR PhosphoSite; Q9UEU0; -.
DR DMDM; 126302613; -.
DR PaxDb; Q9UEU0; -.
DR PRIDE; Q9UEU0; -.
DR DNASU; 10490; -.
DR Ensembl; ENST00000554659; ENSP00000450731; ENSG00000100568.
DR GeneID; 10490; -.
DR KEGG; hsa:10490; -.
DR UCSC; uc001xjt.3; human.
DR CTD; 10490; -.
DR GeneCards; GC14M068117; -.
DR HGNC; HGNC:17793; VTI1B.
DR MIM; 603207; gene.
DR neXtProt; NX_Q9UEU0; -.
DR PharmGKB; PA134861090; -.
DR eggNOG; NOG291765; -.
DR HOGENOM; HOG000116573; -.
DR HOVERGEN; HBG058837; -.
DR InParanoid; Q9UEU0; -.
DR KO; K08493; -.
DR OMA; MMSKLRT; -.
DR OrthoDB; EOG70KGQQ; -.
DR PhylomeDB; Q9UEU0; -.
DR ChiTaRS; VTI1B; human.
DR EvolutionaryTrace; Q9UEU0; -.
DR GeneWiki; VTI1B; -.
DR GenomeRNAi; 10490; -.
DR NextBio; 39804; -.
DR PRO; PR:Q9UEU0; -.
DR ArrayExpress; Q9UEU0; -.
DR Bgee; Q9UEU0; -.
DR Genevestigator; Q9UEU0; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; TAS:ProtInc.
DR InterPro; IPR010989; t-SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
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;
KW Complete proteome; Endosome; Lysosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 232 Vesicle transport through interaction
FT with t-SNAREs homolog 1B.
FT /FTId=PRO_0000218228.
FT TOPO_DOM 2 208 Cytoplasmic (Potential).
FT TRANSMEM 209 229 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 230 232 Vesicular (Potential).
FT COILED 35 98 Potential.
FT COILED 161 198 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 138 138 Phosphoserine (By similarity).
FT VAR_SEQ 1 61 Missing (in isoform Short).
FT /FTId=VSP_006753.
FT CONFLICT 24 24 D -> N (in Ref. 1; AAC52016).
FT TURN 4 6
FT HELIX 9 26
FT TURN 29 31
FT STRAND 32 34
FT HELIX 39 66
FT HELIX 71 93
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
//
MIM
603207
*RECORD*
*FIELD* NO
603207
*FIELD* TI
*603207 VTI1, S. CEREVISIAE, HOMOLOG OF, B; VTI1B
;;VTI1;;
VTI1-LIKE; VTI1L
*FIELD* TX
read more
CLONING
Membrane traffic in eukaryotic cells requires the interaction of a
vesicle-associated soluble NSF attachment protein receptor (v-SNARE) on
transport vesicles with a t-SNARE on the target membrane. See 603215.
Vti1 is an S. cerevisiae v-SNARE that is essential for viability. Vti1
participates both in Golgi to prevacuolar transport and in traffic to
the cis-Golgi. Using a multicopy suppressor screen to identity human
proteins that can functionally complement a yeast vti1 deletion mutant,
Fischer von Mollard and Stevens (1998) isolated a glioblastoma cDNA
encoding VTI1, a human homolog of yeast Vti1. The deduced 232-amino acid
human protein contains a C-terminal transmembrane domain and 2 predicted
coiled-coil regions. The yeast and human proteins are 29% identical.
Expression of human VTI1 in yeast indicated that VTI1 can replace yeast
Vti1 in both Golgi transport reactions. Northern blot analysis detected
a 1.2-kb VTI1 mRNA in all human tissues tested. Searches of an EST
database identified cDNAs encoding a mouse protein with 93% sequence
identity to human VTI1.
BIOCHEMICAL FEATURES
- Crystal Structure
Miller et al. (2007) characterized the molecular details governing the
sorting of a SNARE into clathrin-coated vesicles, namely, the direct
recognition of the 3-helical bundle H(abc) domain of the mouse SNARE
Vti1b by the human clathrin adaptor epsinR (EPNR, also known as CLINT1;
607265). Structures of each domain and of their complex showed that this
interaction (dissociation constant 22 microM) is mediated by surface
patches composed of approximately 15 residues each, the topographies of
which are dependent on each domain's overall fold. Disruption of the
interface with point mutations abolished the interaction in vitro and
caused Vti1b to become relocalized to late endosomes and lysosomes.
Miller et al. (2007) stated that this new class of highly specific,
surface-surface interaction between the clathrin coat component and the
cargo is distinct from the widely observed binding of short, linear
cargo motifs by the assembly polypeptide (AP) complex and GGA adaptors
and is therefore not vulnerable to competition from standard
motif-containing cargoes for incorporation into clathrin-coated
vesicles. Miller et al. (2007) proposed that conceptually similar but
mechanistically different interactions direct the post-Golgi trafficking
of many SNAREs.
*FIELD* RF
1. 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. 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.
*FIELD* CN
Ada Hamosh - updated: 4/22/2008
*FIELD* CD
Rebekah S. Rasooly: 10/26/1998
*FIELD* ED
alopez: 05/14/2008
terry: 4/22/2008
carol: 11/26/2002
psherman: 10/27/1998
*RECORD*
*FIELD* NO
603207
*FIELD* TI
*603207 VTI1, S. CEREVISIAE, HOMOLOG OF, B; VTI1B
;;VTI1;;
VTI1-LIKE; VTI1L
*FIELD* TX
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CLONING
Membrane traffic in eukaryotic cells requires the interaction of a
vesicle-associated soluble NSF attachment protein receptor (v-SNARE) on
transport vesicles with a t-SNARE on the target membrane. See 603215.
Vti1 is an S. cerevisiae v-SNARE that is essential for viability. Vti1
participates both in Golgi to prevacuolar transport and in traffic to
the cis-Golgi. Using a multicopy suppressor screen to identity human
proteins that can functionally complement a yeast vti1 deletion mutant,
Fischer von Mollard and Stevens (1998) isolated a glioblastoma cDNA
encoding VTI1, a human homolog of yeast Vti1. The deduced 232-amino acid
human protein contains a C-terminal transmembrane domain and 2 predicted
coiled-coil regions. The yeast and human proteins are 29% identical.
Expression of human VTI1 in yeast indicated that VTI1 can replace yeast
Vti1 in both Golgi transport reactions. Northern blot analysis detected
a 1.2-kb VTI1 mRNA in all human tissues tested. Searches of an EST
database identified cDNAs encoding a mouse protein with 93% sequence
identity to human VTI1.
BIOCHEMICAL FEATURES
- Crystal Structure
Miller et al. (2007) characterized the molecular details governing the
sorting of a SNARE into clathrin-coated vesicles, namely, the direct
recognition of the 3-helical bundle H(abc) domain of the mouse SNARE
Vti1b by the human clathrin adaptor epsinR (EPNR, also known as CLINT1;
607265). Structures of each domain and of their complex showed that this
interaction (dissociation constant 22 microM) is mediated by surface
patches composed of approximately 15 residues each, the topographies of
which are dependent on each domain's overall fold. Disruption of the
interface with point mutations abolished the interaction in vitro and
caused Vti1b to become relocalized to late endosomes and lysosomes.
Miller et al. (2007) stated that this new class of highly specific,
surface-surface interaction between the clathrin coat component and the
cargo is distinct from the widely observed binding of short, linear
cargo motifs by the assembly polypeptide (AP) complex and GGA adaptors
and is therefore not vulnerable to competition from standard
motif-containing cargoes for incorporation into clathrin-coated
vesicles. Miller et al. (2007) proposed that conceptually similar but
mechanistically different interactions direct the post-Golgi trafficking
of many SNAREs.
*FIELD* RF
1. 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. 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.
*FIELD* CN
Ada Hamosh - updated: 4/22/2008
*FIELD* CD
Rebekah S. Rasooly: 10/26/1998
*FIELD* ED
alopez: 05/14/2008
terry: 4/22/2008
carol: 11/26/2002
psherman: 10/27/1998