Full text data of VTI1A
VTI1A
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Vesicle transport through interaction with t-SNAREs homolog 1A (Vesicle transport v-SNARE protein Vti1-like 2; Vti1-rp2)
Vesicle transport through interaction with t-SNAREs homolog 1A (Vesicle transport v-SNARE protein Vti1-like 2; Vti1-rp2)
UniProt
Q96AJ9
ID VTI1A_HUMAN Reviewed; 217 AA.
AC Q96AJ9; A2A307; B4E137; Q5W0D7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-JAN-2012, sequence version 2.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Vesicle transport through interaction with t-SNAREs homolog 1A;
DE AltName: Full=Vesicle transport v-SNARE protein Vti1-like 2;
DE AltName: Full=Vti1-rp2;
GN Name=VTI1A;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [5]
RP FUNCTION.
RX PubMed=18195106; DOI=10.1083/jcb.200707136;
RA Ganley I.G., Espinosa E., Pfeffer S.R.;
RT "A syntaxin 10-SNARE complex distinguishes two distinct transport
RT routes from endosomes to the trans-Golgi in human cells.";
RL J. Cell Biol. 180:159-172(2008).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19138172; DOI=10.1042/BJ20081736;
RA Flowerdew S.E., Burgoyne R.D.;
RT "A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic
RT route to the cell surface used by KChIP1 and Kv4 potassium channels.";
RL Biochem. J. 418:529-540(2009).
RN [7]
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).
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 Involved in vesicular transport from the late endosomes to the
CC trans-Golgi network. Along with VAMP7, involved in an non-
CC conventional RAB1-dependent traffic route to the cell surface used
CC by KCNIP1 and KCND2. May be involved in increased cytokine
CC secretion associated with cellular senescence.
CC -!- SUBUNIT: Interacts with distinct SNARE complexes that contain
CC either STX5 or STX6 (By similarity). Interacts with NAPA and, to a
CC lesser extent, with NAPG (By similarity). Identified in a complex
CC containing STX6, STX12, VAMP4 and VTI1A (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Golgi apparatus
CC membrane; Single-pass type IV membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q96AJ9-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q96AJ9-1; Sequence=VSP_039848;
CC Note=No experimental confirmation available;
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; AK303646; BAG64649.1; -; mRNA.
DR EMBL; AL139120; CAH71781.2; -; Genomic_DNA.
DR EMBL; AC022018; CAH71781.2; JOINED; Genomic_DNA.
DR EMBL; AL158212; CAH71781.2; JOINED; Genomic_DNA.
DR EMBL; AL139120; CAM15142.1; -; Genomic_DNA.
DR EMBL; AC022018; CAM15142.1; JOINED; Genomic_DNA.
DR EMBL; AL158212; CAM22437.1; -; Genomic_DNA.
DR EMBL; AC022018; CAM22437.1; JOINED; Genomic_DNA.
DR EMBL; AL139120; CAM22437.1; JOINED; Genomic_DNA.
DR EMBL; CH471066; EAW49524.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49525.1; -; Genomic_DNA.
DR EMBL; BC017052; AAH17052.1; -; mRNA.
DR RefSeq; NP_660207.2; NM_145206.2.
DR RefSeq; XP_005269601.1; XM_005269544.1.
DR UniGene; Hs.194554; -.
DR ProteinModelPortal; Q96AJ9; -.
DR SMR; Q96AJ9; 8-94, 113-190.
DR IntAct; Q96AJ9; 3.
DR MINT; MINT-3050814; -.
DR STRING; 9606.ENSP00000376792; -.
DR PhosphoSite; Q96AJ9; -.
DR DMDM; 29337113; -.
DR PaxDb; Q96AJ9; -.
DR PeptideAtlas; Q96AJ9; -.
DR PRIDE; Q96AJ9; -.
DR DNASU; 143187; -.
DR Ensembl; ENST00000393077; ENSP00000376792; ENSG00000151532.
DR Ensembl; ENST00000432306; ENSP00000395017; ENSG00000151532.
DR GeneID; 143187; -.
DR KEGG; hsa:143187; -.
DR UCSC; uc001kzz.3; human.
DR CTD; 143187; -.
DR GeneCards; GC10P114197; -.
DR H-InvDB; HIX0023094; -.
DR HGNC; HGNC:17792; VTI1A.
DR HPA; HPA054108; -.
DR MIM; 614316; gene.
DR neXtProt; NX_Q96AJ9; -.
DR PharmGKB; PA134928049; -.
DR eggNOG; NOG239679; -.
DR HOGENOM; HOG000116573; -.
DR HOVERGEN; HBG104027; -.
DR KO; K08493; -.
DR OMA; LIANTQR; -.
DR OrthoDB; EOG7MKW77; -.
DR GeneWiki; VTI1A; -.
DR GenomeRNAi; 143187; -.
DR NextBio; 84666; -.
DR PRO; PR:Q96AJ9; -.
DR Bgee; Q96AJ9; -.
DR CleanEx; HS_VTI1A; -.
DR Genevestigator; Q96AJ9; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031201; C:SNARE complex; TAS:HGNC.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
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 Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 217 Vesicle transport through interaction
FT with t-SNAREs homolog 1A.
FT /FTId=PRO_0000218225.
FT TOPO_DOM 1 192 Cytoplasmic (Potential).
FT TRANSMEM 193 213 Helical; (Potential).
FT TOPO_DOM 214 217 Extracellular (Potential).
FT COILED 31 92 Potential.
FT COILED 112 178 Potential.
FT VAR_SEQ 188 217 IIQNRILLVILGIIVVITILMAITFSVRRH -> GCSVKKQ
FT CNLSLAPKA (in isoform 1).
FT /FTId=VSP_039848.
FT CONFLICT 83 83 K -> E (in Ref. 1; BAG64649).
SQ SEQUENCE 217 AA; 25218 MW; 3FE5FE787B5958F0 CRC64;
MSSDFEGYEQ DFAVLTAEIT SKIARVPRLP PDEKKQMVAN VEKQLEEAKE LLEQMDLEVR
EIPPQSRGMY SNRMRSYKQE MGKLETDFKR SRIAYSDEVR NELLGDDGNS SENQRAHLLD
NTERLERSSR RLEAGYQIAV ETEQIGQEML ENLSHDREKI QRARERLRET DANLGKSSRI
LTGMLRRIIQ NRILLVILGI IVVITILMAI TFSVRRH
//
ID VTI1A_HUMAN Reviewed; 217 AA.
AC Q96AJ9; A2A307; B4E137; Q5W0D7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-JAN-2012, sequence version 2.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Vesicle transport through interaction with t-SNAREs homolog 1A;
DE AltName: Full=Vesicle transport v-SNARE protein Vti1-like 2;
DE AltName: Full=Vti1-rp2;
GN Name=VTI1A;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [5]
RP FUNCTION.
RX PubMed=18195106; DOI=10.1083/jcb.200707136;
RA Ganley I.G., Espinosa E., Pfeffer S.R.;
RT "A syntaxin 10-SNARE complex distinguishes two distinct transport
RT routes from endosomes to the trans-Golgi in human cells.";
RL J. Cell Biol. 180:159-172(2008).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19138172; DOI=10.1042/BJ20081736;
RA Flowerdew S.E., Burgoyne R.D.;
RT "A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic
RT route to the cell surface used by KChIP1 and Kv4 potassium channels.";
RL Biochem. J. 418:529-540(2009).
RN [7]
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).
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 Involved in vesicular transport from the late endosomes to the
CC trans-Golgi network. Along with VAMP7, involved in an non-
CC conventional RAB1-dependent traffic route to the cell surface used
CC by KCNIP1 and KCND2. May be involved in increased cytokine
CC secretion associated with cellular senescence.
CC -!- SUBUNIT: Interacts with distinct SNARE complexes that contain
CC either STX5 or STX6 (By similarity). Interacts with NAPA and, to a
CC lesser extent, with NAPG (By similarity). Identified in a complex
CC containing STX6, STX12, VAMP4 and VTI1A (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Golgi apparatus
CC membrane; Single-pass type IV membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q96AJ9-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q96AJ9-1; Sequence=VSP_039848;
CC Note=No experimental confirmation available;
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; AK303646; BAG64649.1; -; mRNA.
DR EMBL; AL139120; CAH71781.2; -; Genomic_DNA.
DR EMBL; AC022018; CAH71781.2; JOINED; Genomic_DNA.
DR EMBL; AL158212; CAH71781.2; JOINED; Genomic_DNA.
DR EMBL; AL139120; CAM15142.1; -; Genomic_DNA.
DR EMBL; AC022018; CAM15142.1; JOINED; Genomic_DNA.
DR EMBL; AL158212; CAM22437.1; -; Genomic_DNA.
DR EMBL; AC022018; CAM22437.1; JOINED; Genomic_DNA.
DR EMBL; AL139120; CAM22437.1; JOINED; Genomic_DNA.
DR EMBL; CH471066; EAW49524.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49525.1; -; Genomic_DNA.
DR EMBL; BC017052; AAH17052.1; -; mRNA.
DR RefSeq; NP_660207.2; NM_145206.2.
DR RefSeq; XP_005269601.1; XM_005269544.1.
DR UniGene; Hs.194554; -.
DR ProteinModelPortal; Q96AJ9; -.
DR SMR; Q96AJ9; 8-94, 113-190.
DR IntAct; Q96AJ9; 3.
DR MINT; MINT-3050814; -.
DR STRING; 9606.ENSP00000376792; -.
DR PhosphoSite; Q96AJ9; -.
DR DMDM; 29337113; -.
DR PaxDb; Q96AJ9; -.
DR PeptideAtlas; Q96AJ9; -.
DR PRIDE; Q96AJ9; -.
DR DNASU; 143187; -.
DR Ensembl; ENST00000393077; ENSP00000376792; ENSG00000151532.
DR Ensembl; ENST00000432306; ENSP00000395017; ENSG00000151532.
DR GeneID; 143187; -.
DR KEGG; hsa:143187; -.
DR UCSC; uc001kzz.3; human.
DR CTD; 143187; -.
DR GeneCards; GC10P114197; -.
DR H-InvDB; HIX0023094; -.
DR HGNC; HGNC:17792; VTI1A.
DR HPA; HPA054108; -.
DR MIM; 614316; gene.
DR neXtProt; NX_Q96AJ9; -.
DR PharmGKB; PA134928049; -.
DR eggNOG; NOG239679; -.
DR HOGENOM; HOG000116573; -.
DR HOVERGEN; HBG104027; -.
DR KO; K08493; -.
DR OMA; LIANTQR; -.
DR OrthoDB; EOG7MKW77; -.
DR GeneWiki; VTI1A; -.
DR GenomeRNAi; 143187; -.
DR NextBio; 84666; -.
DR PRO; PR:Q96AJ9; -.
DR Bgee; Q96AJ9; -.
DR CleanEx; HS_VTI1A; -.
DR Genevestigator; Q96AJ9; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031201; C:SNARE complex; TAS:HGNC.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
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 Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 217 Vesicle transport through interaction
FT with t-SNAREs homolog 1A.
FT /FTId=PRO_0000218225.
FT TOPO_DOM 1 192 Cytoplasmic (Potential).
FT TRANSMEM 193 213 Helical; (Potential).
FT TOPO_DOM 214 217 Extracellular (Potential).
FT COILED 31 92 Potential.
FT COILED 112 178 Potential.
FT VAR_SEQ 188 217 IIQNRILLVILGIIVVITILMAITFSVRRH -> GCSVKKQ
FT CNLSLAPKA (in isoform 1).
FT /FTId=VSP_039848.
FT CONFLICT 83 83 K -> E (in Ref. 1; BAG64649).
SQ SEQUENCE 217 AA; 25218 MW; 3FE5FE787B5958F0 CRC64;
MSSDFEGYEQ DFAVLTAEIT SKIARVPRLP PDEKKQMVAN VEKQLEEAKE LLEQMDLEVR
EIPPQSRGMY SNRMRSYKQE MGKLETDFKR SRIAYSDEVR NELLGDDGNS SENQRAHLLD
NTERLERSSR RLEAGYQIAV ETEQIGQEML ENLSHDREKI QRARERLRET DANLGKSSRI
LTGMLRRIIQ NRILLVILGI IVVITILMAI TFSVRRH
//
MIM
614316
*RECORD*
*FIELD* NO
614316
*FIELD* TI
*614316 VTI1, S. CEREVISIAE, HOMOLOG OF, A; VTI1A
;;VTI1RP2
VTI1A/TCF7L2 FUSION GENE, INCLUDED
read more*FIELD* TX
DESCRIPTION
VTI1A is a soluble N-ethylmaleimide-sensitive fusion protein attachment
protein (SNAP; see 603215) receptor (SNARE) that functions in the
transport of vesicles between the Golgi apparatus and the plasma
membrane (Flowerdew and Burgoyne, 2009).
CLONING
Xu et al. (1998) cloned mouse Vti1a, which they called Vti1rp2. The
deduced 217-amino acid protein has 4 putative coiled-coil regions and a
C-terminal transmembrane domain. The final coiled-coil region includes
an ATP/GTP-binding motif A (P loop). Northern blot analysis detected a
2.6-kb transcript in all mouse tissues examined except testis, which
expressed a 1.5-kb Vti1a transcript. Western blot analysis and
differential extraction of fractionated rat liver membranes revealed
that Vti1a was an integral Golgi membrane protein.
By immunohistochemical analysis of HeLa cells, Flowerdew and Burgoyne
(2009) found that human VTI1A showed a punctate vesicular distribution.
GENE FUNCTION
Using protein pull-down assays, Xu et al. (1998) showed that mouse Vti1a
interacted with alpha-SNAP (NAPA; 603215). Coimmunoprecipitation
analysis revealed that Vti1a interacted with 2 distinct SNARE complexes
that contained either syntaxin-5 (STX5; 603189) or syntaxin-6 (STX6;
603944). Immunodepletion of Vti1a from Vero monkey kidney cells
interfered with plasma membrane trafficking of vesicular-stomatitis
virus G protein (VSVG), resulting in accumulation of VSVG in the Golgi
apparatus.
Flowerdew and Burgoyne (2009) showed that potassium channel-interacting
protein-1 (KCHIP1, or KCNIP1; 604660) interacted with the
channel-forming Kv4.2 potassium channel subunit (KCND2; 605410) and was
required for Kv4.2 trafficking to the plasma membrane. Using HeLa and
mouse Neuro2A neuroblastoma cells, they found that KCHIP1 and Kv4.2 used
an intracellular vesicle trafficking pathway that included VTI1A and
VAMP7 (300053) and required the GTPase RAB1 (179508), which is shared
with more conventional vesicle-trafficking pathways. Knockdown of VTI1A
or VAMP7 inhibited transport of Kv4.2 and KCHIP1 to the plasma membrane,
but it had no effect on membrane transport of VSVG.
CYTOGENETICS
- VTI1A/TCF7L2 Fusion Gene
Bass et al. (2011) reported whole-genome sequencing from 9 individuals
with colorectal cancer (114500), including primary colorectal tumors and
matched adjacent nontumor tissues, at an average of 30.7x and 31.9x
coverage, respectively. They identified an average of 75 somatic
rearrangements per tumor, including complex networks of translocations
between pairs of chromosomes. Eleven rearrangements encode predicted
in-frame fusion proteins, including a fusion of VTI1A and TCF7L2
(602278) found in 3 out of 97 colorectal cancers. Although TCF7L2
encodes TCF4, which cooperates with beta-catenin (116806) in colorectal
carcinogenesis, the fusion lacks the TCF4 beta-catenin-binding domain.
Bass et al. (2011) found a colorectal carcinoma cell line harboring the
fusion gene to be dependent on VTI1A-TCF7L2 for anchorage-independent
growth using RNA interference-mediated knockdown.
MAPPING
Hartz (2011) mapped the VTI1A gene to chromosome 10q25.2 based on an
alignment of the VTI1A sequence (GenBank GENBANK BC017052) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Bass, A. J.; Lawrence, M. S.; Brace, L. E.; Ramos, A. H.; Drier,
Y.; Cibulskis, K.; Sougnez, C.; Voet, D.; Saksena, G.; Sivachenko,
A.; Jing, R.; Parkin, M.; and 28 others: Genomic sequencing of
colorectal adenocarcinomas identifies a recurrent VTI1A-TCF7L2 fusion. Nature
Genet. 43: 964-968, 2011.
2. Flowerdew, S. E.; Burgoyne, R. D.: A VAMP7/Vti1a SNARE complex
distinguishes a non-conventional traffic route to the cell surface
used by KChIP1 and Kv4 potassium channels. Biochem. J. 418: 529-540,
2009.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/27/2011.
4. Xu, Y.; Wong, S. H.; Tang, B. L.; Subramaniam, V. N.; Zhang, T.;
Hong, W.: A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive
factor attachment protein receptor (Vti1-rp2) implicated in protein
trafficking in the secretory pathway. J. Biol. Chem. 273: 21783-21789,
1998.
*FIELD* CN
Ada Hamosh - updated: 6/26/2012
*FIELD* CD
Patricia A. Hartz: 10/28/2011
*FIELD* ED
alopez: 06/26/2012
alopez: 6/26/2012
terry: 6/26/2012
mgross: 10/28/2011
*RECORD*
*FIELD* NO
614316
*FIELD* TI
*614316 VTI1, S. CEREVISIAE, HOMOLOG OF, A; VTI1A
;;VTI1RP2
VTI1A/TCF7L2 FUSION GENE, INCLUDED
read more*FIELD* TX
DESCRIPTION
VTI1A is a soluble N-ethylmaleimide-sensitive fusion protein attachment
protein (SNAP; see 603215) receptor (SNARE) that functions in the
transport of vesicles between the Golgi apparatus and the plasma
membrane (Flowerdew and Burgoyne, 2009).
CLONING
Xu et al. (1998) cloned mouse Vti1a, which they called Vti1rp2. The
deduced 217-amino acid protein has 4 putative coiled-coil regions and a
C-terminal transmembrane domain. The final coiled-coil region includes
an ATP/GTP-binding motif A (P loop). Northern blot analysis detected a
2.6-kb transcript in all mouse tissues examined except testis, which
expressed a 1.5-kb Vti1a transcript. Western blot analysis and
differential extraction of fractionated rat liver membranes revealed
that Vti1a was an integral Golgi membrane protein.
By immunohistochemical analysis of HeLa cells, Flowerdew and Burgoyne
(2009) found that human VTI1A showed a punctate vesicular distribution.
GENE FUNCTION
Using protein pull-down assays, Xu et al. (1998) showed that mouse Vti1a
interacted with alpha-SNAP (NAPA; 603215). Coimmunoprecipitation
analysis revealed that Vti1a interacted with 2 distinct SNARE complexes
that contained either syntaxin-5 (STX5; 603189) or syntaxin-6 (STX6;
603944). Immunodepletion of Vti1a from Vero monkey kidney cells
interfered with plasma membrane trafficking of vesicular-stomatitis
virus G protein (VSVG), resulting in accumulation of VSVG in the Golgi
apparatus.
Flowerdew and Burgoyne (2009) showed that potassium channel-interacting
protein-1 (KCHIP1, or KCNIP1; 604660) interacted with the
channel-forming Kv4.2 potassium channel subunit (KCND2; 605410) and was
required for Kv4.2 trafficking to the plasma membrane. Using HeLa and
mouse Neuro2A neuroblastoma cells, they found that KCHIP1 and Kv4.2 used
an intracellular vesicle trafficking pathway that included VTI1A and
VAMP7 (300053) and required the GTPase RAB1 (179508), which is shared
with more conventional vesicle-trafficking pathways. Knockdown of VTI1A
or VAMP7 inhibited transport of Kv4.2 and KCHIP1 to the plasma membrane,
but it had no effect on membrane transport of VSVG.
CYTOGENETICS
- VTI1A/TCF7L2 Fusion Gene
Bass et al. (2011) reported whole-genome sequencing from 9 individuals
with colorectal cancer (114500), including primary colorectal tumors and
matched adjacent nontumor tissues, at an average of 30.7x and 31.9x
coverage, respectively. They identified an average of 75 somatic
rearrangements per tumor, including complex networks of translocations
between pairs of chromosomes. Eleven rearrangements encode predicted
in-frame fusion proteins, including a fusion of VTI1A and TCF7L2
(602278) found in 3 out of 97 colorectal cancers. Although TCF7L2
encodes TCF4, which cooperates with beta-catenin (116806) in colorectal
carcinogenesis, the fusion lacks the TCF4 beta-catenin-binding domain.
Bass et al. (2011) found a colorectal carcinoma cell line harboring the
fusion gene to be dependent on VTI1A-TCF7L2 for anchorage-independent
growth using RNA interference-mediated knockdown.
MAPPING
Hartz (2011) mapped the VTI1A gene to chromosome 10q25.2 based on an
alignment of the VTI1A sequence (GenBank GENBANK BC017052) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Bass, A. J.; Lawrence, M. S.; Brace, L. E.; Ramos, A. H.; Drier,
Y.; Cibulskis, K.; Sougnez, C.; Voet, D.; Saksena, G.; Sivachenko,
A.; Jing, R.; Parkin, M.; and 28 others: Genomic sequencing of
colorectal adenocarcinomas identifies a recurrent VTI1A-TCF7L2 fusion. Nature
Genet. 43: 964-968, 2011.
2. Flowerdew, S. E.; Burgoyne, R. D.: A VAMP7/Vti1a SNARE complex
distinguishes a non-conventional traffic route to the cell surface
used by KChIP1 and Kv4 potassium channels. Biochem. J. 418: 529-540,
2009.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/27/2011.
4. Xu, Y.; Wong, S. H.; Tang, B. L.; Subramaniam, V. N.; Zhang, T.;
Hong, W.: A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive
factor attachment protein receptor (Vti1-rp2) implicated in protein
trafficking in the secretory pathway. J. Biol. Chem. 273: 21783-21789,
1998.
*FIELD* CN
Ada Hamosh - updated: 6/26/2012
*FIELD* CD
Patricia A. Hartz: 10/28/2011
*FIELD* ED
alopez: 06/26/2012
alopez: 6/26/2012
terry: 6/26/2012
mgross: 10/28/2011