ID   VTI1A_HUMAN             Reviewed;         217 AA.
AC   Q96AJ9; A2A307; B4E137; Q5W0D7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   24-JAN-2024, entry version 170.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000312|EMBL:AAH17052.1};
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., 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] {ECO:0000312|EMBL:AAH17052.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   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 routes
RT   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 route
RT   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., 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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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).
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. Involved in
CC       vesicular transport from the late endosomes to the trans-Golgi network.
CC       Along with VAMP7, involved in an non-conventional RAB1-dependent
CC       traffic route to the cell surface used by KCNIP1 and KCND2. May be
CC       involved in increased cytokine secretion associated with cellular
CC       senescence. {ECO:0000269|PubMed:18195106, ECO:0000269|PubMed:19138172}.
CC   -!- SUBUNIT: Interacts with distinct SNARE complexes that contain either
CC       STX5 or STX6. Interacts with NAPA and, to a lesser extent, with NAPG.
CC       Identified in a complex containing STX6, STX12, VAMP4 and VTI1A.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:19138172}. Golgi apparatus membrane {ECO:0000250};
CC       Single-pass type IV membrane protein {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR   EMBL; AK303646; BAG64649.1; -; mRNA.
DR   EMBL; AC022018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL158212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49524.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49525.1; -; Genomic_DNA.
DR   EMBL; BC017052; AAH17052.1; -; mRNA.
DR   CCDS; CCDS7575.2; -. [Q96AJ9-2]
DR   CCDS; CCDS91347.1; -. [Q96AJ9-1]
DR   RefSeq; NP_001305132.1; NM_001318203.1.
DR   RefSeq; NP_001305134.1; NM_001318205.1.
DR   RefSeq; NP_660207.2; NM_145206.3. [Q96AJ9-2]
DR   RefSeq; XP_005269601.1; XM_005269544.4.
DR   AlphaFoldDB; Q96AJ9; -.
DR   SMR; Q96AJ9; -.
DR   BioGRID; 126789; 65.
DR   CORUM; Q96AJ9; -.
DR   DIP; DIP-44223N; -.
DR   IntAct; Q96AJ9; 17.
DR   MINT; Q96AJ9; -.
DR   STRING; 9606.ENSP00000376792; -.
DR   iPTMnet; Q96AJ9; -.
DR   MetOSite; Q96AJ9; -.
DR   PhosphoSitePlus; Q96AJ9; -.
DR   BioMuta; VTI1A; -.
DR   DMDM; 374095459; -.
DR   EPD; Q96AJ9; -.
DR   jPOST; Q96AJ9; -.
DR   MassIVE; Q96AJ9; -.
DR   MaxQB; Q96AJ9; -.
DR   PaxDb; 9606-ENSP00000376792; -.
DR   PeptideAtlas; Q96AJ9; -.
DR   ProteomicsDB; 75969; -. [Q96AJ9-2]
DR   ProteomicsDB; 75970; -. [Q96AJ9-1]
DR   Pumba; Q96AJ9; -.
DR   Antibodypedia; 31821; 306 antibodies from 31 providers.
DR   DNASU; 143187; -.
DR   Ensembl; ENST00000393077.3; ENSP00000376792.2; ENSG00000151532.15. [Q96AJ9-2]
DR   Ensembl; ENST00000432306.5; ENSP00000395017.1; ENSG00000151532.15. [Q96AJ9-1]
DR   GeneID; 143187; -.
DR   KEGG; hsa:143187; -.
DR   MANE-Select; ENST00000393077.3; ENSP00000376792.2; NM_145206.4; NP_660207.2.
DR   UCSC; uc001kzz.5; human. [Q96AJ9-2]
DR   AGR; HGNC:17792; -.
DR   CTD; 143187; -.
DR   DisGeNET; 143187; -.
DR   GeneCards; VTI1A; -.
DR   HGNC; HGNC:17792; VTI1A.
DR   HPA; ENSG00000151532; Low tissue specificity.
DR   MIM; 614316; gene.
DR   neXtProt; NX_Q96AJ9; -.
DR   OpenTargets; ENSG00000151532; -.
DR   PharmGKB; PA134928049; -.
DR   VEuPathDB; HostDB:ENSG00000151532; -.
DR   eggNOG; KOG1666; Eukaryota.
DR   GeneTree; ENSGT00950000183192; -.
DR   HOGENOM; CLU_075474_1_0_1; -.
DR   InParanoid; Q96AJ9; -.
DR   OMA; RGRVESH; -.
DR   OrthoDB; 461374at2759; -.
DR   PhylomeDB; Q96AJ9; -.
DR   TreeFam; TF312874; -.
DR   PathwayCommons; Q96AJ9; -.
DR   Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR   Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   SignaLink; Q96AJ9; -.
DR   SIGNOR; Q96AJ9; -.
DR   BioGRID-ORCS; 143187; 12 hits in 1154 CRISPR screens.
DR   ChiTaRS; VTI1A; human.
DR   GeneWiki; VTI1A; -.
DR   GenomeRNAi; 143187; -.
DR   Pharos; Q96AJ9; Tbio.
DR   PRO; PR:Q96AJ9; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q96AJ9; Protein.
DR   Bgee; ENSG00000151532; Expressed in sural nerve and 183 other cell types or tissues.
DR   GO; GO:0005776; C:autophagosome; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR   GO; GO:0044306; C:neuron projection terminus; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0031201; C:SNARE complex; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR   GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC-UCL.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:ParkinsonsUK-UCL.
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:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR   GO; GO:0016189; P:synaptic vesicle to endosome fusion; IEA:Ensembl.
DR   GO; GO:0048280; P:vesicle fusion with Golgi apparatus; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:UniProtKB.
DR   CDD; cd15891; SNARE_Vti1a; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 1.20.58.400; t-snare proteins; 1.
DR   InterPro; IPR027027; GOSR2/Membrin/Bos1.
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:SF26; VESICLE TRANSPORT THROUGH INTERACTION WITH T-SNARES HOMOLOG 1A; 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   PIRSF; PIRSF028865; Membrin-2; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   Genevisible; Q96AJ9; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasmic vesicle; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..217
FT                   /note="Vesicle transport through interaction with t-SNAREs
FT                   homolog 1A"
FT                   /id="PRO_0000218225"
FT   TOPO_DOM        1..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   COILED          31..92
FT                   /evidence="ECO:0000255"
FT   COILED          112..178
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         188..217
FT                   /note="IIQNRILLVILGIIVVITILMAITFSVRRH -> GCSVKKQCNLSLAPKA
FT                   (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_039848"
FT   CONFLICT        83
FT                   /note="K -> E (in Ref. 1; BAG64649)"
FT                   /evidence="ECO:0000305"
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
//