VTI1A_MOUSE
ID VTI1A_MOUSE Reviewed; 217 AA.
AC O89116; Q545P9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
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; Synonyms=Vti1, Vti1l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NAPA AND NAPG, IDENTIFICATION
RP IN SNARE COMPLEXES WITH STX5 OR STX6, AND TISSUE SPECIFICITY.
RX PubMed=9705316; DOI=10.1074/jbc.273.34.21783;
RA Xu Y., Wong S.H., Tang B.L., Subramaniam V.N., Zhang T., Hong W.;
RT "A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment
RT protein receptor (Vti1-rp2) implicated in protein trafficking in the
RT secretory pathway.";
RL J. Biol. Chem. 273:21783-21789(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9553086; DOI=10.1074/jbc.273.17.10317;
RA Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R.,
RA Yoo J.-S., Scheller R.H.;
RT "Seven novel mammalian SNARE proteins localize to distinct membrane
RT compartments.";
RL J. Biol. Chem. 273:10317-10324(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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=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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP STRUCTURE BY NMR OF 3-94.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-009, an N-terminal domain of VTI1A [Mus
RT musculus].";
RL Submitted (MAY-2005) to the PDB data bank.
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 concerned with increased secretion of cytokines associated with
CC cellular senescence. {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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9705316}.
CC -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR EMBL; AF035823; AAC32049.1; -; mRNA.
DR EMBL; AF035209; AAC23482.1; -; mRNA.
DR EMBL; AK004751; BAB23532.1; -; mRNA.
DR EMBL; AK028646; BAC26046.1; -; mRNA.
DR EMBL; BC019386; AAH19386.1; -; mRNA.
DR CCDS; CCDS29910.1; -.
DR RefSeq; NP_001280615.1; NM_001293686.1.
DR RefSeq; NP_058558.1; NM_016862.4.
DR PDB; 1VCS; NMR; -; A=6-94.
DR PDBsum; 1VCS; -.
DR AlphaFoldDB; O89116; -.
DR SMR; O89116; -.
DR BioGRID; 207331; 12.
DR IntAct; O89116; 1.
DR STRING; 10090.ENSMUSP00000093644; -.
DR iPTMnet; O89116; -.
DR PhosphoSitePlus; O89116; -.
DR EPD; O89116; -.
DR MaxQB; O89116; -.
DR PaxDb; O89116; -.
DR PeptideAtlas; O89116; -.
DR PRIDE; O89116; -.
DR ProteomicsDB; 297615; -.
DR Antibodypedia; 31821; 281 antibodies from 31 providers.
DR DNASU; 53611; -.
DR Ensembl; ENSMUST00000095950; ENSMUSP00000093644; ENSMUSG00000024983.
DR GeneID; 53611; -.
DR KEGG; mmu:53611; -.
DR UCSC; uc008hxw.2; mouse.
DR CTD; 143187; -.
DR MGI; MGI:1855699; Vti1a.
DR VEuPathDB; HostDB:ENSMUSG00000024983; -.
DR eggNOG; KOG1666; Eukaryota.
DR GeneTree; ENSGT00950000183192; -.
DR HOGENOM; CLU_075474_1_0_1; -.
DR InParanoid; O89116; -.
DR OrthoDB; 1195966at2759; -.
DR PhylomeDB; O89116; -.
DR TreeFam; TF312874; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 53611; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Vti1a; mouse.
DR EvolutionaryTrace; O89116; -.
DR PRO; PR:O89116; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O89116; protein.
DR Bgee; ENSMUSG00000024983; Expressed in embryonic brain and 223 other tissues.
DR ExpressionAtlas; O89116; baseline and differential.
DR Genevisible; O89116; MM.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:ParkinsonsUK-UCL.
DR GO; GO:0090161; P:Golgi ribbon formation; ISO: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:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0016189; P:synaptic vesicle to endosome fusion; ISO:MGI.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:MGI.
DR Gene3D; 1.20.58.400; -; 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 Pfam; PF05008; V-SNARE; 1.
DR PIRSF; PIRSF028865; Membrin-2; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..217
FT /note="Vesicle transport through interaction with t-SNAREs
FT homolog 1A"
FT /id="PRO_0000218226"
FT TOPO_DOM 1..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..217
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT COILED 31..92
FT /evidence="ECO:0000255"
FT COILED 112..178
FT /evidence="ECO:0000255"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:1VCS"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1VCS"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1VCS"
FT HELIX 34..59
FT /evidence="ECO:0007829|PDB:1VCS"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1VCS"
FT HELIX 67..87
FT /evidence="ECO:0007829|PDB:1VCS"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1VCS"
SQ SEQUENCE 217 AA; 24986 MW; 3FD7B7A5A16E3522 CRC64;
MSSDFEGYEQ DFAVLTAEIT SKIARVPRLP PDEKKQMVAN VEKQLEEARE LLEQMDLEVR
EIPPQSRGMY SNRMRSYKQE MGKLETDFKR SRIAYSDEVR NELLGDAGNS SENQRAHLLD
NTERLERSSR RLEAGYQIAV ETEQIGQEML ENLSHDREKI QRARDRLRDA DANLGKSSRI
LTGMLRRIIQ NRILLVILGI IVVIAILTAI AFFVKGH
