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Vesicle transport through interaction with t-SNAREs homolog 1A (Vesicle transport v-SNARE protein Vti1-like 2) (Vti1-rp2)

 VTI1A_MOUSE             Reviewed;         217 AA.
O89116; Q545P9;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 140.
RecName: Full=Vesicle transport through interaction with t-SNAREs homolog 1A;
AltName: Full=Vesicle transport v-SNARE protein Vti1-like 2;
AltName: Full=Vti1-rp2;
Name=Vti1a; Synonyms=Vti1, Vti1l2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NAPA AND NAPG,
IDENTIFICATION IN SNARE COMPLEXES WITH STX5 OR STX6, AND TISSUE
SPECIFICITY.
PubMed=9705316; DOI=10.1074/jbc.273.34.21783;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9553086; DOI=10.1074/jbc.273.17.10317;
Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C.,
Prekeris R., Yoo J.-S., Scheller R.H.;
"Seven novel mammalian SNARE proteins localize to distinct membrane
compartments.";
J. Biol. Chem. 273:10317-10324(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=19138172; DOI=10.1042/BJ20081736;
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
STRUCTURE BY NMR OF 3-94.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-009, an N-terminal domain of VTI1A
[Mus musculus].";
Submitted (MAY-2005) to the PDB data bank.
-!- FUNCTION: V-SNARE that mediates vesicle transport pathways through
interactions with t-SNAREs on the target membrane. These
interactions are proposed to mediate aspects of the specificity of
vesicle trafficking and to promote fusion of the lipid bilayers.
Involved in vesicular transport from the late endosomes to the
trans-Golgi network. Along with VAMP7, involved in an non-
conventional RAB1-dependent traffic route to the cell surface used
by KCNIP1 and KCND2. May be concerned with increased secretion of
cytokines associated with cellular senescence.
{ECO:0000269|PubMed:19138172}.
-!- SUBUNIT: Interacts with distinct SNARE complexes that contain
either STX5 or STX6. Interacts with NAPA and, to a lesser extent,
with NAPG. Identified in a complex containing STX6, STX12, VAMP4
and VTI1A (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type IV membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9705316}.
-!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF035823; AAC32049.1; -; mRNA.
EMBL; AF035209; AAC23482.1; -; mRNA.
EMBL; AK004751; BAB23532.1; -; mRNA.
EMBL; AK028646; BAC26046.1; -; mRNA.
EMBL; BC019386; AAH19386.1; -; mRNA.
CCDS; CCDS29910.1; -.
RefSeq; NP_001280615.1; NM_001293686.1.
RefSeq; NP_058558.1; NM_016862.4.
UniGene; Mm.258637; -.
UniGene; Mm.451075; -.
UniGene; Mm.451214; -.
PDB; 1VCS; NMR; -; A=6-94.
PDBsum; 1VCS; -.
ProteinModelPortal; O89116; -.
SMR; O89116; -.
BioGrid; 207331; 2.
IntAct; O89116; 2.
MINT; O89116; -.
STRING; 10090.ENSMUSP00000093644; -.
iPTMnet; O89116; -.
PhosphoSitePlus; O89116; -.
EPD; O89116; -.
MaxQB; O89116; -.
PaxDb; O89116; -.
PeptideAtlas; O89116; -.
PRIDE; O89116; -.
Ensembl; ENSMUST00000095950; ENSMUSP00000093644; ENSMUSG00000024983.
GeneID; 53611; -.
KEGG; mmu:53611; -.
UCSC; uc008hxw.2; mouse.
CTD; 143187; -.
MGI; MGI:1855699; Vti1a.
eggNOG; KOG1666; Eukaryota.
eggNOG; ENOG4111J90; LUCA.
GeneTree; ENSGT00530000063466; -.
HOGENOM; HOG000116573; -.
HOVERGEN; HBG104027; -.
InParanoid; O89116; -.
KO; K08493; -.
OMA; NYEQQYA; -.
OrthoDB; EOG091G0L3Z; -.
PhylomeDB; O89116; -.
TreeFam; TF312874; -.
Reactome; R-MMU-6811438; Intra-Golgi traffic.
Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
ChiTaRS; Vti1a; mouse.
EvolutionaryTrace; O89116; -.
PRO; PR:O89116; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024983; Expressed in 243 organ(s), highest expression level in brain.
ExpressionAtlas; O89116; baseline and differential.
Genevisible; O89116; MM.
GO; GO:0005776; C:autophagosome; ISO:MGI.
GO; GO:0030136; C:clathrin-coated vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0005768; C:endosome; ISS:ParkinsonsUK-UCL.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
GO; GO:0044306; C:neuron projection terminus; ISS:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ParkinsonsUK-UCL.
GO; GO:0031201; C:SNARE complex; ISS:ParkinsonsUK-UCL.
GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0006914; P:autophagy; ISO:MGI.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:ParkinsonsUK-UCL.
GO; GO:0090161; P:Golgi ribbon formation; ISO:MGI.
GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
GO; GO:0048280; P:vesicle fusion with Golgi apparatus; ISS:ParkinsonsUK-UCL.
GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:MGI.
Gene3D; 1.20.58.400; -; 1.
InterPro; IPR027027; GOSR2/Membrin/Bos1.
InterPro; IPR010989; SNARE.
InterPro; IPR000727; T_SNARE_dom.
InterPro; IPR038407; v-SNARE_N_sf.
InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
Pfam; PF05008; V-SNARE; 1.
PIRSF; PIRSF028865; Membrin-2; 1.
SMART; SM00397; t_SNARE; 1.
SUPFAM; SSF47661; SSF47661; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Golgi apparatus;
Membrane; Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 217 Vesicle transport through interaction
with t-SNAREs homolog 1A.
/FTId=PRO_0000218226.
TOPO_DOM 1 192 Cytoplasmic. {ECO:0000255}.
TRANSMEM 193 213 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 214 217 Vesicular. {ECO:0000255}.
COILED 31 92 {ECO:0000255}.
COILED 112 178 {ECO:0000255}.
HELIX 9 25 {ECO:0000244|PDB:1VCS}.
HELIX 26 28 {ECO:0000244|PDB:1VCS}.
TURN 31 33 {ECO:0000244|PDB:1VCS}.
HELIX 34 59 {ECO:0000244|PDB:1VCS}.
TURN 64 66 {ECO:0000244|PDB:1VCS}.
HELIX 67 87 {ECO:0000244|PDB:1VCS}.
HELIX 89 92 {ECO:0000244|PDB:1VCS}.
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


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