VAT1_RAT
ID VAT1_RAT Reviewed; 404 AA.
AC Q3MIE4;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Synaptic vesicle membrane protein VAT-1 homolog;
DE EC=1.-.-.-;
DE AltName: Full=Mitofusin-binding protein;
DE Short=Protein MIB;
GN Name=Vat1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH MFN1
RP AND MFN2, AND MUTAGENESIS OF GLY-210; GLY-211; VAL-212 AND GLY-213.
RX PubMed=17105775; DOI=10.1242/jcs.03253;
RA Eura Y., Ishihara N., Oka T., Mihara K.;
RT "Identification of a novel protein that regulates mitochondrial fusion by
RT modulating mitofusin (Mfn) protein function.";
RL J. Cell Sci. 119:4913-4925(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a part in calcium-regulated keratinocyte activation in
CC epidermal repair mechanisms. Has no effect on cell proliferation (By
CC similarity). Possesses ATPase activity. May negatively regulate
CC mitochondrial fusion. {ECO:0000250, ECO:0000269|PubMed:17105775}.
CC -!- SUBUNIT: Interacts with MFN1 and MFN2. {ECO:0000269|PubMed:17105775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17105775}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:17105775}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17105775}. Note=The majority is
CC localized in the cytoplasm and a small amount is associated with
CC mitochondria.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:17105775}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; AABR03074035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473948; EDM06132.1; -; Genomic_DNA.
DR EMBL; BC101882; AAI01883.1; -; mRNA.
DR RefSeq; NP_001028855.1; NM_001033683.1.
DR AlphaFoldDB; Q3MIE4; -.
DR SMR; Q3MIE4; -.
DR IntAct; Q3MIE4; 1.
DR MINT; Q3MIE4; -.
DR STRING; 10116.ENSRNOP00000028084; -.
DR iPTMnet; Q3MIE4; -.
DR PhosphoSitePlus; Q3MIE4; -.
DR jPOST; Q3MIE4; -.
DR PaxDb; Q3MIE4; -.
DR PRIDE; Q3MIE4; -.
DR Ensembl; ENSRNOT00000028084; ENSRNOP00000028084; ENSRNOG00000020684.
DR GeneID; 287721; -.
DR KEGG; rno:287721; -.
DR UCSC; RGD:1308943; rat.
DR CTD; 10493; -.
DR RGD; 1308943; Vat1.
DR eggNOG; KOG1197; Eukaryota.
DR GeneTree; ENSGT00940000157579; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; Q3MIE4; -.
DR OMA; MQYVTAW; -.
DR OrthoDB; 1085436at2759; -.
DR PhylomeDB; Q3MIE4; -.
DR TreeFam; TF314255; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q3MIE4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000020684; Expressed in lung and 18 other tissues.
DR Genevisible; Q3MIE4; RN.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISO:RGD.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99536"
FT CHAIN 2..404
FT /note="Synaptic vesicle membrane protein VAT-1 homolog"
FT /id="PRO_0000417041"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q99536"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99536"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99536"
FT MUTAGEN 210
FT /note="G->A: Fails to induce mitochondrial fragmentation;
FT when associated with A-212."
FT /evidence="ECO:0000269|PubMed:17105775"
FT MUTAGEN 211
FT /note="G->A: Fails to induce mitochondrial fragmentation;
FT when associated with A-211."
FT /evidence="ECO:0000269|PubMed:17105775"
FT MUTAGEN 212
FT /note="V->A: Fails to induce mitochondrial fragmentation
FT and mitochondrial targeting. Fail to induce mitochondrial
FT fragmentation; when associated with A-213."
FT /evidence="ECO:0000269|PubMed:17105775"
FT MUTAGEN 213
FT /note="G->A: Fails to induce mitochondrial fragmentation.
FT Fail to induce mitochondrial fragmentation; when associated
FT with A-212."
FT /evidence="ECO:0000269|PubMed:17105775"
SQ SEQUENCE 404 AA; 43119 MW; 1C436DAF35A94D9C CRC64;
MSAEREATEA ATVAAAAEAR AETGAGEGAP SQPPTVEVAS DPQPPPAPEA SASASAPPLR
CLVLTGFGGY DKVKLQSRPA VPPAPGPGQV TLRVRACGLN FADLMGRQGL YDRLPPLPVT
PGMEGAGVVV AVGEGVSDRK AGDRVMVLNR SGMWQEEVTV PSAQTFLMPE AMTFEEAAAL
LVNYITAYMV LFDFGNLRPG HSVLVHMAAG GVGMAALQLC RTVENVTVFG TASASKHEVL
KENGVTHPID YHTTDYVDEI KKISPKGVDI VMDPLGGSDT AKGYHLLKPM GKVVTYGMAN
LLTGPKRNLM AMARTWWNQF SVTALQLLQA NRAVCGFHLG YLDGEVELVS RVVTHLLALY
NQGHIKPRID SVWPFEKVAD AMRQMQEKKN IGKVLLVPGP EKET
