VAT1L_HUMAN
ID VAT1L_HUMAN Reviewed; 419 AA.
AC Q9HCJ6; Q8IYW8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Synaptic vesicle membrane protein VAT-1 homolog-like;
DE EC=1.-.-.-;
GN Name=VAT1L; Synonyms=KIAA1576;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=19844255; DOI=10.1038/ejhg.2009.157;
RA Dastani Z., Pajukanta P., Marcil M., Rudzicz N., Ruel I., Bailey S.D.,
RA Lee J.C., Lemire M., Faith J., Platko J., Rioux J., Hudson T.J., Gaudet D.,
RA Engert J.C., Genest J.;
RT "Fine mapping and association studies of a high-density lipoprotein
RT cholesterol linkage region on chromosome 16 in French-Canadian subjects.";
RL Eur. J. Hum. Genet. 18:342-347(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 41-387.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human synaptic vesicle membrane protein Vat-1
RT homolog-like protein.";
RL Submitted (SEP-2011) to the PDB data bank.
CC -!- INTERACTION:
CC Q9HCJ6; P42858: HTT; NbExp=3; IntAct=EBI-10234766, EBI-466029;
CC Q9HCJ6; Q14CS0: UBXN2B; NbExp=3; IntAct=EBI-10234766, EBI-1993619;
CC -!- TISSUE SPECIFICITY: Detected in skin fibroblasts.
CC {ECO:0000269|PubMed:19844255}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB046796; BAB13402.1; ALT_INIT; mRNA.
DR EMBL; BC033537; AAH33537.1; -; mRNA.
DR CCDS; CCDS32492.1; -.
DR RefSeq; NP_065978.1; NM_020927.2.
DR PDB; 4A27; X-ray; 2.10 A; A/B=41-387.
DR PDBsum; 4A27; -.
DR AlphaFoldDB; Q9HCJ6; -.
DR SMR; Q9HCJ6; -.
DR BioGRID; 121713; 10.
DR IntAct; Q9HCJ6; 7.
DR STRING; 9606.ENSP00000303129; -.
DR iPTMnet; Q9HCJ6; -.
DR MetOSite; Q9HCJ6; -.
DR PhosphoSitePlus; Q9HCJ6; -.
DR BioMuta; VAT1L; -.
DR DMDM; 52783098; -.
DR EPD; Q9HCJ6; -.
DR jPOST; Q9HCJ6; -.
DR MassIVE; Q9HCJ6; -.
DR MaxQB; Q9HCJ6; -.
DR PaxDb; Q9HCJ6; -.
DR PeptideAtlas; Q9HCJ6; -.
DR PRIDE; Q9HCJ6; -.
DR ProteomicsDB; 81741; -.
DR Antibodypedia; 30406; 163 antibodies from 19 providers.
DR DNASU; 57687; -.
DR Ensembl; ENST00000302536.3; ENSP00000303129.2; ENSG00000171724.3.
DR GeneID; 57687; -.
DR KEGG; hsa:57687; -.
DR MANE-Select; ENST00000302536.3; ENSP00000303129.2; NM_020927.3; NP_065978.1.
DR UCSC; uc002ffg.2; human.
DR CTD; 57687; -.
DR DisGeNET; 57687; -.
DR GeneCards; VAT1L; -.
DR HGNC; HGNC:29315; VAT1L.
DR HPA; ENSG00000171724; Group enriched (adrenal gland, brain, choroid plexus, retina).
DR neXtProt; NX_Q9HCJ6; -.
DR OpenTargets; ENSG00000171724; -.
DR PharmGKB; PA164727497; -.
DR VEuPathDB; HostDB:ENSG00000171724; -.
DR eggNOG; KOG1198; Eukaryota.
DR GeneTree; ENSGT00940000159184; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; Q9HCJ6; -.
DR OMA; INYRTDR; -.
DR OrthoDB; 1085436at2759; -.
DR PhylomeDB; Q9HCJ6; -.
DR TreeFam; TF314255; -.
DR PathwayCommons; Q9HCJ6; -.
DR SignaLink; Q9HCJ6; -.
DR BioGRID-ORCS; 57687; 18 hits in 1062 CRISPR screens.
DR ChiTaRS; VAT1L; human.
DR EvolutionaryTrace; Q9HCJ6; -.
DR GenomeRNAi; 57687; -.
DR Pharos; Q9HCJ6; Tdark.
DR PRO; PR:Q9HCJ6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9HCJ6; protein.
DR Bgee; ENSG00000171724; Expressed in pigmented layer of retina and 139 other tissues.
DR Genevisible; Q9HCJ6; HS.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 3D-structure; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..419
FT /note="Synaptic vesicle membrane protein VAT-1 homolog-
FT like"
FT /id="PRO_0000160922"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TB8"
FT MOD_RES 393
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80TB8"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80TB8"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TB8"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:4A27"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:4A27"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:4A27"
SQ SEQUENCE 419 AA; 45899 MW; BA962924662987AC CRC64;
MAKEGVEKAE ETEQMIEKEA GKEPAEGGGG DGSHRLGDAQ EMRAVVLAGF GGLNKLRLFR
KAMPEPQDGE LKIRVKACGL NFIDLMVRQG NIDNPPKTPL VPGFECSGIV EALGDSVKGY
EIGDRVMAFV NYNAWAEVVC TPVEFVYKIP DDMSFSEAAA FPMNFVTAYV MLFEVANLRE
GMSVLVHSAG GGVGQAVAQL CSTVPNVTVF GTASTFKHEA IKDSVTHLFD RNADYVQEVK
RISAEGVDIV LDCLCGDNTG KGLSLLKPLG TYILYGSSNM VTGETKSFFS FAKSWWQVEK
VNPIKLYEEN KVIAGFSLLN LLFKQGRAGL IRGVVEKLIG LYNQKKIKPV VDSLWALEEV
KEAMQRIHDR GNIGKLILDV EKTPTPLMAN DSTETSEAGE EEEDHEGDSE NKERMPFIQ
