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 24-JAN-2024, entry version 156. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 11. DR IntAct; Q9HCJ6; 8. 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; 9606-ENSP00000303129; -. DR PeptideAtlas; Q9HCJ6; -. DR ProteomicsDB; 81741; -. DR Pumba; Q9HCJ6; -. DR Antibodypedia; 30406; 194 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 AGR; HGNC:29315; -. DR CTD; 57687; -. DR DisGeNET; 57687; -. DR GeneCards; VAT1L; -. DR HGNC; HGNC:29315; VAT1L. DR HPA; ENSG00000171724; Tissue enhanced (brain, choroid plexus, retina). DR MIM; 620202; gene. 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; 6736at2759; -. DR PhylomeDB; Q9HCJ6; -. DR TreeFam; TF314255; -. DR PathwayCommons; Q9HCJ6; -. DR SignaLink; Q9HCJ6; -. DR BioGRID-ORCS; 57687; 18 hits in 1140 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 140 other cell types or tissues. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd08275; MDR3; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR44054; SYNAPTIC VESICLE MEMBRANE PROTEIN VAT-1 HOMOLOG-LIKE; 1. DR PANTHER; PTHR44054:SF2; SYNAPTIC VESICLE MEMBRANE PROTEIN VAT-1 HOMOLOG-LIKE; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF13602; ADH_zinc_N_2; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. DR Genevisible; Q9HCJ6; HS. 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 //