VNNL1_DROME
ID VNNL1_DROME Reviewed; 558 AA.
AC Q9NFP1; Q9W431;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Vanin-like protein 1 {ECO:0000312|FlyBase:FBgn0040069};
DE EC=3.5.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=vanin-like {ECO:0000303|PubMed:10501839,
GN ECO:0000312|FlyBase:FBgn0040069};
GN ORFNames=CG32754 {ECO:0000312|FlyBase:FBgn0040069};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10501839; DOI=10.1007/s002510050580;
RA Granjeaud S., Naquet P., Galland F.;
RT "An ESTs description of the new vanin gene family conserved from fly to
RT human.";
RL Immunogenetics 49:964-972(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-354, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25387828; DOI=10.1534/g3.114.015040;
RA Logan-Garbisch T., Bortolazzo A., Luu P., Ford A., Do D., Khodabakhshi P.,
RA French R.L.;
RT "Developmental ethanol exposure leads to dysregulation of lipid metabolism
RT and oxidative stress in Drosophila.";
RL G3 (Bethesda) 5:49-59(2014).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in larvae and early pupae
CC (PubMed:10501839). Expressed in third instar larvae (PubMed:25387828).
CC {ECO:0000269|PubMed:10501839, ECO:0000269|PubMed:25387828}.
CC -!- INDUCTION: Induced by ethanol. {ECO:0000269|PubMed:25387828}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC BTD/VNN family. {ECO:0000305}.
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DR EMBL; AJ276261; CAB77020.1; -; mRNA.
DR EMBL; AE014298; AAN09161.1; -; Genomic_DNA.
DR EMBL; AY052034; AAK93458.1; -; mRNA.
DR RefSeq; NP_572297.1; NM_132069.3.
DR AlphaFoldDB; Q9NFP1; -.
DR SMR; Q9NFP1; -.
DR BioGRID; 58043; 6.
DR STRING; 7227.FBpp0070844; -.
DR GlyGen; Q9NFP1; 7 sites.
DR iPTMnet; Q9NFP1; -.
DR PaxDb; Q9NFP1; -.
DR PRIDE; Q9NFP1; -.
DR DNASU; 31551; -.
DR EnsemblMetazoa; FBtr0070879; FBpp0070844; FBgn0040069.
DR GeneID; 31551; -.
DR KEGG; dme:Dmel_CG32754; -.
DR UCSC; CG32754-RA; d. melanogaster.
DR CTD; 31551; -.
DR FlyBase; FBgn0040069; vanin-like.
DR VEuPathDB; VectorBase:FBgn0040069; -.
DR eggNOG; KOG0806; Eukaryota.
DR GeneTree; ENSGT00390000013823; -.
DR HOGENOM; CLU_033209_1_0_1; -.
DR InParanoid; Q9NFP1; -.
DR OMA; SNSLCCH; -.
DR OrthoDB; 1276751at2759; -.
DR PhylomeDB; Q9NFP1; -.
DR Reactome; R-DME-196780; Biotin transport and metabolism.
DR BioGRID-ORCS; 31551; 0 hits in 3 CRISPR screens.
DR ChiTaRS; vanin-like; fly.
DR GenomeRNAi; 31551; -.
DR PRO; PR:Q9NFP1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0040069; Expressed in adult midgut (Drosophila) and 9 other tissues.
DR Genevisible; Q9NFP1; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; NAS:UniProtKB.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07567; biotinidase_like; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR012101; Biotinidase-like_euk.
DR InterPro; IPR040154; Biotinidase/VNN.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR043957; Vanin_C.
DR PANTHER; PTHR10609; PTHR10609; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF19018; Vanin_C; 1.
DR PIRSF; PIRSF011861; Biotinidase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..531
FT /note="Vanin-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019724"
FT PROPEP 532..558
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450614"
FT DOMAIN 33..299
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT LIPID 531
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 558 AA; 62342 MW; 7920621923BB7779 CRC64;
MSNTWWWLSV VLLILGLMPG MSQQAALAES DYYTAGVVEF KQSILSLSAW SDSLAGYVEI
INSENASATD IIVFPESTLN SAGSTTFVPN PEDQINPCLS DPNATYYEEF LVTLSCAARN
ASKYIVINLT EKQKCEDIPE DTRPCASNGL NVFNTNVVFD RQGVVVSRYR KVHLYGEAKN
STFLPELITF ETDFGVTFGH FICFDILFYT PAHQLIVEQG ITDFVYPAMW FSQLPFLTAV
QTQQGWAYAN DVNLLASGAS RPSIGNSGSG IYHGRSGTLT SVMRQDSGER AIYVAQVPKY
TRSRSLKKRA KRSLQEIQTR QVASSSSFYM KRDYVENYES ELLKLDEGTS GAINRTICQG
SFCCNFDIAW RSLGTATENG SYYSYRLGTY DGWRNENNVD ANYIRNCALF TCSGDSIDDC
GKLLPTEGEL QQSRVTFTRL AIGVTYPESR EFLLFPDTLQ DSLLPLEPSQ FEWSQRKPTE
DSYVQEVRFA LKETQELSNL LTFGIYGNYY DNECTFGVGT EEEQLACGYR SGSPGLRILG
GWLAMPLIIL AIARTMSS
