VNN1_HUMAN
ID VNN1_HUMAN Reviewed; 513 AA.
AC O95497; A8K310; Q4JFW6; Q4VAS7; Q4VAS8; Q4VAS9; Q9UF16; Q9UJF4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Pantetheinase;
DE EC=3.5.1.92 {ECO:0000269|PubMed:11491533, ECO:0000269|PubMed:25478849};
DE AltName: Full=Pantetheine hydrolase;
DE AltName: Full=Tiff66;
DE AltName: Full=Vascular non-inflammatory molecule 1;
DE Short=Vanin-1;
DE Flags: Precursor;
GN Name=VNN1;
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 [MRNA], AND VARIANT ILE-26.
RC TISSUE=Liver;
RX PubMed=9790769; DOI=10.1006/geno.1998.5481;
RA Galland F., Malergue F., Bazin H., Mattei M.-G., Aurrand-Lions M.,
RA Theillet C., Naquet P.;
RT "Two human genes related to murine vanin-1 are located on the long arm of
RT human chromosome 6.";
RL Genomics 53:203-213(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-26.
RA Prehn S., Friedrichson T., Henske A., Boehm S., Hartmann E.,
RA Kurzchalia T.V.;
RT "Human Tiff66.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-26.
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-26; THR-63; SER-131;
RP LEU-136; ASN-146; ASP-296; GLU-325; ALA-336 AND THR-373.
RG NIEHS SNPs program;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-131.
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 [7]
RP IDENTIFICATION.
RX PubMed=10567687; DOI=10.1016/s0014-5793(99)01439-8;
RA Maras B., Barra D., Dupre S., Pitari G.;
RT "Is pantetheinase the actual identity of mouse and human vanin-1
RT proteins?";
RL FEBS Lett. 461:149-152(1999).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=11491533; DOI=10.1007/s002510100327;
RA Martin F., Malergue F., Pitari G., Philippe J.M., Philips S., Chabret C.,
RA Granjeaud S., Mattei M.G., Mungall A.J., Naquet P., Galland F.;
RT "Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode
RT isoforms of pantetheinase ectoenzymes.";
RL Immunogenetics 53:296-306(2001).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38 AND ASN-353.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-283; ASN-315 AND
RP ASN-353.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP TISSUE SPECIFICITY, AND INDUCTION BY CYTOKINES.
RX PubMed=19322213; DOI=10.1038/jid.2009.67;
RA Jansen P.A.M., Kamsteeg M., Rodijk-Olthuis D.,
RA van Vlijmen-Willems I.M.J.J., de Jongh G.J., Bergers M., Tjabringa G.S.,
RA Zeeuwen P.L.J.M., Schalkwijk J.;
RT "Expression of the vanin gene family in normal and inflamed human skin:
RT induction by proinflammatory cytokines.";
RL J. Invest. Dermatol. 129:2167-2174(2009).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-353.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 22-513 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-38; ASN-130;
RP ASN-200; ASN-315 AND ASN-353, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF
RP GLU-79 AND LYS-178.
RX PubMed=25478849; DOI=10.1107/s1399004714022767;
RA Boersma Y.L., Newman J., Adams T.E., Cowieson N., Krippner G., Bozaoglu K.,
RA Peat T.S.;
RT "The structure of vanin 1: a key enzyme linking metabolic disease and
RT inflammation.";
RL Acta Crystallogr. D 70:3320-3329(2014).
CC -!- FUNCTION: Amidohydrolase that hydrolyzes specifically one of the
CC carboamide linkages in D-pantetheine thus recycling pantothenic acid
CC (vitamin B5) and releasing cysteamine. {ECO:0000269|PubMed:10567687,
CC ECO:0000269|PubMed:11491533, ECO:0000269|PubMed:25478849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantetheine + H2O = (R)-pantothenate + cysteamine;
CC Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753,
CC ChEBI:CHEBI:29032, ChEBI:CHEBI:58029; EC=3.5.1.92;
CC Evidence={ECO:0000269|PubMed:11491533, ECO:0000269|PubMed:25478849};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25478849}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11491533};
CC Lipid-anchor, GPI-anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in spleen,
CC kidney and blood. Overexpressed in lesional psoriatic skin.
CC {ECO:0000269|PubMed:19322213}.
CC -!- INDUCTION: By Th17/Th1 type cytokines, but not by Th2-type.
CC {ECO:0000269|PubMed:19322213}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC BTD/VNN family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/vnn1/";
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; AJ132099; CAA10568.1; -; mRNA.
DR EMBL; U39664; AAF21453.1; -; mRNA.
DR EMBL; AK290425; BAF83114.1; -; mRNA.
DR EMBL; DQ100297; AAY88742.1; -; Genomic_DNA.
DR EMBL; AL032821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096265; AAH96265.1; -; mRNA.
DR EMBL; BC096266; AAH96266.1; -; mRNA.
DR EMBL; BC096267; AAH96267.1; -; mRNA.
DR EMBL; BC096268; AAH96268.1; -; mRNA.
DR CCDS; CCDS5159.1; -.
DR RefSeq; NP_004657.2; NM_004666.2.
DR PDB; 4CYF; X-ray; 2.25 A; A/B=22-513.
DR PDB; 4CYG; X-ray; 2.30 A; A/B=22-513.
DR PDB; 4CYY; X-ray; 2.89 A; A=27-513.
DR PDB; 7SLV; X-ray; 2.13 A; A=22-483.
DR PDB; 7SLX; X-ray; 2.35 A; A=22-483.
DR PDB; 7SLY; X-ray; 2.17 A; A=22-483.
DR PDBsum; 4CYF; -.
DR PDBsum; 4CYG; -.
DR PDBsum; 4CYY; -.
DR PDBsum; 7SLV; -.
DR PDBsum; 7SLX; -.
DR PDBsum; 7SLY; -.
DR AlphaFoldDB; O95497; -.
DR SMR; O95497; -.
DR BioGRID; 114395; 13.
DR STRING; 9606.ENSP00000356905; -.
DR BindingDB; O95497; -.
DR ChEMBL; CHEMBL4739843; -.
DR GuidetoPHARMACOLOGY; 3063; -.
DR GlyConnect; 1966; 12 N-Linked glycans (4 sites).
DR GlyGen; O95497; 7 sites, 12 N-linked glycans (4 sites).
DR iPTMnet; O95497; -.
DR PhosphoSitePlus; O95497; -.
DR BioMuta; VNN1; -.
DR jPOST; O95497; -.
DR MassIVE; O95497; -.
DR PaxDb; O95497; -.
DR PeptideAtlas; O95497; -.
DR PRIDE; O95497; -.
DR ProteomicsDB; 50924; -.
DR Antibodypedia; 32934; 254 antibodies from 32 providers.
DR DNASU; 8876; -.
DR Ensembl; ENST00000367928.5; ENSP00000356905.4; ENSG00000112299.8.
DR GeneID; 8876; -.
DR KEGG; hsa:8876; -.
DR MANE-Select; ENST00000367928.5; ENSP00000356905.4; NM_004666.3; NP_004657.2.
DR UCSC; uc003qdo.4; human.
DR CTD; 8876; -.
DR DisGeNET; 8876; -.
DR GeneCards; VNN1; -.
DR HGNC; HGNC:12705; VNN1.
DR HPA; ENSG00000112299; Group enriched (gallbladder, intestine, liver).
DR MIM; 603570; gene.
DR neXtProt; NX_O95497; -.
DR OpenTargets; ENSG00000112299; -.
DR PharmGKB; PA37321; -.
DR VEuPathDB; HostDB:ENSG00000112299; -.
DR eggNOG; KOG0806; Eukaryota.
DR GeneTree; ENSGT00390000013823; -.
DR HOGENOM; CLU_033209_2_0_1; -.
DR InParanoid; O95497; -.
DR OMA; YEKDWAS; -.
DR OrthoDB; 1276751at2759; -.
DR PhylomeDB; O95497; -.
DR TreeFam; TF323645; -.
DR BRENDA; 3.5.1.92; 2681.
DR PathwayCommons; O95497; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 8876; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; VNN1; human.
DR GeneWiki; VNN1; -.
DR GenomeRNAi; 8876; -.
DR Pharos; O95497; Tchem.
DR PRO; PR:O95497; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95497; protein.
DR Bgee; ENSG00000112299; Expressed in jejunal mucosa and 121 other tissues.
DR Genevisible; O95497; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0017159; F:pantetheine hydrolase activity; IDA:UniProtKB.
DR GO; GO:0002526; P:acute inflammatory response; ISS:BHF-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0002544; P:chronic inflammatory response; ISS:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; ISS:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; ISS:BHF-UCL.
DR GO; GO:0015939; P:pantothenate metabolic process; IDA:UniProtKB.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:BHF-UCL.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; ISS:BHF-UCL.
DR GO; GO:0006979; P:response to oxidative stress; TAS:BHF-UCL.
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 3D-structure; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..491
FT /note="Pantetheinase"
FT /id="PRO_0000019712"
FT PROPEP 492..513
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019713"
FT DOMAIN 39..306
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 79
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT ECO:0000305|PubMed:25478849"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT ECO:0000305|PubMed:25478849"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT ECO:0000269|PubMed:25478849"
FT LIPID 491
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0007744|PDB:4CYF, ECO:0007744|PDB:4CYG,
FT ECO:0007744|PDB:4CYY"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0007744|PDB:4CYF, ECO:0007744|PDB:4CYG,
FT ECO:0007744|PDB:4CYY"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0007744|PDB:4CYY"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0007744|PDB:4CYF, ECO:0007744|PDB:4CYG,
FT ECO:0007744|PDB:4CYY"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0007744|PDB:4CYF, ECO:0007744|PDB:4CYG,
FT ECO:0007744|PDB:4CYY"
FT VARIANT 26
FT /note="T -> I (in dbSNP:rs2294757)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9790769, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_023529"
FT VARIANT 63
FT /note="A -> T"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023967"
FT VARIANT 131
FT /note="N -> S (in dbSNP:rs2272996)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_023968"
FT VARIANT 136
FT /note="V -> L (in dbSNP:rs45610032)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023969"
FT VARIANT 146
FT /note="D -> N (in dbSNP:rs45624336)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023970"
FT VARIANT 296
FT /note="E -> D (in dbSNP:rs45523444)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023971"
FT VARIANT 325
FT /note="A -> E (in dbSNP:rs34535050)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023972"
FT VARIANT 336
FT /note="T -> A (in dbSNP:rs45562238)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023973"
FT VARIANT 373
FT /note="I -> T (in dbSNP:rs35938565)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023974"
FT MUTAGEN 79
FT /note="E->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25478849"
FT MUTAGEN 178
FT /note="K->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:25478849"
FT CONFLICT 101
FT /note="D -> N (in Ref. 6; AAH96268)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> I (in Ref. 4; AAY88742)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="E -> D (in Ref. 2; AAF21453)"
FT /evidence="ECO:0000305"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 46..69
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:7SLV"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:7SLV"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:7SLV"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:7SLV"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4CYY"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:7SLV"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 349..358
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 361..371
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 378..387
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 393..402
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:7SLV"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:7SLV"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:7SLV"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:7SLV"
SQ SEQUENCE 513 AA; 57012 MW; 018D2417C12E403F CRC64;
MTTQLPAYVA ILLFYVSRAS CQDTFTAAVY EHAAILPNAT LTPVSREEAL ALMNRNLDIL
EGAITSAADQ GAHIIVTPED AIYGWNFNRD SLYPYLEDIP DPEVNWIPCN NRNRFGQTPV
QERLSCLAKN NSIYVVANIG DKKPCDTSDP QCPPDGRYQY NTDVVFDSQG KLVARYHKQN
LFMGENQFNV PKEPEIVTFN TTFGSFGIFT CFDILFHDPA VTLVKDFHVD TIVFPTAWMN
VLPHLSAVEF HSAWAMGMRV NFLASNIHYP SKKMTGSGIY APNSSRAFHY DMKTEEGKLL
LSQLDSHPSH SAVVNWTSYA SSIEALSSGN KEFKGTVFFD EFTFVKLTGV AGNYTVCQKD
LCCHLSYKMS ENIPNEVYAL GAFDGLHTVE GRYYLQICTL LKCKTTNLNT CGDSAETAST
RFEMFSLSGT FGTQYVFPEV LLSENQLAPG EFQVSTDGRL FSLKPTSGPV LTVTLFGRLY
EKDWASNASS GLTAQARIIM LIVIAPIVCS LSW
