ID BTD_HUMAN Reviewed; 543 AA. AC P43251; A6NHF2; B2R865; B4DFX1; B4DLJ9; B7Z7C9; F8W1Q3; Q96EM9; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 2. DT 27-MAR-2024, entry version 193. DE RecName: Full=Biotinidase {ECO:0000305}; DE Short=Biotinase; DE EC=3.5.1.12 {ECO:0000305|PubMed:9099842, ECO:0000305|PubMed:9654207}; DE Flags: Precursor; GN Name=BTD {ECO:0000312|HGNC:HGNC:1122}; 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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=7509806; DOI=10.1016/s0021-9258(17)37409-4; RA Cole H., Reynolds T.R., Lockyer J.M., Buck G.A., Denson T., Spence J.E., RA Hymes J., Wolf B.; RT "Human serum biotinidase. cDNA cloning, sequence, and characterization."; RL J. Biol. Chem. 269:6566-6570(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9530634; DOI=10.1007/s003359900760; RA Knight H.C., Reynolds T.R., Meyers G.A., Pomponio R.J., Buck G.A., Wolf B.; RT "Structure of the human biotinidase gene."; RL Mamm. Genome 9:327-330(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Amygdala, Pericardium, and 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-203; ASN-349 RP AND ASN-402. 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 [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-349 AND RP ASN-402. 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 [9] RP GLYCOSYLATION AT ASN-150. RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., RA Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core fucosylated RT glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [10] RP VARIANT BTD DEFICIENCY CYS-538, CHARACTERIZATION OF VARIANT BTD DEFICIENCY RP CYS-538, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9099842; DOI=10.1007/s004390050397; RA Pomponio R.J., Norrgard K.J., Hymes J., Reynolds T.R., Buck G.A., RA Baumgartner R., Suormala T., Wolf B.; RT "Arg538 to Cys mutation in a CpG dinucleotide of the human biotinidase gene RT is the second most common cause of profound biotinidase deficiency in RT symptomatic children."; RL Hum. Genet. 99:506-512(1997). RN [11] RP VARIANTS BTD DEFICIENCY VAL-128; THR-171; TYR-228; ARG-323; HIS-444; RP ASP-451; HIS-456; MET-532 AND CYS-538, CHARACTERIZATION OF VARIANT BTD RP DEFICIENCY HIS-444, CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9654207; DOI=10.1007/s004390050742; RA Swango K.L., Demirkol M., Huener G., Pronicka E., Sykut-Cegielska J., RA Schulze A., Mayatepek E., Wolf B.; RT "Partial biotinidase deficiency is usually due to the D444H mutation in the RT biotinidase gene."; RL Hum. Genet. 102:571-575(1998). RN [12] RP VARIANTS BTD DEFICIENCY THR-171 AND HIS-444. RX PubMed=10206677; RX DOI=10.1002/(sici)1098-1004(1998)11:5<410::aid-humu10>3.0.co;2-8; RA Norrgard K.J., Pomponio R.J., Swango K.L., Hymes J., Reynolds T., RA Buck G.A., Wolf B.; RT "Double mutation (A171T and D444H) is a common cause of profound RT biotinidase deficiency in children ascertained by newborn screening in the RT United States."; RL Hum. Mutat. 11:410-410(1998). CC -!- FUNCTION: Catalytic release of biotin from biocytin, the product of CC biotin-dependent carboxylases degradation. {ECO:0000305|PubMed:9099842, CC ECO:0000305|PubMed:9654207}. CC -!- CATALYTIC ACTIVITY: CC Reaction=biocytin + H2O = biotin + L-lysine; Xref=Rhea:RHEA:77171, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:57586, CC ChEBI:CHEBI:195545; EC=3.5.1.12; CC Evidence={ECO:0000305|PubMed:9099842, ECO:0000305|PubMed:9654207}; CC -!- CATALYTIC ACTIVITY: CC Reaction=biotin amide + H2O = biotin + NH4(+); Xref=Rhea:RHEA:13081, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16615, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:57586; Evidence={ECO:0000305|PubMed:9099842, CC ECO:0000305|PubMed:9654207}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13082; CC Evidence={ECO:0000305|PubMed:9099842, ECO:0000305|PubMed:9654207}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000305|PubMed:9099842, ECO:0000305|PubMed:9654207}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P43251-1; Sequence=Displayed; CC Name=2; CC IsoId=P43251-2; Sequence=VSP_054925; CC Name=3; CC IsoId=P43251-3; Sequence=VSP_054926; CC Name=4; CC IsoId=P43251-4; Sequence=VSP_055921; CC -!- DISEASE: Biotinidase deficiency (BTD deficiency) [MIM:253260]: A CC juvenile form of multiple carboxylase deficiency, an autosomal CC recessive disorder of biotin metabolism, characterized by ketoacidosis, CC hyperammonemia, excretion of abnormal organic acid metabolites, and CC dermatitis. Biotinidase deficiency is characterized by seizures, CC hypotonia, skin rash, alopecia, ataxia, hearing loss, and optic CC atrophy. If untreated, symptoms usually become progressively worse, and CC coma and death may occur. {ECO:0000269|PubMed:10206677, CC ECO:0000269|PubMed:9099842, ECO:0000269|PubMed:9654207}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. CC BTD/VNN family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator. CC {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; U03274; AAC04318.1; -; mRNA. DR EMBL; AF018631; AAC21679.1; -; Genomic_DNA. DR EMBL; AF018630; AAC21679.1; JOINED; Genomic_DNA. DR EMBL; AK294301; BAG57582.1; -; mRNA. DR EMBL; AK297033; BAG59561.1; -; mRNA. DR EMBL; AK301838; BAH13565.1; -; mRNA. DR EMBL; AK313252; BAG36062.1; -; mRNA. DR EMBL; AC027129; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64254.1; -; Genomic_DNA. DR EMBL; BC012099; AAH12099.1; -; mRNA. DR CCDS; CCDS63565.1; -. [P43251-4] DR PIR; A54362; A54362. DR RefSeq; NP_000051.1; NM_000060.4. DR RefSeq; NP_001268652.1; NM_001281723.2. [P43251-4] DR RefSeq; NP_001268653.1; NM_001281724.2. [P43251-4] DR RefSeq; NP_001268654.1; NM_001281725.2. [P43251-4] DR RefSeq; NP_001310511.1; NM_001323582.1. [P43251-4] DR RefSeq; XP_011532343.1; XM_011534041.2. DR RefSeq; XP_016862577.1; XM_017007088.1. DR AlphaFoldDB; P43251; -. DR SMR; P43251; -. DR BioGRID; 107151; 36. DR IntAct; P43251; 8. DR STRING; 9606.ENSP00000500193; -. DR BindingDB; P43251; -. DR ChEMBL; CHEMBL4802066; -. DR GlyConnect; 1043; 15 N-Linked glycans (5 sites). DR GlyCosmos; P43251; 6 sites, 21 glycans. DR GlyGen; P43251; 7 sites, 27 N-linked glycans (5 sites), 1 O-linked glycan (1 site). DR iPTMnet; P43251; -. DR PhosphoSitePlus; P43251; -. DR SwissPalm; P43251; -. DR BioMuta; BTD; -. DR DMDM; 226693503; -. DR CPTAC; CPTAC-655; -. DR CPTAC; non-CPTAC-2634; -. DR CPTAC; non-CPTAC-2635; -. DR EPD; P43251; -. DR jPOST; P43251; -. DR MassIVE; P43251; -. DR MaxQB; P43251; -. DR PaxDb; 9606-ENSP00000400995; -. DR PeptideAtlas; P43251; -. DR ProteomicsDB; 1193; -. DR ProteomicsDB; 29669; -. DR ProteomicsDB; 4540; -. DR ProteomicsDB; 55605; -. [P43251-1] DR Pumba; P43251; -. DR Antibodypedia; 26848; 258 antibodies from 28 providers. DR DNASU; 686; -. DR Ensembl; ENST00000303498.10; ENSP00000306477.6; ENSG00000169814.17. [P43251-4] DR Ensembl; ENST00000427382.2; ENSP00000397113.2; ENSG00000169814.17. [P43251-4] DR Ensembl; ENST00000436193.6; ENSP00000394277.2; ENSG00000169814.17. [P43251-4] DR Ensembl; ENST00000437172.6; ENSP00000400995.2; ENSG00000169814.17. [P43251-4] DR Ensembl; ENST00000449107.7; ENSP00000388212.2; ENSG00000169814.17. [P43251-4] DR Ensembl; ENST00000643237.3; ENSP00000495254.2; ENSG00000169814.17. [P43251-4] DR Ensembl; ENST00000646371.1; ENSP00000495866.1; ENSG00000169814.17. [P43251-4] DR GeneID; 686; -. DR KEGG; hsa:686; -. DR MANE-Select; ENST00000643237.3; ENSP00000495254.2; NM_001370658.1; NP_001357587.1. [P43251-4] DR UCSC; uc003cah.5; human. [P43251-1] DR AGR; HGNC:1122; -. DR CTD; 686; -. DR DisGeNET; 686; -. DR GeneCards; BTD; -. DR GeneReviews; BTD; -. DR HGNC; HGNC:1122; BTD. DR HPA; ENSG00000169814; Tissue enhanced (liver). DR MalaCards; BTD; -. DR MIM; 253260; phenotype. DR MIM; 609019; gene. DR neXtProt; NX_P43251; -. DR OpenTargets; ENSG00000169814; -. DR Orphanet; 79241; Biotinidase deficiency. DR PharmGKB; PA25443; -. DR VEuPathDB; HostDB:ENSG00000169814; -. DR eggNOG; KOG0806; Eukaryota. DR GeneTree; ENSGT00390000013823; -. DR HOGENOM; CLU_033209_0_0_1; -. DR InParanoid; P43251; -. DR OrthoDB; 4006627at2759; -. DR PhylomeDB; P43251; -. DR TreeFam; TF323645; -. DR BRENDA; 3.5.1.12; 2681. DR PathwayCommons; P43251; -. DR Reactome; R-HSA-196780; Biotin transport and metabolism. DR Reactome; R-HSA-3371598; Defective BTD causes biotidinase deficiency. DR SABIO-RK; P43251; -. DR SignaLink; P43251; -. DR BioGRID-ORCS; 686; 13 hits in 1160 CRISPR screens. DR ChiTaRS; BTD; human. DR GenomeRNAi; 686; -. DR Pharos; P43251; Tbio. DR PRO; PR:P43251; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P43251; Protein. DR Bgee; ENSG00000169814; Expressed in islet of Langerhans and 187 other cell types or tissues. DR ExpressionAtlas; P43251; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0047708; F:biotinidase activity; TAS:Reactome. DR GO; GO:0006768; P:biotin metabolic process; IBA:GO_Central. DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc. DR CDD; cd07567; biotinidase_like; 1. DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 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:SF14; BIOTINIDASE; 1. DR PANTHER; PTHR10609; BIOTINIDASE-RELATED; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR Pfam; PF19018; Vanin_C; 1. DR PIRSF; PIRSF011861; Biotinidase; 1. DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. DR Genevisible; P43251; HS. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Disease variant; KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal. FT SIGNAL 1..41 FT CHAIN 42..543 FT /note="Biotinidase" FT /id="PRO_0000019707" FT DOMAIN 72..351 FT /note="CN hydrolase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" FT ACT_SITE 112 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" FT ACT_SITE 212 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" FT ACT_SITE 245 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054" FT CARBOHYD 119 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 150 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218" FT CARBOHYD 203 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 349 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 402 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 489 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..20 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055921" FT VAR_SEQ 1..14 FT /note="MAHAHIQGGRRAKS -> MARKETQLIIKMNHLA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054925" FT VAR_SEQ 1..13 FT /note="MAHAHIQGGRRAK -> MPEGGGTSRRLLPMQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054926" FT VARIANT 128 FT /note="F -> V (in BTD deficiency; dbSNP:rs397514355)" FT /evidence="ECO:0000269|PubMed:9654207" FT /id="VAR_005113" FT VARIANT 171 FT /note="A -> T (in BTD deficiency; dbSNP:rs13073139)" FT /evidence="ECO:0000269|PubMed:10206677, FT ECO:0000269|PubMed:9654207" FT /id="VAR_005114" FT VARIANT 228 FT /note="D -> Y (in BTD deficiency; dbSNP:rs397514380)" FT /evidence="ECO:0000269|PubMed:9654207" FT /id="VAR_005115" FT VARIANT 323 FT /note="H -> R (in BTD deficiency; partial; FT dbSNP:rs397507176)" FT /evidence="ECO:0000269|PubMed:9654207" FT /id="VAR_005116" FT VARIANT 391 FT /note="P -> S (in dbSNP:rs35034250)" FT /id="VAR_056238" FT VARIANT 444 FT /note="D -> H (in BTD deficiency; profound and partial; 52% FT decrease in biotinyl-transferase activity; FT dbSNP:rs13078881)" FT /evidence="ECO:0000269|PubMed:10206677, FT ECO:0000269|PubMed:9654207" FT /id="VAR_005117" FT VARIANT 451 FT /note="G -> D (in BTD deficiency; partial; FT dbSNP:rs397514419)" FT /evidence="ECO:0000269|PubMed:9654207" FT /id="VAR_005118" FT VARIANT 456 FT /note="Q -> H (in BTD deficiency; dbSNP:rs80338685)" FT /evidence="ECO:0000269|PubMed:9654207" FT /id="VAR_005119" FT VARIANT 532 FT /note="T -> M (in BTD deficiency; dbSNP:rs104893688)" FT /evidence="ECO:0000269|PubMed:9654207" FT /id="VAR_005120" FT VARIANT 538 FT /note="R -> C (in BTD deficiency; not detectable protein FT levels; loss of biotinyl-transferase activity; FT dbSNP:rs80338686)" FT /evidence="ECO:0000269|PubMed:9099842, FT ECO:0000269|PubMed:9654207" FT /id="VAR_005121" FT CONFLICT 379 FT /note="H -> Y (in Ref. 3; BAH13565)" FT /evidence="ECO:0000305" SQ SEQUENCE 543 AA; 61133 MW; 1A999893A0784944 CRC64; MAHAHIQGGR RAKSRFVVCI MSGARSKLAL FLCGCYVVAL GAHTGEESVA DHHEAEYYVA AVYEHPSILS LNPLALISRQ EALELMNQNL DIYEQQVMTA AQKDVQIIVF PEDGIHGFNF TRTSIYPFLD FMPSPQVVRW NPCLEPHRFN DTEVLQRLSC MAIRGDMFLV ANLGTKEPCH SSDPRCPKDG RYQFNTNVVF SNNGTLVDRY RKHNLYFEAA FDVPLKVDLI TFDTPFAGRF GIFTCFDILF FDPAIRVLRD YKVKHVVYPT AWMNQLPLLA AIEIQKAFAV AFGINVLAAN VHHPVLGMTG SGIHTPLESF WYHDMENPKS HLIIAQVAKN PVGLIGAENA TGETDPSHSK FLKILSGDPY CEKDAQEVHC DEATKWNVNA PPTFHSEMMY DNFTLVPVWG KEGYLHVCSN GLCCYLLYER PTLSKELYAL GVFDGLHTVH GTYYIQVCAL VRCGGLGFDT CGQEITEATG IFEFHLWGNF STSYIFPLFL TSGMTLEVPD QLGWENDHYF LRKSRLSSGL VTAALYGRLY ERD //