BTD_HUMAN
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 03-AUG-2022, entry version 184.
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=biotin amide + H2O = biotin + NH4(+); Xref=Rhea:RHEA:13081,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16615, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57586; EC=3.5.1.12; 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; CCDS2628.1; -. [P43251-4]
DR CCDS; CCDS63563.1; -. [P43251-4]
DR CCDS; CCDS63564.1; -. [P43251-4]
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. [P43251-4]
DR RefSeq; XP_016862577.1; XM_017007088.1. [P43251-4]
DR AlphaFoldDB; P43251; -.
DR SMR; P43251; -.
DR BioGRID; 107151; 27.
DR IntAct; P43251; 8.
DR STRING; 9606.ENSP00000400995; -.
DR ChEMBL; CHEMBL4802066; -.
DR GlyConnect; 1043; 15 N-Linked glycans (5 sites).
DR GlyGen; P43251; 6 sites, 22 N-linked glycans (5 sites).
DR iPTMnet; P43251; -.
DR PhosphoSitePlus; 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; P43251; -.
DR PeptideAtlas; P43251; -.
DR PRIDE; P43251; -.
DR ProteomicsDB; 1193; -.
DR ProteomicsDB; 29669; -.
DR ProteomicsDB; 4540; -.
DR ProteomicsDB; 55605; -. [P43251-1]
DR Antibodypedia; 26848; 227 antibodies from 28 providers.
DR DNASU; 686; -.
DR Ensembl; ENST00000303498.10; ENSP00000306477.6; ENSG00000169814.16. [P43251-4]
DR Ensembl; ENST00000383778.5; ENSP00000373288.4; ENSG00000169814.16. [P43251-4]
DR Ensembl; ENST00000427382.2; ENSP00000397113.2; ENSG00000169814.16. [P43251-4]
DR Ensembl; ENST00000437172.6; ENSP00000400995.2; ENSG00000169814.16. [P43251-4]
DR Ensembl; ENST00000449107.7; ENSP00000388212.2; ENSG00000169814.16. [P43251-4]
DR Ensembl; ENST00000643237.3; ENSP00000495254.2; ENSG00000169814.16. [P43251-4]
DR Ensembl; ENST00000646371.1; ENSP00000495866.1; ENSG00000169814.16. [P43251-4]
DR Ensembl; ENST00000672065.1; ENSP00000500403.1; ENSG00000169814.16. [P43251-1]
DR Ensembl; ENST00000672112.1; ENSP00000500193.1; ENSG00000169814.16. [P43251-2]
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 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; 1276751at2759; -.
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 1081 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 185 other tissues.
DR ExpressionAtlas; P43251; baseline and differential.
DR Genevisible; P43251; HS.
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; -; 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 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
