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P43251 (BTD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotinidase

Short name=Biotinase
EC=3.5.1.12
Gene names
Name:BTD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.

Catalytic activity

Biotin amide + H2O = biotin + NH3.

Subcellular location

Secretedextracellular space.

Involvement in disease

Biotinidase deficiency (BTD deficiency) [MIM:253260]: A juvenile form of multiple carboxylase deficiency, an autosomal recessive disorder of biotin metabolism, characterized by ketoacidosis, hyperammonemia, excretion of abnormal organic acid metabolites, and dermatitis. Biotinidase deficiency is characterized by seizures, hypotonia, skin rash, alopecia, ataxia, hearing loss, and optic atrophy. If untreated, symptoms usually become progressively worse, and coma and death may occur.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the carbon-nitrogen hydrolase superfamily. BTD/VNN family.

Contains 1 CN hydrolase domain.

Caution

It is uncertain whether Met-1 or Met-21 is the initiator.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43251-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P43251-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MAHAHIQGGRRAKS → MARKETQLIIKMNHLA
Note: No experimental confirmation available.
Isoform 3 (identifier: P43251-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MAHAHIQGGRRAK → MPEGGGTSRRLLPMQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141
Chain42 – 543502Biotinidase
PRO_0000019707

Regions

Domain57 – 363307CN hydrolase

Sites

Active site1121Proton acceptor By similarity
Active site2121Proton donor By similarity
Active site2451Nucleophile By similarity

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...) Ref.7 Ref.8
Glycosylation1501N-linked (GlcNAc...) (complex) Ref.7 Ref.8 Ref.9
Glycosylation2031N-linked (GlcNAc...) Ref.7
Glycosylation3491N-linked (GlcNAc...) Ref.7 Ref.8
Glycosylation4021N-linked (GlcNAc...) Ref.7 Ref.8
Glycosylation4891N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 1414MAHAH…RRAKS → MARKETQLIIKMNHLA in isoform 2.
VSP_054925
Alternative sequence1 – 1313MAHAH…GRRAK → MPEGGGTSRRLLPMQ in isoform 3.
VSP_054926
Natural variant1281F → V in BTD deficiency. Ref.11
VAR_005113
Natural variant1711A → T in BTD deficiency. Ref.11 Ref.12
Corresponds to variant rs13073139 [ dbSNP | Ensembl ].
VAR_005114
Natural variant2281D → Y in BTD deficiency. Ref.11
VAR_005115
Natural variant3231H → R in BTD deficiency; partial. Ref.11
VAR_005116
Natural variant3911P → S.
Corresponds to variant rs35034250 [ dbSNP | Ensembl ].
VAR_056238
Natural variant4441D → H in BTD deficiency; profound and partial; 52% decrease in activity. Ref.11 Ref.12
Corresponds to variant rs13078881 [ dbSNP | Ensembl ].
VAR_005117
Natural variant4511G → D in BTD deficiency; partial. Ref.11
VAR_005118
Natural variant4561Q → H in BTD deficiency. Ref.11
Corresponds to variant rs80338685 [ dbSNP | Ensembl ].
VAR_005119
Natural variant5321T → M in BTD deficiency. Ref.11
Corresponds to variant rs104893688 [ dbSNP | Ensembl ].
VAR_005120
Natural variant5381R → C in BTD deficiency. Ref.10 Ref.11
VAR_005121

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 14, 2009. Version 2.
Checksum: 1A999893A0784944

FASTA54361,133
        10         20         30         40         50         60 
MAHAHIQGGR RAKSRFVVCI MSGARSKLAL FLCGCYVVAL GAHTGEESVA DHHEAEYYVA 

        70         80         90        100        110        120 
AVYEHPSILS LNPLALISRQ EALELMNQNL DIYEQQVMTA AQKDVQIIVF PEDGIHGFNF 

       130        140        150        160        170        180 
TRTSIYPFLD FMPSPQVVRW NPCLEPHRFN DTEVLQRLSC MAIRGDMFLV ANLGTKEPCH 

       190        200        210        220        230        240 
SSDPRCPKDG RYQFNTNVVF SNNGTLVDRY RKHNLYFEAA FDVPLKVDLI TFDTPFAGRF 

       250        260        270        280        290        300 
GIFTCFDILF FDPAIRVLRD YKVKHVVYPT AWMNQLPLLA AIEIQKAFAV AFGINVLAAN 

       310        320        330        340        350        360 
VHHPVLGMTG SGIHTPLESF WYHDMENPKS HLIIAQVAKN PVGLIGAENA TGETDPSHSK 

       370        380        390        400        410        420 
FLKILSGDPY CEKDAQEVHC DEATKWNVNA PPTFHSEMMY DNFTLVPVWG KEGYLHVCSN 

       430        440        450        460        470        480 
GLCCYLLYER PTLSKELYAL GVFDGLHTVH GTYYIQVCAL VRCGGLGFDT CGQEITEATG 

       490        500        510        520        530        540 
IFEFHLWGNF STSYIFPLFL TSGMTLEVPD QLGWENDHYF LRKSRLSSGL VTAALYGRLY 


ERD 

« Hide

Isoform 2 [UniParc].

Checksum: BD12F620C4FF7EE9
Show »

FASTA54561,510
Isoform 3 [UniParc].

Checksum: AC348AE5C8DF373C
Show »

FASTA54561,330

References

« Hide 'large scale' references
[1]"Human serum biotinidase. cDNA cloning, sequence, and characterization."
Cole H., Reynolds T.R., Lockyer J.M., Buck G.A., Denson T., Spence J.E., Hymes J., Wolf B.
J. Biol. Chem. 269:6566-6570(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Structure of the human biotinidase gene."
Knight H.C., Reynolds T.R., Meyers G.A., Pomponio R.J., Buck G.A., Wolf B.
Mamm. Genome 9:327-330(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Amygdala, Pericardium and Umbilical cord blood.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[7]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-203; ASN-349 AND ASN-402.
Tissue: Plasma.
[8]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119; ASN-150; ASN-349 AND ASN-402.
Tissue: Liver.
[9]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-150.
[10]"Arg538 to Cys mutation in a CpG dinucleotide of the human biotinidase gene is the second most common cause of profound biotinidase deficiency in symptomatic children."
Pomponio R.J., Norrgard K.J., Hymes J., Reynolds T.R., Buck G.A., Baumgartner R., Suormala T., Wolf B.
Hum. Genet. 99:506-512(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BTD DEFICIENCY CYS-538.
[11]"Partial biotinidase deficiency is usually due to the D444H mutation in the biotinidase gene."
Swango K.L., Demirkol M., Huener G., Pronicka E., Sykut-Cegielska J., Schulze A., Mayatepek E., Wolf B.
Hum. Genet. 102:571-575(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BTD DEFICIENCY VAL-128; THR-171; TYR-228; ARG-323; HIS-444; ASP-451; HIS-456; MET-532 AND CYS-538.
[12]"Double mutation (A171T and D444H) is a common cause of profound biotinidase deficiency in children ascertained by newborn screening in the United States."
Norrgard K.J., Pomponio R.J., Swango K.L., Hymes J., Reynolds T., Buck G.A., Wolf B.
Hum. Mutat. 11:410-410(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BTD DEFICIENCY THR-171 AND HIS-444.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03274 mRNA. Translation: AAC04318.1.
AF018631, AF018630 Genomic DNA. Translation: AAC21679.1.
AK294301 mRNA. Translation: BAG57582.1.
AK297033 mRNA. Translation: BAG59561.1.
AK313252 mRNA. Translation: BAG36062.1.
AC027129 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64254.1.
BC012099 mRNA. Translation: AAH12099.1.
CCDSCCDS2628.1.
PIRA54362.
RefSeqNP_000051.1. NM_000060.3.
NP_001268652.1. NM_001281723.1.
NP_001268653.1. NM_001281724.1.
UniGeneHs.517830.

3D structure databases

ProteinModelPortalP43251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107151. 1 interaction.
IntActP43251. 1 interaction.
STRING9606.ENSP00000306477.

PTM databases

PhosphoSiteP43251.

Polymorphism databases

DMDM226693503.

Proteomic databases

MaxQBP43251.
PaxDbP43251.
PRIDEP43251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303498; ENSP00000306477; ENSG00000169814.
ENST00000437172; ENSP00000400995; ENSG00000169814.
ENST00000449107; ENSP00000388212; ENSG00000169814.
GeneID686.
KEGGhsa:686.
UCSCuc003cah.3. human. [P43251-1]

Organism-specific databases

CTD686.
GeneCardsGC03P015621.
GeneReviewsBTD.
HGNCHGNC:1122. BTD.
HPAHPA052275.
MIM253260. phenotype.
609019. gene.
neXtProtNX_P43251.
Orphanet79241. Biotinidase deficiency.
PharmGKBPA25443.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270742.
HOGENOMHOG000007627.
HOVERGENHBG003996.
InParanoidP43251.
KOK01435.
PhylomeDBP43251.
TreeFamTF323645.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP43251.

Gene expression databases

ArrayExpressP43251.
BgeeP43251.
CleanExHS_BTD.
GenevestigatorP43251.

Family and domain databases

Gene3D3.60.110.10. 1 hit.
InterProIPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view]
PANTHERPTHR10609. PTHR10609. 1 hit.
PfamPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PIRSFPIRSF011861. Biotinidase. 1 hit.
SUPFAMSSF56317. SSF56317. 1 hit.
PROSITEPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi686.
NextBio2824.
PROP43251.
SOURCESearch...

Entry information

Entry nameBTD_HUMAN
AccessionPrimary (citable) accession number: P43251
Secondary accession number(s): A6NHF2 expand/collapse secondary AC list , B2R865, B4DFX1, B4DLJ9, Q96EM9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 14, 2009
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM