Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Biotinidase

Gene

Btd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Biotin amide + H2O = biotin + NH3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891Proton acceptorPROSITE-ProRule annotation
Active sitei189 – 1891Proton donorPROSITE-ProRule annotation
Active sitei222 – 2221NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  • biotinidase activity Source: MGI

GO - Biological processi

  • biotin metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

SABIO-RKQ8CIF4.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotinidase (EC:3.5.1.12)
Short name:
Biotinase
Gene namesi
Name:Btd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1347001. Btd.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • nucleolus Source: MGI
  • perikaryon Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Chaini22 – 520499BiotinidasePRO_0000019708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)1 Publication
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence analysis
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ8CIF4.
MaxQBiQ8CIF4.
PaxDbiQ8CIF4.
PRIDEiQ8CIF4.

PTM databases

PhosphoSiteiQ8CIF4.

Expressioni

Gene expression databases

BgeeiQ8CIF4.
CleanExiMM_BTD.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000087608.

Structurei

3D structure databases

ProteinModelPortaliQ8CIF4.
SMRiQ8CIF4. Positions 35-519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 357324CN hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0806. Eukaryota.
COG0388. LUCA.
HOGENOMiHOG000007627.
HOVERGENiHBG003996.
InParanoidiQ8CIF4.
KOiK01435.
OrthoDBiEOG7HF1J0.
PhylomeDBiQ8CIF4.
TreeFamiTF323645.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view]
PANTHERiPTHR10609. PTHR10609. 1 hit.
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PIRSFiPIRSF011861. Biotinidase. 1 hit.
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CIF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGARTAPAL FFLGCSALAL GVSSASQEHR EAEYYVAAVY EHPSVLSPNP
60 70 80 90 100
LELVSRQEAL ELMKQNLDVY EQQVMAAAQK GVQIIVFPED GIHGFNFTRT
110 120 130 140 150
SIYPFLDFMP SPKLVRWNPC LEPFRFNDTE VLQRLSCMAI KGGMFLVANL
160 170 180 190 200
GTKQPCLSSD PGCPQDGRYQ FNTNVVFSDN GTLVDRYRKH NLYFEAAFDT
210 220 230 240 250
PANVDLITFD TPFAGKFGVF TCFDILFFDP AVRLLRDFEV KHIVYPTAWM
260 270 280 290 300
NQLPLLAAIE IQKAFATAFG VNVLAANIHH PTLGMTGSGI HTPLKSFWYH
310 320 330 340 350
DMDDPKGHLI IAQVATNPQG LTGTGNTTSE MDPSHRKFLK ILSGDPYCEK
360 370 380 390 400
DAQEVHCDEA AKWNVNVPPT FHSEMMYDNF TLVPVWGTEG HLQVCSNSLC
410 420 430 440 450
CHLLYERPTL SKELYALGVF DGLHTVHGTY YIQTCALVKC GGLGFDTCGQ
460 470 480 490 500
EITEAEGLFD FHLWGNFSTL YIFPLFLTSG MTLDTPDQLG WENDHYFLRK
510 520
RGLSSGLVTA ALYGRLYERK
Length:520
Mass (Da):58,154
Last modified:June 26, 2007 - v2
Checksum:i0929361BD1E3D746
GO

Sequence cautioni

The sequence AAH24051.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB24086.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE22509.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811G → V in BAE22509 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005506 mRNA. Translation: BAB24086.1. Different initiation.
AK135375 mRNA. Translation: BAE22509.1. Different initiation.
BC024051 mRNA. Translation: AAH24051.2. Different initiation.
RefSeqiNP_079571.1. NM_025295.4.
UniGeneiMm.282679.

Genome annotation databases

GeneIDi26363.
KEGGimmu:26363.
UCSCiuc007sxy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005506 mRNA. Translation: BAB24086.1. Different initiation.
AK135375 mRNA. Translation: BAE22509.1. Different initiation.
BC024051 mRNA. Translation: AAH24051.2. Different initiation.
RefSeqiNP_079571.1. NM_025295.4.
UniGeneiMm.282679.

3D structure databases

ProteinModelPortaliQ8CIF4.
SMRiQ8CIF4. Positions 35-519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000087608.

PTM databases

PhosphoSiteiQ8CIF4.

Proteomic databases

EPDiQ8CIF4.
MaxQBiQ8CIF4.
PaxDbiQ8CIF4.
PRIDEiQ8CIF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi26363.
KEGGimmu:26363.
UCSCiuc007sxy.2. mouse.

Organism-specific databases

CTDi686.
MGIiMGI:1347001. Btd.

Phylogenomic databases

eggNOGiKOG0806. Eukaryota.
COG0388. LUCA.
HOGENOMiHOG000007627.
HOVERGENiHBG003996.
InParanoidiQ8CIF4.
KOiK01435.
OrthoDBiEOG7HF1J0.
PhylomeDBiQ8CIF4.
TreeFamiTF323645.

Enzyme and pathway databases

SABIO-RKQ8CIF4.

Miscellaneous databases

ChiTaRSiBtd. mouse.
PROiQ8CIF4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CIF4.
CleanExiMM_BTD.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view]
PANTHERiPTHR10609. PTHR10609. 1 hit.
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PIRSFiPIRSF011861. Biotinidase. 1 hit.
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Muellerian duct and Placenta.
  2. "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].
    Strain: FVB/N.
    Tissue: Liver.
  3. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127.
    Strain: C57BL/6J.
    Tissue: Plasma.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung and Testis.

Entry informationi

Entry nameiBTD_MOUSE
AccessioniPrimary (citable) accession number: Q8CIF4
Secondary accession number(s): Q3UXQ4, Q9DAV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 26, 2007
Last modified: June 8, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.