BTD_MOUSE
ID BTD_MOUSE Reviewed; 520 AA.
AC Q8CIF4; Q3UXQ4; Q9DAV0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Biotinidase;
DE Short=Biotinase;
DE EC=3.5.1.12 {ECO:0000250|UniProtKB:P43251};
DE Flags: Precursor;
GN Name=Btd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalytic release of biotin from biocytin, the product of
CC biotin-dependent carboxylases degradation.
CC {ECO:0000250|UniProtKB:P43251}.
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;
CC Evidence={ECO:0000250|UniProtKB:P43251};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13082;
CC Evidence={ECO:0000250|UniProtKB:P43251};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P43251}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC BTD/VNN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24051.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB24086.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE22509.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK005506; BAB24086.1; ALT_INIT; mRNA.
DR EMBL; AK135375; BAE22509.1; ALT_INIT; mRNA.
DR EMBL; BC024051; AAH24051.2; ALT_INIT; mRNA.
DR RefSeq; NP_079571.1; NM_025295.4.
DR AlphaFoldDB; Q8CIF4; -.
DR SMR; Q8CIF4; -.
DR BioGRID; 204923; 17.
DR STRING; 10090.ENSMUSP00000087608; -.
DR GlyConnect; 2155; 1 N-Linked glycan (1 site).
DR GlyGen; Q8CIF4; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8CIF4; -.
DR PhosphoSitePlus; Q8CIF4; -.
DR EPD; Q8CIF4; -.
DR jPOST; Q8CIF4; -.
DR MaxQB; Q8CIF4; -.
DR PaxDb; Q8CIF4; -.
DR PeptideAtlas; Q8CIF4; -.
DR PRIDE; Q8CIF4; -.
DR ProteomicsDB; 273713; -.
DR DNASU; 26363; -.
DR GeneID; 26363; -.
DR KEGG; mmu:26363; -.
DR UCSC; uc007sxy.2; mouse.
DR CTD; 686; -.
DR MGI; MGI:1347001; Btd.
DR eggNOG; KOG0806; Eukaryota.
DR InParanoid; Q8CIF4; -.
DR OrthoDB; 1276751at2759; -.
DR PhylomeDB; Q8CIF4; -.
DR TreeFam; TF323645; -.
DR Reactome; R-MMU-196780; Biotin transport and metabolism.
DR SABIO-RK; Q8CIF4; -.
DR BioGRID-ORCS; 26363; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Btd; mouse.
DR PRO; PR:Q8CIF4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CIF4; protein.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IDA:MGI.
DR GO; GO:0047708; F:biotinidase activity; IMP:MGI.
DR GO; GO:0006768; P:biotin metabolic process; IMP:MGI.
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 Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..520
FT /note="Biotinidase"
FT /id="PRO_0000019708"
FT DOMAIN 49..333
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 81
FT /note="G -> V (in Ref. 1; BAE22509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58154 MW; 0929361BD1E3D746 CRC64;
MSGARTAPAL FFLGCSALAL GVSSASQEHR EAEYYVAAVY EHPSVLSPNP LELVSRQEAL
ELMKQNLDVY EQQVMAAAQK GVQIIVFPED GIHGFNFTRT SIYPFLDFMP SPKLVRWNPC
LEPFRFNDTE VLQRLSCMAI KGGMFLVANL GTKQPCLSSD PGCPQDGRYQ FNTNVVFSDN
GTLVDRYRKH NLYFEAAFDT PANVDLITFD TPFAGKFGVF TCFDILFFDP AVRLLRDFEV
KHIVYPTAWM NQLPLLAAIE IQKAFATAFG VNVLAANIHH PTLGMTGSGI HTPLKSFWYH
DMDDPKGHLI IAQVATNPQG LTGTGNTTSE MDPSHRKFLK ILSGDPYCEK DAQEVHCDEA
AKWNVNVPPT FHSEMMYDNF TLVPVWGTEG HLQVCSNSLC CHLLYERPTL SKELYALGVF
DGLHTVHGTY YIQTCALVKC GGLGFDTCGQ EITEAEGLFD FHLWGNFSTL YIFPLFLTSG
MTLDTPDQLG WENDHYFLRK RGLSSGLVTA ALYGRLYERK