ID   BTD_RAT                 Reviewed;         521 AA.
AC   Q5FVF9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Biotinidase;
DE            Short=Biotinase;
DE            EC=3.5.1.12 {ECO:0000250|UniProtKB:P43251};
DE   Flags: Precursor;
GN   Name=Btd {ECO:0000312|EMBL:AAH90017.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:AAH90017.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver {ECO:0000312|EMBL:AAH90017.1};
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).
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}.
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DR   EMBL; BC090017; AAH90017.1; -; mRNA.
DR   RefSeq; NP_001012047.1; NM_001012047.1.
DR   RefSeq; XP_006252673.1; XM_006252611.2.
DR   RefSeq; XP_006252674.1; XM_006252612.1.
DR   RefSeq; XP_006252676.1; XM_006252614.1.
DR   RefSeq; XP_006252677.1; XM_006252615.2.
DR   RefSeq; XP_006252678.1; XM_006252616.2.
DR   RefSeq; XP_006252679.1; XM_006252617.1.
DR   RefSeq; XP_006252680.1; XM_006252618.2.
DR   RefSeq; XP_006252684.1; XM_006252622.3.
DR   RefSeq; XP_008769221.1; XM_008770999.1.
DR   RefSeq; XP_017455568.1; XM_017600079.1.
DR   AlphaFoldDB; Q5FVF9; -.
DR   SMR; Q5FVF9; -.
DR   STRING; 10116.ENSRNOP00000057779; -.
DR   GlyGen; Q5FVF9; 3 sites.
DR   PaxDb; Q5FVF9; -.
DR   PRIDE; Q5FVF9; -.
DR   GeneID; 306262; -.
DR   KEGG; rno:306262; -.
DR   UCSC; RGD:1305316; rat.
DR   CTD; 686; -.
DR   RGD; 1305316; Btd.
DR   eggNOG; KOG0806; Eukaryota.
DR   HOGENOM; CLU_033209_0_0_1; -.
DR   InParanoid; Q5FVF9; -.
DR   PhylomeDB; Q5FVF9; -.
DR   Reactome; R-RNO-196780; Biotin transport and metabolism.
DR   SABIO-RK; Q5FVF9; -.
DR   PRO; PR:Q5FVF9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q5FVF9; RN.
DR   GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0043204; C:perikaryon; ISO:RGD.
DR   GO; GO:0047708; F:biotinidase activity; ISO:RGD.
DR   GO; GO:0006768; P:biotin metabolic process; ISO:RGD.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..521
FT                   /note="Biotinidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000292882"
FT   DOMAIN          50..329
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        90
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        223
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   521 AA;  58021 MW;  809E61A25C76B269 CRC64;
     MSGARTAHAL VFLLGCSALA LGVCSASLEH GEAEYYVAAV YEHRSVLSPN PLELSSRQQA
     LELMKQNLDV YEQQVMAAAQ KGAHIIVFPE DGIHGFNFTR TSIYPFLDLM PSPRLVSWNP
     CLEPFRFNDT EVLQRLSCMA IKGKMFLVAN LGTKQPCLGS DPGCPQDGRY QFNTNVAFSD
     NGTLVGRYRK HNLYFEEAFD SPADVDLTTF DTPFAGKFGM FTCFDILFFD PAVRLLRDFE
     VKHIAYPTAW MNQLPLLAAI EIQKAFATAF GVTVLAANIH HPTLGMTGSG IHTPLKSFWY
     HNMDDPEGHL IIARVATNPQ GLVGTENTTS EMDPSHRKFL KVLSGDPYCE KDAQEVRCDE
     AAKWNLNAPP TFHSEMMYDN FTLVPVWGKE GHLQVCSNSL CCHLLFERPA LSKELYALGV
     FDGLHTVHGT YYVQACALVK CGGAGFETCG QEISEAEGLF DFHLWGNFST LYVFPLFLTS
     GMTLDTPDQL GWESDHYFLR KRGLSSGLVT AALYGRLYER N