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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
 
 
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