DIAC_MOUSE
ID DIAC_MOUSE Reviewed; 366 AA.
AC Q8R242; Q9D7V4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Di-N-acetylchitobiase;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=Ctbs;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-366 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Involved in the degradation of asparagine-linked
CC glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-
CC acetylglucosamine chitobiose core from the reducing end of the bond, it
CC requires prior cleavage by glycosylasparaginase (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R242-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R242-2; Sequence=VSP_013909;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; AK008791; BAB25896.1; -; mRNA.
DR EMBL; AC124987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022594; AAH22594.1; -; mRNA.
DR CCDS; CCDS17902.1; -. [Q8R242-2]
DR CCDS; CCDS80048.1; -. [Q8R242-1]
DR RefSeq; NP_001280601.1; NM_001293672.1. [Q8R242-1]
DR RefSeq; NP_083112.1; NM_028836.4. [Q8R242-2]
DR AlphaFoldDB; Q8R242; -.
DR SMR; Q8R242; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyGen; Q8R242; 5 sites.
DR PhosphoSitePlus; Q8R242; -.
DR CPTAC; non-CPTAC-3571; -.
DR EPD; Q8R242; -.
DR MaxQB; Q8R242; -.
DR PeptideAtlas; Q8R242; -.
DR PRIDE; Q8R242; -.
DR ProteomicsDB; 279690; -. [Q8R242-1]
DR ProteomicsDB; 279691; -. [Q8R242-2]
DR Antibodypedia; 4472; 162 antibodies from 27 providers.
DR DNASU; 74245; -.
DR Ensembl; ENSMUST00000029840; ENSMUSP00000029840; ENSMUSG00000028189. [Q8R242-2]
DR Ensembl; ENSMUST00000061937; ENSMUSP00000059167; ENSMUSG00000028189. [Q8R242-1]
DR GeneID; 74245; -.
DR KEGG; mmu:74245; -.
DR UCSC; uc008rrg.2; mouse. [Q8R242-2]
DR UCSC; uc008rrh.2; mouse. [Q8R242-1]
DR CTD; 1486; -.
DR MGI; MGI:1921495; Ctbs.
DR VEuPathDB; HostDB:ENSMUSG00000028189; -.
DR GeneTree; ENSGT00390000012891; -.
DR HOGENOM; CLU_061189_1_0_1; -.
DR InParanoid; Q8R242; -.
DR OMA; YKWIMKQ; -.
DR PhylomeDB; Q8R242; -.
DR TreeFam; TF332677; -.
DR BioGRID-ORCS; 74245; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q8R242; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R242; protein.
DR Bgee; ENSMUSG00000028189; Expressed in proximal tubule and 199 other tissues.
DR ExpressionAtlas; Q8R242; baseline and differential.
DR Genevisible; Q8R242; MM.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; ISO:MGI.
DR GO; GO:0006032; P:chitin catabolic process; ISO:MGI.
DR GO; GO:0009313; P:oligosaccharide catabolic process; ISO:MGI.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..366
FT /note="Di-N-acetylchitobiase"
FT /id="PRO_0000011962"
FT DOMAIN 23..366
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 251..304
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013909"
SQ SEQUENCE 366 AA; 41295 MW; 1075F6EAD7AD024A CRC64;
MALCGLPEFT LLLLPLLARL SAGDCPCSEA ALCQPIRHRP DFEVFVFDVG QKTWKSYDWS
QITTVAAFGK YDPELMCYAH SKGARVVLKG DISLKNIIDP TFRASWIAQK VDLAKAQYMD
GINIDIEQEV NCSSPEYEAL TALVKETTES FQREIEGSQV TFDVAWSPKR IDKRCYNYTG
IADACDFLFV MSYDEQSQIW SECIAAANAP YNQTLTGYID YIKMGISPKK LVMGVPWYGY
DYICLNLSKD DICTITKVPF RGAPCSDAAG HQVPYKVIMK QVNGSVSGSQ WNKDQQAPYY
NYKDPAGRFH QVWYDNPQSI SLKAAYVKNY GLRGIGMWNA NCLDYSDDAL AREQTQEMWG
ALKPRL
