ID   DIAC_RAT                Reviewed;         367 AA.
AC   Q01460;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Di-N-acetylchitobiase;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=Ctbs; Synonyms=Ctb;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-32.
RC   TISSUE=Liver;
RX   PubMed=1527079; DOI=10.1016/s0021-9258(18)41818-2;
RA   Fisher K.J., Aronson N.N. Jr.;
RT   "Cloning and expression of the cDNA sequence encoding the lysosomal
RT   glycosidase di-N-acetylchitobiase.";
RL   J. Biol. Chem. 267:19607-19616(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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).
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.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR   EMBL; M95768; AAA40924.1; -; mRNA.
DR   EMBL; BC088129; AAH88129.1; -; mRNA.
DR   PIR; C44102; C44102.
DR   RefSeq; NP_112285.1; NM_031023.1.
DR   AlphaFoldDB; Q01460; -.
DR   SMR; Q01460; -.
DR   STRING; 10116.ENSRNOP00000020972; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GlyGen; Q01460; 4 sites.
DR   PaxDb; Q01460; -.
DR   PRIDE; Q01460; -.
DR   Ensembl; ENSRNOT00000020972; ENSRNOP00000020972; ENSRNOG00000015573.
DR   GeneID; 81652; -.
DR   KEGG; rno:81652; -.
DR   CTD; 1486; -.
DR   RGD; 621338; Ctbs.
DR   eggNOG; KOG2806; Eukaryota.
DR   GeneTree; ENSGT00390000012891; -.
DR   HOGENOM; CLU_061189_1_0_1; -.
DR   InParanoid; Q01460; -.
DR   OMA; YKWIMKQ; -.
DR   OrthoDB; 826687at2759; -.
DR   PhylomeDB; Q01460; -.
DR   TreeFam; TF332677; -.
DR   PRO; PR:Q01460; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000015573; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q01460; RN.
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; IDA:RGD.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; TAS:RGD.
DR   GO; GO:0006032; P:chitin catabolic process; IDA:RGD.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IDA:RGD.
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   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:1527079"
FT   CHAIN           24..367
FT                   /note="Di-N-acetylchitobiase"
FT                   /id="PRO_0000011963"
FT   DOMAIN          24..367
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   367 AA;  41531 MW;  29AB8BE4FC157C16 CRC64;
     MALSDLLELT LLLLLPLLER LSAEDCPCSE ASLCRPIRHH RDFEVFVFDV GQKTWKSYDW
     SQITTVAVFG KYDSELMCYA HSKGARVVLK GDVALKDIIN PTFRASWIAQ KVALAKAQHM
     DGINIDIEQE VDCSSPEYEA LTALVRETTE GFHREIEGSQ VTFDVAWSPK GIDKRCYNYT
     GIADACDFLF VMSYDEQSQI WSECIAAANA PYNQTLTGYG DYLRMGISPR KLVMGIPWYG
     YDYICLNLSK DDVCAIAKVP FRGAPCSDAA GHQVPYRVIM KQVNSSVSGS QWNQDQQAPY
     YNYKDPTGRL HQVWYDNPRS ISLKAAFVKH YGLRGIGMWN ANCLDYSDDA LAREQTEEMW
     GALRPRL