DIAC_HUMAN
ID DIAC_HUMAN Reviewed; 385 AA.
AC Q01459; Q5VX50;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Di-N-acetylchitobiase;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=CTBS; Synonyms=CTB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
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 [GENOMIC DNA].
RX PubMed=10336991; DOI=10.1093/glycob/9.6.589;
RA Liu B., Ahmad W., Aronson N.N. Jr.;
RT "Structure of the human gene for lysosomal di-N-acetylchitobiase.";
RL Glycobiology 9:589-593(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
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; M95767; AAA35684.1; -; mRNA.
DR EMBL; AF085706; AAC35852.1; -; Genomic_DNA.
DR EMBL; AF085700; AAC35852.1; JOINED; Genomic_DNA.
DR EMBL; AF085701; AAC35852.1; JOINED; Genomic_DNA.
DR EMBL; AF085702; AAC35852.1; JOINED; Genomic_DNA.
DR EMBL; AF085703; AAC35852.1; JOINED; Genomic_DNA.
DR EMBL; AF085704; AAC35852.1; JOINED; Genomic_DNA.
DR EMBL; AF085705; AAC35852.1; JOINED; Genomic_DNA.
DR EMBL; AL359762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73232.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73233.1; -; Genomic_DNA.
DR EMBL; BC126333; AAI26334.1; -; mRNA.
DR EMBL; BC126335; AAI26336.1; -; mRNA.
DR CCDS; CCDS698.1; -.
DR PIR; A44102; A44102.
DR RefSeq; NP_004379.1; NM_004388.2.
DR AlphaFoldDB; Q01459; -.
DR SMR; Q01459; -.
DR BioGRID; 107868; 58.
DR IntAct; Q01459; 7.
DR STRING; 9606.ENSP00000359664; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GlyConnect; 1173; 3 N-Linked glycans (1 site).
DR GlyGen; Q01459; 4 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q01459; -.
DR PhosphoSitePlus; Q01459; -.
DR BioMuta; CTBS; -.
DR DMDM; 399376; -.
DR EPD; Q01459; -.
DR jPOST; Q01459; -.
DR MassIVE; Q01459; -.
DR PaxDb; Q01459; -.
DR PeptideAtlas; Q01459; -.
DR PRIDE; Q01459; -.
DR ProteomicsDB; 57956; -.
DR Antibodypedia; 4472; 162 antibodies from 27 providers.
DR DNASU; 1486; -.
DR Ensembl; ENST00000370630.6; ENSP00000359664.4; ENSG00000117151.13.
DR GeneID; 1486; -.
DR KEGG; hsa:1486; -.
DR MANE-Select; ENST00000370630.6; ENSP00000359664.4; NM_004388.3; NP_004379.1.
DR UCSC; uc001dka.3; human.
DR CTD; 1486; -.
DR DisGeNET; 1486; -.
DR GeneCards; CTBS; -.
DR HGNC; HGNC:2496; CTBS.
DR HPA; ENSG00000117151; Low tissue specificity.
DR MIM; 600873; gene.
DR neXtProt; NX_Q01459; -.
DR OpenTargets; ENSG00000117151; -.
DR PharmGKB; PA26997; -.
DR VEuPathDB; HostDB:ENSG00000117151; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00390000012891; -.
DR HOGENOM; CLU_061189_1_0_1; -.
DR InParanoid; Q01459; -.
DR OMA; YKWIMKQ; -.
DR OrthoDB; 826687at2759; -.
DR PhylomeDB; Q01459; -.
DR TreeFam; TF332677; -.
DR PathwayCommons; Q01459; -.
DR SignaLink; Q01459; -.
DR BioGRID-ORCS; 1486; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; CTBS; human.
DR GeneWiki; CTBS; -.
DR GenomeRNAi; 1486; -.
DR Pharos; Q01459; Tbio.
DR PRO; PR:Q01459; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q01459; protein.
DR Bgee; ENSG00000117151; Expressed in choroid plexus epithelium and 168 other tissues.
DR ExpressionAtlas; Q01459; baseline and differential.
DR Genevisible; Q01459; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
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 Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000250"
FT CHAIN 39..385
FT /note="Di-N-acetylchitobiase"
FT /id="PRO_0000011961"
FT DOMAIN 39..385
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 143
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VARIANT 274
FT /note="V -> I (in dbSNP:rs15911)"
FT /id="VAR_049197"
FT VARIANT 310
FT /note="D -> Y (in dbSNP:rs3768249)"
FT /id="VAR_020160"
SQ SEQUENCE 385 AA; 43760 MW; 0A9D14C8B26B52EE CRC64;
MSRPQLRRWR LVSSPPSGVP GLALLALLAL LALRLAAGTD CPCPEPELCR PIRHHPDFEV
FVFDVGQKTW KSYDWSQITT VATFGKYDSE LMCYAHSKGA RVVLKGDVSL KDIIDPAFRA
SWIAQKLNLA KTQYMDGINI DIEQEVNCLS PEYDALTALV KETTDSFHRE IEGSQVTFDV
AWSPKNIDRR CYNYTGIADA CDFLFVMSYD EQSQIWSECI AAANAPYNQT LTGYNDYIKM
SINPKKLVMG VPWYGYDYTC LNLSEDHVCT IAKVPFRGAP CSDAAGRQVP YKTIMKQINS
SISGNLWDKD QRAPYYNYKD PAGHFHQVWY DNPQSISLKA TYIQNYRLRG IGMWNANCLD
YSGDAVAKQQ TEEMWEVLKP KLLQR
