CDA2_CRYNB
ID CDA2_CRYNB Reviewed; 458 AA.
AC Q55U20; Q96W71;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Chitin deacetylase 2 {ECO:0000305};
DE EC=3.5.1.41 {ECO:0000250|UniProtKB:J9VND2};
DE Flags: Precursor;
GN Name=CDA2 {ECO:0000250|UniProtKB:J9VND2};
GN Synonyms=MP98 {ECO:0000303|PubMed:11504924};
GN OrderedLocusNames=CNBD2840 {ECO:0000312|EMBL:EAL21229.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643 {ECO:0000312|Proteomes:UP000001435};
RN [1] {ECO:0000312|EMBL:AAK50770.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-71, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, AND BIOTECHNOLOGY.
RC STRAIN=cap67;
RX PubMed=11504924; DOI=10.1073/pnas.181331398;
RA Levitz S.M., Nong S., Mansour M.K., Huang C., Specht C.A.;
RT "Molecular characterization of a mannoprotein with homology to chitin
RT deacetylases that stimulates T cell responses to Cryptococcus neoformans.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10422-10427(2001).
RN [2] {ECO:0000312|Proteomes:UP000001435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A {ECO:0000312|Proteomes:UP000001435};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC residues in chitin to form chitosan and acetate (By similarity).
CC Chitosan is required to anchor melanin to the cell wall, for
CC maintenance of cell wall integrity, and for cytokinesis (By
CC similarity). {ECO:0000250|UniProtKB:J9VND2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate +
CC chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-
CC COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57704; EC=3.5.1.41;
CC Evidence={ECO:0000250|UniProtKB:J9VND2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC Evidence={ECO:0000250|UniProtKB:J9VND2};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q6DWK3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11504924}. Secreted,
CC cell wall {ECO:0000250|UniProtKB:J9VND2}. Cell membrane
CC {ECO:0000250|UniProtKB:J9VND2}; Lipid-anchor, GPI-anchor {ECO:0000255}.
CC Note=GPI-anchored cell membrane protein (GPI-PMP) (By similarity). Non-
CC covalently associated to the cell wall by means independent of both its
CC GPI-anchor and beta-1,6-glucan (By similarity). Cell membrane
CC localization is critical for effective deacetylase activity (By
CC similarity). {ECO:0000250|UniProtKB:J9VND2}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11504924}.
CC -!- BIOTECHNOLOGY: Potential vaccine candidate; elicits T-cell activation
CC when injected in mice. {ECO:0000269|PubMed:11504924}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; AF361369; AAK50770.1; -; mRNA.
DR EMBL; AAEY01000020; EAL21229.1; -; Genomic_DNA.
DR RefSeq; XP_775876.1; XM_770783.1.
DR AlphaFoldDB; Q55U20; -.
DR SMR; Q55U20; -.
DR EnsemblFungi; EAL21229; EAL21229; CNBD2840.
DR GeneID; 4935673; -.
DR KEGG; cnb:CNBD2840; -.
DR VEuPathDB; FungiDB:CNBD2840; -.
DR HOGENOM; CLU_035539_0_0_1; -.
DR Proteomes; UP000001435; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Cell wall;
KW Cell wall biogenesis/degradation; Chitin degradation; Cobalt;
KW Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..51
FT /evidence="ECO:0000269|PubMed:11504924"
FT CHAIN 52..427
FT /note="Chitin deacetylase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5004250730"
FT PROPEP 428..458
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451811"
FT DOMAIN 158..348
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT REGION 382..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 165
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 166
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 215
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 219
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT BINDING 256
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000250|UniProtKB:Q6DWK3"
FT LIPID 427
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 458 AA; 48462 MW; 4B10BF71E8C64770 CRC64;
MIPSTAAAAL LTLTAGVALA HPGCGGQEIG RRNVGGPMVY RRDVTDEASA AASTDVNTEC
TAYGYAPVTE IASSFPTIWE TASILSNDTE GQQLFATINS TLNTKLPNDV PHGTPTGDWT
GVNYNSSDPD CWWTHNKCTT PASDTGLEAD ITIVPEPMTW GLGFDDGPNC SHNALYNLLS
ENNQKATMFF IGSNVMDWPL QAMRAHDEGH QICVHTWSHQ YMTALSNEVV FAELYYTQKA
IKAVLGVTPQ CWRPPYGDVD NRVRMIAQAL NLTTIIWSDD TDDWAAGTDG VTEQDVTDNY
QAVIDKAGNG TYTTHGPVVL NHELTNYTMS VFMTMFPKIK SAFSYIVPMC TAYNITQPYL
ESNVTCPNFE TYISGVTNIS SSTTQKDGSS STNTSSSGSG SAAGSASATS SSDDSSSSGS
ASASSSSSNA SSGALGMFDG LSGVGLVLSG VVAGVMLL
