DCW1_CANAL
ID DCW1_CANAL Reviewed; 452 AA.
AC Q5AD78; A0A1D8PGD3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Mannan endo-1,6-alpha-mannosidase DCW1;
DE EC=3.2.1.101;
DE AltName: Full=Defective cell wall 1;
DE AltName: Full=Endo-alpha-1->6-D-mannanase DCW1;
DE AltName: Full=GPI-anchored protein 51;
DE Flags: Precursor;
GN Name=DCW1; Synonyms=PGA51; OrderedLocusNames=CAALFM_C201360CA;
GN ORFNames=CaO19.1989, CaO19.9540;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=12912894; DOI=10.1128/ec.2.4.746-755.2003;
RA Spreghini E., Davis D.A., Subaran R., Kim M., Mitchell A.P.;
RT "Roles of Candida albicans Dfg5p and Dcw1p cell surface proteins in growth
RT and hypha formation.";
RL Eukaryot. Cell 2:746-755(2003).
RN [5]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [6]
RP INDUCTION.
RX PubMed=15269278; DOI=10.1091/mbc.e04-02-0144;
RA Harcus D., Nantel A., Marcil A., Rigby T., Whiteway M.;
RT "Transcription profiling of cyclic AMP signaling in Candida albicans.";
RL Mol. Biol. Cell 15:4490-4499(2004).
RN [7]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
CC -!- FUNCTION: Probable mannosidase required for normal synthesis of the
CC cell wall. {ECO:0000269|PubMed:12912894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in
CC unbranched (1->6)-mannans.; EC=3.2.1.101;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- INDUCTION: Induced by HAP43 and up-regulated in absence of CYR1.
CC {ECO:0000269|PubMed:15269278, ECO:0000269|PubMed:21592964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 76 family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27182.1; -; Genomic_DNA.
DR RefSeq; XP_719439.1; XM_714346.1.
DR AlphaFoldDB; Q5AD78; -.
DR SMR; Q5AD78; -.
DR STRING; 237561.Q5AD78; -.
DR GeneID; 3638842; -.
DR KEGG; cal:CAALFM_C201360CA; -.
DR CGD; CAL0000197643; DCW1.
DR VEuPathDB; FungiDB:C2_01360C_A; -.
DR eggNOG; ENOG502QSWP; Eukaryota.
DR HOGENOM; CLU_025694_1_2_1; -.
DR InParanoid; Q5AD78; -.
DR OMA; TWNNGYD; -.
DR OrthoDB; 844700at2759; -.
DR PRO; PR:Q5AD78; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0046658; C:anchored component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0008496; F:mannan endo-1,6-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007117; P:budding cell bud growth; IBA:GO_Central.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IBA:GO_Central.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR005198; Glyco_hydro_76.
DR InterPro; IPR014480; Mannan-1_6-alpha_mannosidase.
DR PANTHER; PTHR12145; PTHR12145; 1.
DR Pfam; PF03663; Glyco_hydro_76; 1.
DR PIRSF; PIRSF016302; Man_a_manosd; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..431
FT /note="Mannan endo-1,6-alpha-mannosidase DCW1"
FT /id="PRO_0000424805"
FT PROPEP 432..452
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424806"
FT LIPID 431
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
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 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 452 AA; 50348 MW; 12A17AC5718B65B0 CRC64;
MKFSIYLIIS LFSSFSHAIW LDTNNETTIR EDCNIIAKGL LDYYEGTKYG GVIGMFSWPY
YWWEAGGAWG SLIDYTFYFD NDTLVPLITD ALLYQTGDDD NYIPLNQSTT EGNDDQAFWG
IAVMAAAERN FTNPKDPTKA WLTLAQAVFN TMQARWDTET CNGGLRWQIF QWNSGYDYKN
SVSNGALFHL AARLARYTGN DSYVVWAERV WDWMYGVGLL TEQNWWFVYD GVKIANNCSN
ITKYQWSYNQ GLMLAGCAYL YNYTEEEKWY NYTIKLLESA QVFFKNISGS MVMYEAACQP
SNSCNNDQRS FKAYFSRFLG LTSVLVPQTE PVITKWLVDS ANGAAGSCSG GSDGVTCGLS
WTDWSQGWDG KWGLGEQMSA LEVMQNLMVH KRPAPYTADT GGSSIGNPAA GYGKLTSDAT
PLSIDGGDKA GAGIITAIIG ASLVGSCVWL IL
