DFG5_CANAL
ID DFG5_CANAL Reviewed; 451 AA.
AC Q5ACZ2; A0A1D8PG43;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Mannan endo-1,6-alpha-mannosidase DFG5;
DE EC=3.2.1.101;
DE AltName: Full=Endo-alpha-1->6-D-mannanase DFG5;
DE Flags: Precursor;
GN Name=DFG5; OrderedLocusNames=CAALFM_C200520WA;
GN ORFNames=CaO19.2075, CaO19.9622;
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, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
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=12734798; DOI=10.1002/yea.988;
RA Lee S.A., Wormsley S., Kamoun S., Lee A.F., Joiner K., Wong B.;
RT "An analysis of the Candida albicans genome database for soluble secreted
RT proteins using computer-based prediction algorithms.";
RL Yeast 20:595-610(2003).
RN [6]
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 [7]
RP INDUCTION.
RX PubMed=16552442; DOI=10.1371/journal.ppat.0020021;
RA Bruno V.M., Kalachikov S., Subaran R., Nobile C.J., Kyratsous C.,
RA Mitchell A.P.;
RT "Control of the C. albicans cell wall damage response by transcriptional
RT regulator Cas5.";
RL PLoS Pathog. 2:E21-E21(2006).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=18765290; DOI=10.1016/j.fgb.2008.08.003;
RA Plaine A., Walker L., Da Costa G., Mora-Montes H.M., McKinnon A., Gow N.A.,
RA Gaillardin C., Munro C.A., Richard M.L.;
RT "Functional analysis of Candida albicans GPI-anchored proteins: roles in
RT cell wall integrity and caspofungin sensitivity.";
RL Fungal Genet. Biol. 45:1404-1414(2008).
RN [9]
RP INDUCTION.
RX PubMed=23731904; DOI=10.1016/j.ijmm.2013.05.003;
RA Yu Q., Ding X., Zhang B., Xu N., Cheng X., Qian K., Zhang B., Xing L.,
RA Li M.;
RT "The P-type ATPase Spf1 is required for endoplasmic reticulum functions and
RT cell wall integrity in Candida albicans.";
RL Int. J. Med. Microbiol. 303:257-266(2013).
CC -!- FUNCTION: Required for normal synthesis of the cell wall and alkaline
CC pH-induced hypha formation. {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: Secreted, cell wall
CC {ECO:0000269|PubMed:12912894}. Cell membrane
CC {ECO:0000269|PubMed:12912894}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:12912894}.
CC -!- INDUCTION: Induced by caspofungin. Expression is also regulated by
CC SPF1. {ECO:0000269|PubMed:16552442, ECO:0000269|PubMed:23731904}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- PTM: N-mannosylated.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased caspofungin sensitivity.
CC {ECO:0000269|PubMed:18765290}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 76 family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27106.1; -; Genomic_DNA.
DR RefSeq; XP_719522.1; XM_714429.1.
DR AlphaFoldDB; Q5ACZ2; -.
DR SMR; Q5ACZ2; -.
DR STRING; 237561.Q5ACZ2; -.
DR GeneID; 3638867; -.
DR KEGG; cal:CAALFM_C200520WA; -.
DR CGD; CAL0000185288; DFG5.
DR VEuPathDB; FungiDB:C2_00520W_A; -.
DR eggNOG; ENOG502QWHG; Eukaryota.
DR HOGENOM; CLU_025694_1_1_1; -.
DR InParanoid; Q5ACZ2; -.
DR OMA; QQSFKGY; -.
DR OrthoDB; 844700at2759; -.
DR PRO; PR:Q5ACZ2; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
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:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
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; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..429
FT /note="Mannan endo-1,6-alpha-mannosidase DFG5"
FT /id="PRO_0000424807"
FT PROPEP 430..451
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424808"
FT LIPID 429
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 451 AA; 50031 MW; 106267B6077A9CA0 CRC64;
MVSLQQLTIS ILLLFTASVQ SLDINVDDKD SICSAAKYVV QGIWNYYEGL KYGGTVGMFA
PPNYWWNAGE AFGGLVDFYT YCQSDNSTLE KLIYNGMYHQ AGENYNYIPS NQSMTEGNDD
QGVWGMAIME AVERNFTEPE SHSWLEMVQA VFNTMNARWD ADNCGGGLRW QIFTWNSGYD
YKNSISNGCL FHLAARLARY TGNSSVYVDT AEKVWKWMED VGFLTEEDNG DVRIYDGAKI
TNNCSSVTDL RWSYTYGVFM AGCAYLYNFT GDDVWLTRTN EIVQASLSYF FANKIMQETT
CQPQNKCNND QRSFRCLFSR CLGLTTQLAP ETKDRIREVL EASAEGAAKS CSGGSDGVTC
GENWAIDKWD GVYGLGEQTS ALEVMMALIV EPPLSVKTGG TNRTDYSAGT NSEDNANKNE
LTITGKDKAG AGVLTAIVLA VILGGAIWMI F
