HSP21_CANAL
ID HSP21_CANAL Reviewed; 189 AA.
AC Q5AHH4; A0A1D8PH06;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Small heat shock protein 21;
GN Name=HSP21; OrderedLocusNames=CAALFM_C204010CA;
GN ORFNames=CaO19.822, CaO19.8442;
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 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 [5]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16389478; DOI=10.1007/s11046-005-0167-2;
RA Vediyappan G., Chaffin W.L.;
RT "Non-glucan attached proteins of Candida albicans biofilm formed on various
RT surfaces.";
RL Mycopathologia 161:3-10(2006).
RN [6]
RP INDUCTION.
RX PubMed=17588813; DOI=10.1016/j.ijmm.2007.03.020;
RA Kusch H., Engelmann S., Bode R., Albrecht D., Morschhauser J., Hecker M.;
RT "A proteomic view of Candida albicans yeast cell metabolism in exponential
RT and stationary growth phases.";
RL Int. J. Med. Microbiol. 298:291-318(2008).
RN [7]
RP FUNCTION.
RX PubMed=22685587; DOI=10.1371/journal.pone.0038584;
RA Mayer F.L., Wilson D., Jacobsen I.D., Miramon P., Slesiona S.,
RA Bohovych I.M., Brown A.J., Hube B.;
RT "Small but crucial: the novel small heat shock protein Hsp21 mediates
RT stress adaptation and virulence in Candida albicans.";
RL PLoS ONE 7:E38584-E38584(2012).
RN [8]
RP FUNCTION.
RX PubMed=23533680; DOI=10.1371/journal.pone.0060417;
RA Mayer F.L., Wilson D., Hube B.;
RT "Hsp21 potentiates antifungal drug tolerance in Candida albicans.";
RL PLoS ONE 8:E60417-E60417(2013).
CC -!- FUNCTION: Heat shock protein required for pathogenicity. Mediates
CC thermotolerance and adaptation to oxidative stress and ethanol-induced
CC stress. Required for invasive growth and filament formation under
CC various filament inducing conditions. Plays a role in the capacity of
CC damaging human-derived endothelial and oral epithelial cells during
CC infection. Potentiates resistance to antifungal drugs, as well as
CC resistance to killing by human neutrophils. Plays a major role in
CC trehalose homeostasis in response to elevated temperatures. Regulates
CC CEK1 activation by phosphorylation in response to elevated
CC temperatures. {ECO:0000269|PubMed:22685587,
CC ECO:0000269|PubMed:23533680}.
CC -!- INDUCTION: Only expressed in stationary phase. Expression is increased
CC in the absence of adenylyl cyclase and in biofilms.
CC {ECO:0000269|PubMed:15269278, ECO:0000269|PubMed:16389478,
CC ECO:0000269|PubMed:17588813}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; CP017624; AOW27428.1; -; Genomic_DNA.
DR RefSeq; XP_720946.1; XM_715853.2.
DR AlphaFoldDB; Q5AHH4; -.
DR SMR; Q5AHH4; -.
DR BioGRID; 1220397; 2.
DR STRING; 237561.Q5AHH4; -.
DR PRIDE; Q5AHH4; -.
DR GeneID; 3637364; -.
DR KEGG; cal:CAALFM_C204010CA; -.
DR CGD; CAL0000174399; HSP21.
DR VEuPathDB; FungiDB:C2_04010C_A; -.
DR eggNOG; ENOG502RQBX; Eukaryota.
DR HOGENOM; CLU_114640_0_0_1; -.
DR InParanoid; Q5AHH4; -.
DR OMA; LECDEEN; -.
DR OrthoDB; 1543154at2759; -.
DR PRO; PR:Q5AHH4; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0070414; P:trehalose metabolism in response to heat stress; IMP:CGD.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Stress response; Virulence.
FT CHAIN 1..189
FT /note="Small heat shock protein 21"
FT /id="PRO_0000424598"
FT DOMAIN 77..183
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 26..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 189 AA; 21495 MW; 65DC479318CE3609 CRC64;
MSWFGFFDPD FDDFFGRPRK YATEVPPNFN PRKIAQGDNG KGQQVSRYGA GAGHPHRALA
RRDDFFDDFW KNFSSGKYFV GFDDNVKTTE ESDKYVVSYD QENLSPDEVN VDFDKQENEL
IITVTQETEK DGTKKSSTFH SNLKFEKPVN FDDISAEIGE QGVQVTLPKV HADHEKIVNI
PISKAAAKK
