DNJ1_CRYNH
ID DNJ1_CRYNH Reviewed; 522 AA.
AC J9VKM5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Tetratricopeptide repeat and J domain-containing co-chaperone DNJ1 {ECO:0000303|PubMed:34566931};
DE Flags: Precursor;
GN Name=DNJ1 {ECO:0000303|PubMed:34566931}; ORFNames=CNAG_01347;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=34566931; DOI=10.3389/fmicb.2021.727039;
RA Horianopoulos L.C., Lee C.W.J., Hu G., Caza M., Kronstad J.W.;
RT "Dnj1 promotes virulence in Cryptococcus neoformans by maintaining robust
RT endoplasmic reticulum homeostasis under temperature stress.";
RL Front. Microbiol. 12:727039-727039(2021).
CC -!- FUNCTION: Endoplasmic reticulum co-chaperone crucial for survival and
CC virulence factor production at elevated temperatures representative of
CC febrile patients during infection (PubMed:34566931). Contributes to
CC virulence in a mouse model of cryptococcosis (PubMed:34566931). With
CC chaperone CNE1, coordinately maintains ER homeostasis and contributes
CC to maintenance of cell wall architecture (PubMed:34566931).
CC {ECO:0000269|PubMed:34566931}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:34566931}.
CC -!- INDUCTION: Protein amounts are increased by ER stress elicited by
CC tunicamycin. {ECO:0000269|PubMed:34566931}.
CC -!- DOMAIN: The TPR repeats mediate interaction with unfolded polypeptides
CC and the J-domain is essential to stimulate the ATPase activity of the
CC chaperone and to increase its substrate affinity during the folding
CC cycle. {ECO:0000250|UniProtKB:A0A0D1E2P6}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to endoplasmic
CC reticulum (ER) stress caused by the N-glycosylation inhibitor
CC tunicamycin (PubMed:34566931). Markedly impairs the elaboration of
CC virulence factors such as the polysaccharide capsule and extracellular
CC urease activity, when induced at 37 degrees Celsius corresponsing to
CC the human body temperature (PubMed:34566931). Impairs also induction of
CC the cytokines IL-6, IL-10, and MCP-1 in the lungs of mice and
CC attenuates virulence in an intranasal murine model of cryptococcosis
CC (PubMed:34566931). Leads to abnormal cell morphology of enlarged cells
CC with collapsed cell walls and increased chitin within the cell walls,
CC as well as strong growth defects at both 30 and 37 degrees Celsius when
CC both DNJ1 and CNE1 are deleted (PubMed:34566931).
CC {ECO:0000269|PubMed:34566931}.
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DR EMBL; CP003824; AFR94798.1; -; Genomic_DNA.
DR RefSeq; XP_012049486.1; XM_012194096.1.
DR EnsemblFungi; AFR94798; AFR94798; CNAG_01347.
DR GeneID; 23885071; -.
DR VEuPathDB; FungiDB:CNAG_01347; -.
DR HOGENOM; CLU_015935_0_1_1; -.
DR Proteomes; UP000010091; Chromosome 5.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50005; TPR; 2.
PE 2: Evidence at transcript level;
KW Chaperone; Endoplasmic reticulum; Repeat; Signal; TPR repeat; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..522
FT /note="Tetratricopeptide repeat and J domain-containing co-
FT chaperone DNJ1"
FT /id="PRO_5003827926"
FT REPEAT 29..62
FT /note="TPR 1"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 63..96
FT /note="TPR 2"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 97..130
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 142..175
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 210..243
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 256..289
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 356..389
FT /note="TPR 7"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT DOMAIN 410..471
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 465..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 58281 MW; 2BE3A3D83EA5D4B0 CRC64;
MKGFLLVALP VLFLSLSTQV FGEPSIPSAA QIVQNANRLL AEGSYSAAAR AYGEAIELDP
TGYANYYKRA TAYLSMGRHN AALDDFEQIL RINPGFVQAH YQRAKILAKE GDFAKAQYEL
KAYVRTKSDS EAEELSHLLT VGEAAEKSAL QAFEKGKWQV CVEHSTKALE VGPNSEKLRR
LRVNCATELG DINMVYGDLS RLASLDPSTT YLPLQLSNIA YFIRASSQAA AHIKQCLHFD
PDSKPCKAVH KTIRSLEKDA ARVRNFIESG TYRQAIKILD GDDGLLVRFE KALDDATKPK
DGLPPYLAPQ FHPKKNSQMR LDLYALACKA SVMANDFGEK GAHWCEETMS MNEENVDSWI
SRGERLLRVE KWEEAMRAVE KAFELSGRSQ DILPRVQKAQ RLLKQSKQKD YYKVLGVPRD
ADERAIKKAF RKAAKLAHPD VGGSEEKMAA LNEAYEVLSN TELRQRYDNG DDPNDPTGGQ
QHNPFAHHGG GMPFQFFQQG GGFQGFHQGF PGGGQKMHFQ WN