CML1_CRYNH
ID CML1_CRYNH Reviewed; 174 AA.
AC J9W034;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Calmodulin-like protein 1 {ECO:0000303|PubMed:24520056};
GN Name=CML1 {ECO:0000303|PubMed:24520056};
GN ORFNames=CNAG_05655 {ECO:0000312|EMBL:AFR99086.1};
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 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|Proteomes:UP000010091}
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] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24520056; DOI=10.1128/mbio.00765-13;
RA Butts A., Koselny K., Chabrier-Rosello Y., Semighini C.P., Brown J.C.,
RA Wang X., Annadurai S., DiDone L., Tabroff J., Childers W.E. Jr.,
RA Abou-Gharbia M., Wellington M., Cardenas M.E., Madhani H.D., Heitman J.,
RA Krysan D.J.;
RT "Estrogen receptor antagonists are anti-cryptococcal agents that directly
RT bind EF hand proteins and synergize with fluconazole in vivo.";
RL MBio 5:e00765-e00765(2014).
CC -!- FUNCTION: Calmodulin-like protein which plays a role in the activation
CC of calcineurin (CNA1). {ECO:0000269|PubMed:24520056}.
CC -!- DISRUPTION PHENOTYPE: Resistance to the estrogen receptor-modulating
CC drug toremifene. {ECO:0000269|PubMed:24520056}.
CC -!- MISCELLANEOUS: The breast cancer drug toremifene modulates the ability
CC of CML1 to activate calcineurin (CNA1). {ECO:0000269|PubMed:24520056}.
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DR EMBL; CP003833; AFR99086.1; -; Genomic_DNA.
DR RefSeq; XP_012053911.1; XM_012198521.1.
DR AlphaFoldDB; J9W034; -.
DR SMR; J9W034; -.
DR EnsemblFungi; AFR99086; AFR99086; CNAG_05655.
DR GeneID; 23888953; -.
DR VEuPathDB; FungiDB:CNAG_05655; -.
DR HOGENOM; CLU_061288_18_1_1; -.
DR Proteomes; UP000010091; Chromosome 14.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 4: Predicted;
KW Calcium; Metal-binding; Repeat.
FT CHAIN 1..174
FT /note="Calmodulin-like protein 1"
FT /id="PRO_0000451158"
FT DOMAIN 33..68
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 105..140
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 141..174
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 174 AA; 19926 MW; 041E250D71B0C667 CRC64;
MSHYTKPKSR RPATLPSSHS HATTSNSRSL TEDQRGEIKE AFELFDVDKD GAIDYHELKV
AMRALGFDVK KGEVMKLLKE HGGEDGLMDF LAFERIMTEK ILARNPEHEL RRAFELFDDD
RTGKISLKNL RRVARELGET LGEEELQAMI DEFDLDQDGE INLEEFLAIM LDGE
