PP2B1_CRYNH
ID PP2B1_CRYNH Reviewed; 639 AA.
AC O42773; J9W089;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit A1;
DE EC=3.1.3.16;
DE AltName: Full=Calcineurin A1;
GN Name=CNA1; ORFNames=CNAG_04796;
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 [GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=9184205; DOI=10.1093/emboj/16.10.2576;
RA Odom A., Muir S., Lim E., Toffaletti D.L., Perfect J.R., Heitman J.;
RT "Calcineurin is required for virulence of Cryptococcus neoformans.";
RL EMBO J. 16:2576-2589(1997).
RN [2]
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).
CC -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase.
CC This subunit may have a role in the calmodulin activation of
CC calcineurin (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Composed of two components (A and B), the A component is the
CC catalytic subunit and the B component confers calcium sensitivity.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000305}.
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DR EMBL; AF042082; AAB97372.1; -; Genomic_DNA.
DR EMBL; CP003829; AFR97420.1; -; Genomic_DNA.
DR RefSeq; XP_012052213.1; XM_012196823.1.
DR PDB; 6TZ8; X-ray; 3.30 A; A/D=34-402.
DR PDBsum; 6TZ8; -.
DR AlphaFoldDB; O42773; -.
DR SMR; O42773; -.
DR PRIDE; O42773; -.
DR EnsemblFungi; AFR97420; AFR97420; CNAG_04796.
DR GeneID; 23888175; -.
DR VEuPathDB; FungiDB:CNAG_04796; -.
DR HOGENOM; CLU_004962_6_1_1; -.
DR PHI-base; PHI:89; -.
DR Proteomes; UP000010091; Chromosome 10.
DR GO; GO:0005955; C:calcineurin complex; IPI:UniProtKB.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IEA:EnsemblFungi.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IEA:EnsemblFungi.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:EnsemblFungi.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IEA:EnsemblFungi.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:1903473; P:positive regulation of mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IEA:EnsemblFungi.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:EnsemblFungi.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041751; MPP_PP2B.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; PTHR45673; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Hydrolase; Iron; Metal-binding;
KW Protein phosphatase; Zinc.
FT CHAIN 1..639
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit A1"
FT /id="PRO_0000058832"
FT REGION 494..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:6TZ8"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:6TZ8"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6TZ8"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:6TZ8"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:6TZ8"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:6TZ8"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:6TZ8"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:6TZ8"
FT HELIX 379..398
FT /evidence="ECO:0007829|PDB:6TZ8"
SQ SEQUENCE 639 AA; 71500 MW; 4B92EBE361C80579 CRC64;
MASPATQTAN AIAAINNRSN LVIPEIDFTQ HQLENGEIVS TTERVIKDVQ APAMYVPTDD
QFWSKVDKTK PDIAFLKNHF YREGRLTEEQ ALYILEKGGE LLRSEPNLLE VDAPITVCGD
IHGQYYDLMK LFEVGGNPAD TRYLFLGDYV DRGYFSIECV LYLWSLKMWY PDTLFLLRGN
HECRHLTDYF TFKLECKHKY SETVYNACME SFCNLPLAAV MNKQFLCIHG GLSPELHTLD
DLRSINRFRE PPTQGLMCDI LWADPLEDFG SEKTNENFLH NHVRGCSYFF TYNAACQFLE
RNNLLSIIRA HEAQDAGYRM YRKTKTTGFP SVMTIFSAPN YLDVYSNKAA VLKYESNVMN
IRQFNCTPHP YWLPNFMDVF TWSLPFVGEK ITDMLIAILN CCTKEELEEE DEEFPLNAPE
PTDAESAAER RQIIKNKILA VGRMSRVFSL LREESERVSE LKSISGSNAL PAGMLASGAE
GIKEAIQGFE DARKSDIENE RLPPDIIDPD EDKPASPSAS PIMPATPEEI PSEIPYDSPI
TGTPRTPISS AIASGSPGSP GTPTSPSIGG PPLTAWRPGH GRRTSLGTTK TSPSTRRRSL
ENTMHLIRDV VGGKDAQGDG QLERLAEVIS SPTKGGQGE
