ID PP2B_NEUCR Reviewed; 558 AA.
AC Q05681; Q1K7G7; Q9HEE2; V5INZ9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit;
DE EC=3.1.3.16;
DE AltName: Full=Calmodulin-dependent calcineurin A subunit;
GN Name=cna-1; ORFNames=99H12.070, NCU03804;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1655737; DOI=10.1016/s0021-9258(18)55242-x;
RA Higuchi S., Tamura J., Rathna Giri P., Polli J.W., Kincaid R.L.;
RT "Calmodulin-dependent protein phosphatase from Neurospora crassa. Molecular
RT cloning and expression of recombinant catalytic subunit.";
RL J. Biol. Chem. 266:18104-18112(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase.
CC This subunit may have a role in the calmodulin activation of
CC calcineurin.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC18243.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M73032; AAA33565.1; ALT_INIT; mRNA.
DR EMBL; AL451018; CAC18243.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002240; ESA42471.1; -; Genomic_DNA.
DR PIR; A40942; A40942.
DR RefSeq; XP_011394597.1; XM_011396295.1.
DR AlphaFoldDB; Q05681; -.
DR SMR; Q05681; -.
DR STRING; 367110.Q05681; -.
DR PaxDb; 5141-EFNCRP00000003478; -.
DR EnsemblFungi; ESA42471; ESA42471; NCU03804.
DR GeneID; 3877353; -.
DR KEGG; ncr:NCU03804; -.
DR VEuPathDB; FungiDB:NCU03804; -.
DR HOGENOM; CLU_004962_6_0_1; -.
DR InParanoid; Q05681; -.
DR OrthoDB; 1488111at2759; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
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; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; Hydrolase; Iron; Metal-binding; Protein phosphatase;
KW Reference proteome; Zinc.
FT CHAIN 1..558
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit"
FT /id="PRO_0000058833"
FT REGION 415..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 63914 MW; FDE74D72A000A55E CRC64;
MESNNGTGAP GAFHTQQVDN AIRAIQHKRP LPEIDFTIHT MEDGSQVSTM ERVCKDVQAP
AMFKPSDEQF FEDETHTKPD IQFLKQHFYR EGRLTEEQAL WIIREGTKLL RAEPNLLEMD
APITVCGDVH GQYYDLMKLF EVGGDPAETR YLFLGDYVDR GYFSIECVLY LWALKIHYPK
TLWLLRGNHE CRHLTDYFTF KLECKHKYSE AIYEACMESF CCLPLAAVMN KQFLCIHGGL
SPELHTLDDI RNIDRFREPP TQGLMCDILW ADPLEDFGQE KTTDFFVHNH VRGCSYFFSY
SAACHFLEKN NLLSIIRAHE AQDAGYRMYR KTRTTGFPSV MTIFSAPNYL DVYNNKAAVL
KYENNVMNIR QFNCTPHPYW LPNFMDVFTW SLPFVGEKIT DMLIAILSTC SEEELREDSA
TTSPGSASPA LPSAANQDPD SIEFKRRAIK NKILAIGRLS RVFQVLREES ERVTELKTVS
GGRLPAGTLM LGAEGIKNAI SSFEDARKVD LQNERLPPSH DEVVKMQDEE RAQALERATR
EADNDKKLQT LSRRLSTS
//
