ID G3RAA2_GORGO Unreviewed; 483 AA.
AC G3RAA2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE AltName: Full=CAM-PRP catalytic subunit {ECO:0000256|ARBA:ARBA00031196};
GN Name=PPP3CC {ECO:0000313|Ensembl:ENSGGOP00000012368.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000012368.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000012368.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000012368.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000012368.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001512};
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 Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000256|ARBA:ARBA00009905}.
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DR EMBL; CABD030057332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030057341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3RAA2; -.
DR STRING; 9593.ENSGGOP00000012368; -.
DR Ensembl; ENSGGOT00000012725.3; ENSGGOP00000012368.2; ENSGGOG00000012671.3.
DR eggNOG; KOG0375; Eukaryota.
DR GeneTree; ENSGT00940000154115; -.
DR HOGENOM; CLU_004962_6_0_1; -.
DR InParanoid; G3RAA2; -.
DR OMA; CMNTFDC; -.
DR TreeFam; TF105557; -.
DR Proteomes; UP000001519; Chromosome 8.
DR Bgee; ENSGGOG00000012671; Expressed in testis and 5 other cell types or tissues.
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:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 2.
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:SF2; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT GAMMA ISOFORM; 1.
DR Pfam; PF00149; Metallophos; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 52..305
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|SMART:SM00156"
FT REGION 442..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 54660 MW; 9BB5BB6581E32F03 CRC64;
MSGRRFHLST TDRVIKAVPF PPTQRLTFKE VFENGKPKVD VLKNHLVKEG RLEEEVALKI
INDGAAILRQ EKTMIEVDAP ITVCGDIHGQ FFDLMKLFEV GGSPSNTRYL FLGDYVDRGY
FSIERIKYSE QVYDACMETF DCLPLAALLN QQFLCVHGGM SPEITSLDDI RKLDRFTEPP
AFGPVCDLLW SDPSEDYGNE KTLEHYTHNT VRGCSYFYSY PAVCEFLQNN NLLSIIRAHE
AQDAGYRMYR KSQATGFPSL ITIFSAPNYL DVYNNKAAVL KYENNVMNIR QFNCSPHPYW
LPNFMDVFTW SLPFVGEKVT EMLVNVLNIC SDDELISDDE AEDHYIPSYQ KGSTTVRKEI
IRNKIRAIGK MARVFSILRQ ESESVLTLKG LTPTGTLPLG VLSGGKQTIE TATVEAVEAR
EAIRGFSLQH KIRSFEEARG LDRINERMPP RKDSIHADGP MKSVTSAHSH AAHRSDQGKK
AQS
//
