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Database: UniProt
Entry: A0A1S3GHW1_DIPOR
LinkDB: A0A1S3GHW1_DIPOR
Original site: A0A1S3GHW1_DIPOR 
ID   A0A1S3GHW1_DIPOR        Unreviewed;       655 AA.
AC   A0A1S3GHW1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Serine/threonine-protein phosphatase with EF-hands {ECO:0000256|PIRNR:PIRNR000912};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000912};
GN   Name=Ppef1 {ECO:0000313|RefSeq:XP_012887597.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012887597.1};
RN   [1] {ECO:0000313|RefSeq:XP_012887597.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012887597.1};
RG   RefSeq;
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         ECO:0000256|PIRNR:PIRNR000912, ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00008294, ECO:0000256|PIRNR:PIRNR000912,
CC       ECO:0000256|RuleBase:RU004273}.
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DR   RefSeq; XP_012887597.1; XM_013032143.1.
DR   AlphaFoldDB; A0A1S3GHW1; -.
DR   GeneID; 105997653; -.
DR   KEGG; dord:105997653; -.
DR   CTD; 5475; -.
DR   InParanoid; A0A1S3GHW1; -.
DR   OrthoDB; 3076469at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:UniProtKB-UniRule.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd07420; MPP_RdgC; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR012008; Ser/Thr-Pase_EF-hand_contain.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE WITH EF-HANDS 1; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   PIRSF; PIRSF000912; PPEF; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000912};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000912};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          566..601
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          606..641
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   655 AA;  76018 MW;  A5C66DFBD1D65D23 CRC64;
     MGCGTSSLRN KQPEKVVKAA LVIQNWYRGY RARLMARQHY ALAIFQSIEY ADEQSQMQLS
     NFFSFMLEHY KHARKEDLVL VNRLRETNLQ DLKDRQSYVE LVEVPKSYDG PRLQFPLTFT
     DIDVLLEAFR QQQVLHAHYV LEVLFETKKI LRKMPNFTHV TTSPSKEITI CGDLHGSLED
     LLLIFYKNGL PSENNSYIFN GDFVDRGRNS IETLMVLFVS FLVYPSDLHL NRGNHEDFMM
     NLRYGFTQEV LYKYKLHGKQ ILKVLEEVYT WLPIGTIIDD EILIIHGGIS ESTDLNLLHR
     LERNKMKTVL MPPMSVNRDQ AVDLKKDKAG KIMASGKATS SNSLSEQLSK HEWEQIIDLL
     WSDPRGKDGC YPNTSRGGGC YFGPDVTAKF LNKYHLKTII RSHECKPDGY DICHDGKVIT
     VFSASDYYEE GSNRGAYIRL AHDMAPRFFQ YRATSASCLS PLYQRVEVME YSAIRILKER
     IIARKTDLIR AFQLRDHSRS GKISVAQWAF SMENILELNL PWRTLSPHLV NIDSDGNVDY
     MSIFQDVHIV KSLETVKSAV IETLYRYRSD LKIIFNIIDS DHSGMISIEE FRAMWKLFSS
     HYNVCIDNTQ LDELAHTMDL NRDGSIDFNE FLKTFYIVHK YDKLKTPHNK FAKFK
//
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