ID   C9JY08_HUMAN            Unreviewed;       635 AA.
AC   C9JY08;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
DE   Flags: Fragment;
GN   Name=PPEF1 {ECO:0000313|Ensembl:ENSP00000419948.2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000419948.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000419948.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [2] {ECO:0000313|Ensembl:ENSP00000419948.2}
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         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|RuleBase:RU004273}.
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DR   EMBL; KF459018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF459020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF495797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z94056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; C9JY08; -.
DR   SMR; C9JY08; -.
DR   MassIVE; C9JY08; -.
DR   PeptideAtlas; C9JY08; -.
DR   ProteomicsDB; 12191; -.
DR   Antibodypedia; 24151; 192 antibodies from 23 providers.
DR   Ensembl; ENST00000472826.6; ENSP00000419948.2; ENSG00000086717.19.
DR   UCSC; uc064yfp.1; human.
DR   HGNC; HGNC:9243; PPEF1.
DR   VEuPathDB; HostDB:ENSG00000086717; -.
DR   GeneTree; ENSGT00940000159830; -.
DR   HOGENOM; CLU_2402494_0_0_1; -.
DR   ChiTaRS; PPEF1; human.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000086717; Expressed in sperm and 120 other cell types or tissues.
DR   ExpressionAtlas; C9JY08; baseline and differential.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro.
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; 3.
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   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:C9JY08,
KW   ECO:0007829|ProteomicsDB:C9JY08};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          566..601
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          606..635
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   NON_TER         635
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000419948.2"
SQ   SEQUENCE   635 AA;  73661 MW;  D40089C0EB5C1052 CRC64;
     MGCSSSSTKT RRSDTSLRAA LIIQNWYRGY KARLKARQHY ALTIFQSIEY ADEQGQMQLS
     TFFSFMLENY THIHKEELEL RNQSLESEQD MRDRWDYVDS IDVPDSYNGP RLQFPLTCTD
     IDLLLEAFKE QQILHAHYVL EVLFETKKVL KQMPNFTHIQ TSPSKEVTIC GDLHGKLDDL
     FLIFYKNGLP SERNPYVFNG DFVDRGKNSI EILMILCVSF LVYPNDLHLN RGNHEDFMMN
     LRYGFTKEIL HKYKLHGKRI LQILEEFYAW LPIGTIVDNE ILVIHGGISE TTDLNLLHRV
     ERNKMKSVLI PPTETNRDHD TDSKHNKVGV TFNAHGRIKT NGSPTEHLTE HEWEQIIDIL
     WSDPRGKNGC FPNTCRGGGC YFGPDVTSKI LNKYQLKMLI RSHECKPEGY EICHDGKVVT
     IFSASNYYEE GSNRGAYIKL CSGTTPRFFQ YQVTKATCFQ PLRQRVDTME NSAIKILRER
     VISRKSDLTR AFQLQDHRKS GKLSVSQWAF CMENILGLNL PWRSLSSNLV NIDQNGNVEY
     MSSFQNIRIE KPVQEAHSTL VETLYRYRSD LEIIFNAIDT DHSGLISVEE FRAMWKLFSS
     HYNVHIDDSQ VNKLANIMDL NKDGSIDFNE FLKAF
//