(data stored in ACNUC27125 zone)

SWISSPROT: Q8HZM9_RABIT

ID   Q8HZM9_RABIT            Unreviewed;       524 AA.
AC   Q8HZM9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|EMBL:AAN23153.1};
RN   [1] {ECO:0000313|EMBL:AAN23153.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12419772;
RA   Sun L., Moonga B.S., Lu M., Zaidi N., Iqbal J., Blair H.C., Epstein S.,
RA   Abe E., Troen B.R., Huang C.L., Zaidi M.;
RT   "Molecular cloning, expression, and function of osteoclastic calcineurin
RT   Aalpha.";
RL   Am. J. Physiol. Renal Physiol. 284:F575-F583(2003).
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|RuleBase:RU004273};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273}.
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DR   EMBL; AF541961; AAN23153.1; -; mRNA.
DR   RefSeq; NP_001076196.1; NM_001082727.1.
DR   GeneID; 100009487; -.
DR   KEGG; ocu:100009487; -.
DR   CTD; 5532; -.
DR   eggNOG; KOG0375; Eukaryota.
DR   eggNOG; COG0639; LUCA.
DR   HOGENOM; HOG000172699; -.
DR   KO; K04348; -.
DR   OrthoDB; 463522at2759; -.
DR   GO; GO:0005955; C:calcineurin complex; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0008144; F:drug binding; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR   GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
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; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q8HZM9.
DR   SWISS-2DPAGE; Q8HZM9.
KW   Hydrolase {ECO:0000256|RuleBase:RU004273}.
FT   DOMAIN          156..161
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  59023 MW;  7361F77A3CD9C31E CRC64;
     MAAPEPARAA PPPPPPPPPP PGADRVVKAV PFPPTHRLTS EEVFDVDGIP RVDVLKNHLV
     KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI HGQFFDLMKL FEVGGSPANT
     RYLFLGDYVD RGYFSIECVL YLWVLKILYP STLFLLRGNH ECRHLTEYFT FKQECKIKYS
     ERVYEACMEA FDSLPLAALL NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL
     WSDPSEDFGN EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
     RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY WLPNFMDVFT
     WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDGSAAA RKEIIRNKIR AIGKMARVFS
     VLREESESVL TLKGLTPTGM LPSGVLAGGR QTLQSATVEA IEAEKAIRGF SPPHRICSFE
     EAKGLDRINE RMPPRKDAVQ QDGFNSLNTA HATENHGTGN HNAQ
//

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