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Database: UniProt
Entry: Q5ZL39_CHICK
LinkDB: Q5ZL39_CHICK
Original site: Q5ZL39_CHICK 
ID   Q5ZL39_CHICK            Unreviewed;       323 AA.
AC   Q5ZL39;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=PPP1CC {ECO:0000313|Ensembl:ENSGALP00010038670.1};
GN   ORFNames=RCJMB04_7p6 {ECO:0000313|EMBL:CAG31554.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:CAG31554.1};
RN   [1] {ECO:0000313|EMBL:CAG31554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB {ECO:0000313|EMBL:CAG31554.1};
RC   TISSUE=Bursa {ECO:0000313|EMBL:CAG31554.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2] {ECO:0000313|Ensembl:ENSGALP00010038670.1}
RP   IDENTIFICATION.
RC   STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010038670.1};
RG   Ensembl;
RL   Submitted (JUL-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   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}. Cleavage furrow
CC       {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. Midbody
CC       {ECO:0000256|ARBA:ARBA00004214}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}. Nucleus speckle
CC       {ECO:0000256|ARBA:ARBA00004324}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005333}.
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DR   EMBL; AJ719895; CAG31554.1; -; mRNA.
DR   RefSeq; NP_001006190.1; NM_001006190.1.
DR   IntAct; Q5ZL39; 1.
DR   PaxDb; 9031-ENSGALP00000007265; -.
DR   Ensembl; ENSGALT00010062539.1; ENSGALP00010038670.1; ENSGALG00010025621.1.
DR   GeneID; 416872; -.
DR   KEGG; gga:416872; -.
DR   CTD; 5501; -.
DR   VEuPathDB; HostDB:geneid_416872; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   GeneTree; ENSGT00940000153472; -.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   OMA; EEHEIRY; -.
DR   OrthoDB; 19833at2759; -.
DR   TreeFam; TF354243; -.
DR   Proteomes; UP000000539; Chromosome 15.
DR   Bgee; ENSGALG00000004571; Expressed in spermatocyte and 13 other cell types or tissues.
DR   ExpressionAtlas; Q5ZL39; baseline and differential.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF204; SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q5ZL39};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000539}.
FT   DOMAIN          121..126
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          300..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   323 AA;  37000 MW;  5A6C112C16898615 CRC64;
     MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK
     ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
     LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
     QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD
     LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
     KKKPNASRPV TPPRSMITKQ AKK
//
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