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Database: UniProt
Entry: G1P2P3_MYOLU
LinkDB: G1P2P3_MYOLU
Original site: G1P2P3_MYOLU 
ID   G1P2P3_MYOLU            Unreviewed;       145 AA.
AC   G1P2P3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 14 {ECO:0000256|RuleBase:RU369059};
GN   Name=PPP1R14D {ECO:0000313|Ensembl:ENSMLUP00000004141.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000004141.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000004141.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000004141.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Inhibitor of PPP1CA. {ECO:0000256|RuleBase:RU369059}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369059}.
CC   -!- SIMILARITY: Belongs to the PP1 inhibitor family.
CC       {ECO:0000256|ARBA:ARBA00005483, ECO:0000256|RuleBase:RU369059}.
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DR   EMBL; AAPE02025705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006093093.1; XM_006093031.2.
DR   AlphaFoldDB; G1P2P3; -.
DR   STRING; 59463.ENSMLUP00000004141; -.
DR   Ensembl; ENSMLUT00000004552.2; ENSMLUP00000004141.2; ENSMLUG00000004560.2.
DR   GeneID; 102437810; -.
DR   KEGG; mlf:102437810; -.
DR   CTD; 54866; -.
DR   eggNOG; ENOG502RZZY; Eukaryota.
DR   GeneTree; ENSGT00950000182985; -.
DR   HOGENOM; CLU_114155_0_0_1; -.
DR   InParanoid; G1P2P3; -.
DR   OMA; LDMEQWV; -.
DR   OrthoDB; 4637057at2759; -.
DR   TreeFam; TF105546; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0042325; P:regulation of phosphorylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.150.220; CPI-17; 1.
DR   InterPro; IPR008025; CPI-17.
DR   InterPro; IPR036658; CPI-17_sf.
DR   PANTHER; PTHR16188; PROTEIN PHOSPHATASE 1 INHIBITOR POTENTIATED BY PROTEIN KINASE C; 1.
DR   PANTHER; PTHR16188:SF13; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 14D; 1.
DR   Pfam; PF05361; PP1_inhibitor; 1.
DR   SUPFAM; SSF81790; Myosin phosphatase inhibitor 17kDa protein, CPI-17; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369059};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU369059};
KW   Protein phosphatase inhibitor {ECO:0000256|ARBA:ARBA00023272,
KW   ECO:0000256|RuleBase:RU369059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   145 AA;  16639 MW;  E23F11C3E97BC1FA CRC64;
     MLSSNPASCT SPNPDRENSS KKVQWASGKR RTSSTDSESK SHPDPSKASR SRRPSRLTVK
     YDRGHLQRWL DVEQWVDAKV QELFQDQPTP SEPEVDLEVL MELSTEEQKT HLEALLRDCP
     SPTEPFISEL LSQLKKLRRL SRPQK
//
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