YPI1_COPC7
ID YPI1_COPC7 Reviewed; 175 AA.
AC A8P353;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Type 1 phosphatases regulator YPI1;
GN Name=YPI1; ORFNames=CC1G_12398;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- FUNCTION: Regulator of type 1 phosphatases which maintains protein
CC phosphatase activity under strict control. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the YPI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU83337.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACS02000004; EAU83337.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001838474.2; XM_001838422.2.
DR AlphaFoldDB; A8P353; -.
DR STRING; 5346.XP_001838474.2; -.
DR PRIDE; A8P353; -.
DR EnsemblFungi; EAU83337; EAU83337; CC1G_12398.
DR GeneID; 6015074; -.
DR KEGG; cci:CC1G_12398; -.
DR eggNOG; KOG4102; Eukaryota.
DR HOGENOM; CLU_098333_0_2_1; -.
DR InParanoid; A8P353; -.
DR OrthoDB; 1599272at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:InterPro.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:InterPro.
DR InterPro; IPR011107; PPI_Ypi1.
DR PANTHER; PTHR20835; PTHR20835; 1.
DR Pfam; PF07491; PPI_Ypi1; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome.
FT CHAIN 1..175
FT /note="Type 1 phosphatases regulator YPI1"
FT /id="PRO_0000333474"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 175 AA; 19173 MW; F3C46D493755944D CRC64;
MSRTATAAGP STSAPNDGSR TITITNVPTN EGGDDIIPEE DGPVGTLRLR AARTRTGPRV
TWDEDVVDNE HAGKKKSKIC CIFRPTRDFG ESSSSDSDSD SSCDHDHDRE EGPSGEGSSS
NRPRQGPMQI HDCCDSDDDK NAYERLPSYQ RKKIKAKRRA GRFSSLYESQ DAHTL