CPP1_CANAL
ID CPP1_CANAL Reviewed; 597 AA.
AC Q5APU2; A0A1D8PER3; Q5AP98;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Dual specificity protein tyrosine phosphatase CCP1;
DE EC=3.1.3.48;
GN Name=CPP1; OrderedLocusNames=CAALFM_C110000CA;
GN ORFNames=CaO19.12330, CaO19.4866;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-516, AND
RP FUNCTION.
RX PubMed=9398674; DOI=10.1091/mbc.8.12.2539;
RA Csank C., Makris C., Meloche S., Schroppel K., Rollinghoff M., Dignard D.,
RA Thomas D.Y., Whiteway M.;
RT "Derepressed hyphal growth and reduced virulence in a VH1 family-related
RT protein phosphatase mutant of the human pathogen Candida albicans.";
RL Mol. Biol. Cell 8:2539-2551(1997).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9890266; DOI=10.1111/j.1699-0463.1998.tb00257.x;
RA Guhad F.A., Csank C., Jensen H.E., Thomas D.Y., Whiteway M., Hau J.;
RT "Reduced pathogenicity of a Candida albicans MAP kinase phosphatase (CPP1)
RT mutant in the murine mastitis model.";
RL APMIS 106:1049-1055(1998).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9596738; DOI=10.1128/iai.66.6.2713-2721.1998;
RA Csank C., Schroppel K., Leberer E., Harcus D., Mohamed O., Meloche S.,
RA Thomas D.Y., Whiteway M.;
RT "Roles of the Candida albicans mitogen-activated protein kinase homolog,
RT Cek1p, in hyphal development and systemic candidiasis.";
RL Infect. Immun. 66:2713-2721(1998).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11083847; DOI=10.1128/iai.68.12.7159-7161.2000;
RA Schroppel K., Sprosser K., Whiteway M., Thomas D.Y., Rollinghoff M.,
RA Csank C.;
RT "Repression of hyphal proteinase expression by the mitogen-activated
RT protein (MAP) kinase phosphatase Cpp1p of Candida albicans is independent
RT of the MAP kinase Cek1p.";
RL Infect. Immun. 68:7159-7161(2000).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=20140194; DOI=10.1371/journal.ppat.1000752;
RA Blankenship J.R., Fanning S., Hamaker J.J., Mitchell A.P.;
RT "An extensive circuitry for cell wall regulation in Candida albicans.";
RL PLoS Pathog. 6:E1000752-E1000752(2010).
CC -!- FUNCTION: Protein tyrosine phosphatase that acts as a repressor of the
CC yeast-hyphal switch. Plays an important role in virulence. Negatively
CC regulates CST20-HST7-CEK1-CPH1 filamentous growth pathway. Represses
CC hyphal genes such as SAP4, SA5, SAP6, and HYR1, by acting through a
CC CEK1-independent mechanism. {ECO:0000269|PubMed:11083847,
CC ECO:0000269|PubMed:9398674, ECO:0000269|PubMed:9596738,
CC ECO:0000269|PubMed:9890266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:9398674};
CC -!- DISRUPTION PHENOTYPE: Derepresses filamentous growth and decreases
CC virulence and resistance to cell wall and osmotic stress.
CC {ECO:0000269|PubMed:11083847, ECO:0000269|PubMed:20140194,
CC ECO:0000269|PubMed:9398674, ECO:0000269|PubMed:9596738,
CC ECO:0000269|PubMed:9890266}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017623; AOW26631.1; -; Genomic_DNA.
DR RefSeq; XP_723551.2; XM_718458.2.
DR AlphaFoldDB; Q5APU2; -.
DR SMR; Q5APU2; -.
DR STRING; 237561.Q5APU2; -.
DR PRIDE; Q5APU2; -.
DR GeneID; 3634865; -.
DR KEGG; cal:CAALFM_C110000CA; -.
DR CGD; CAL0000191382; CPP1.
DR VEuPathDB; FungiDB:C1_10000C_A; -.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_032220_0_0_1; -.
DR OrthoDB; 1123995at2759; -.
DR PRO; PR:Q5APU2; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IDA:CGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0060258; P:negative regulation of filamentous growth; IMP:CGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:CGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..597
FT /note="Dual specificity protein tyrosine phosphatase CCP1"
FT /id="PRO_0000425803"
FT DOMAIN 428..579
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 55..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 516
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MUTAGEN 516
FT /note="C->S: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:9398674"
SQ SEQUENCE 597 AA; 65560 MW; 05D1A9DF94E57C62 CRC64;
MTTPLSSYST TVTNHHPTFS FESLNSISSN NSTRNNQSNS VNSLLYFNSS GSSMVSSSSD
AAPTSISTTT TSTTSMTGAS ANADNQQVYT ITEEDSINDI NRKEQNSFSI QPNQTPTMLP
TSSYTLQRPP GLHEYTSSIS SISSTSSNST SAPVSPALIN YSPKHSRKPN SLNLNRNMKN
LSLNLHDSTN GYTSPLPKST NSNQPRSNFI MDSPSKKSTP VNRIGNNNGN DYINATLLQT
PSITQTPTMP PPLSLAQGPP SSVGSESVYK FPPISNACLN YSAGDSDSEV ESMSMKQAAK
NTIIPPMAPP FALQSKSSPL STPPRLHSPL GVDRGLPISM SPIQSSLNQK FNNITLQTPL
NSSFSINNDE ATNFNNKNNK NNNNNSTATT TITNTILSTP QNVRYNSKKF HPPEELQEST
SINAYPNGPK NVLNNLIYLY SDPAQGKIDI NKFDLVINVA KECDNMSLQY MNQVPNQREY
VYIPWSHNSN ISKDLFQITN KIDQFFTNGR KILIHCQCGV SRSACVVVAF YMKKFQLGVN
EAYELLKNGD QKYIDACDRI CPNMNLIFEL MEFGDKLNNN EISTQQLLMN SPPTINL
