PRK1_CANAL
ID PRK1_CANAL Reviewed; 690 AA.
AC Q5A961; A0A1D8PS40;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Actin-regulating kinase PRK1;
DE EC=2.7.11.1;
GN Name=PRK1; Synonyms=ARK1; OrderedLocusNames=CAALFM_CR02040WA;
GN ORFNames=CaO19.10136, CaO19.2605;
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 FUNCTION, AND 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).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF SLA1.
RX PubMed=22787279; DOI=10.1091/mbc.e12-03-0231;
RA Zeng G., Wang Y.M., Wang Y.;
RT "Cdc28-Cln3 phosphorylation of Sla1 regulates actin patch dynamics in
RT different modes of fungal growth.";
RL Mol. Biol. Cell 23:3485-3497(2012).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23982070; DOI=10.1128/mbio.00476-13;
RA Epp E., Nazarova E., Regan H., Douglas L.M., Konopka J.B., Vogel J.,
RA Whiteway M.;
RT "Clathrin- and Arp2/3-independent endocytosis in the fungal pthogen Candida
RT albicans.";
RL MBio 4:E00476-E00476(2013).
CC -!- FUNCTION: Protein kinase involved in regulation of actin cytoskeleton
CC organization and endocytosis. Phosphorylates the endocytic protein
CC SLA1. The CDC28-CLN3 complex phosphorylation of SLA1 enhances its
CC further phosphorylation by PRK1, weakening SLA1 association with PAN1,
CC an activator of the actin-nucleating ARP2/3 complex. Plays a role in
CC cell wall regulation and required for oxidative stress survival.
CC {ECO:0000269|PubMed:20140194, ECO:0000269|PubMed:22787279,
CC ECO:0000269|PubMed:23982070}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:23982070}. Note=Localized to sites of endocytosis.
CC -!- DISRUPTION PHENOTYPE: Leads to increased caspofungin sensitivity.
CC {ECO:0000269|PubMed:20140194}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CP017630; AOW30955.1; -; Genomic_DNA.
DR RefSeq; XP_718270.2; XM_713177.2.
DR AlphaFoldDB; Q5A961; -.
DR SMR; Q5A961; -.
DR STRING; 237561.Q5A961; -.
DR PRIDE; Q5A961; -.
DR GeneID; 3640153; -.
DR KEGG; cal:CAALFM_CR02040WA; -.
DR CGD; CAL0000183416; PRK1.
DR VEuPathDB; FungiDB:CR_02040W_A; -.
DR eggNOG; KOG1989; Eukaryota.
DR HOGENOM; CLU_011638_4_0_1; -.
DR InParanoid; Q5A961; -.
DR OrthoDB; 857825at2759; -.
DR PRO; PR:Q5A961; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000147; P:actin cortical patch assembly; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..690
FT /note="Actin-regulating kinase PRK1"
FT /id="PRO_0000424378"
FT DOMAIN 22..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 478..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 690 AA; 77639 MW; DB391E40775ECB13 CRC64;
MPQPPPNAYK AGTRLTVGSH KVSIIKYISE GGFAHVYTCT IDPPFQGSTV ACLKRVVVPS
KWQLSLLRQE VDAMRRLRGN KHIVSYIDSH ASRLGDSNTS GTNHSQQQQY EVFLLMEYCE
NNGLIDFMNT RLVNKLTEKE IIDIMYQVTI GVAMCHHLRP PLIHRDIKIE NVLIDGKGVF
KLCDFGSSVN YLPPPRNPQE LQLMKDDLMQ HTTPQYRAPE MIDLSKGFPI DDKSDIWALG
IFLYKLCYYT TPFERPNQSS LQELEHTILN CSETLRFSDQ PGSIFSPRLK NAIKVCLRAD
PRRRPNAVQL LGEIAAMKGE KTIPNVVPYS VIEQQRTKQA SALEEDTKKG QASFVETKKI
TSKPKTDPFA NIDKSKFLNK SGYKLSSVTA ESRTVPARPL SAFFDDGNTP RIYSQGNRST
PSVQDYVKEE LAKGESYEFN EPDGTLEFLK SREEEKLNQR NDTGGSFKAA FKNGLRKIST
GGNISANNTG SSVKSNRRAS LKRIITGGSN HNRKHSEENT KNVEDSNPVS SAPKKLSIQH
RMQQLLNQND HQRVQKSAQG YGKYTDIKAS EDIDEINKPT LSKHSQKKLS PPAVPVNLSS
QRNKSQQSSS TTKKYPIKDS KPLSKVRNNP PKDSVKTKPP PPKPKKPVYL KSPTKLEIAD
QRRLSDASEI SMPDLDDLEK QFSKRFPSYV
