PIK1A_CANAL
ID PIK1A_CANAL Reviewed; 956 AA.
AC Q9UW24; A0A1D8PNA2; Q59YI1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphatidylinositol 4-kinase PIK1a;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
GN Name=PIKA; OrderedLocusNames=CAALFM_C501760CA; ORFNames=CaO19.3199;
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 [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=10455055; DOI=10.1126/science.285.5431.1271;
RA Hull C.M., Johnson A.D.;
RT "Identification of a mating type-like locus in the asexual pathogenic yeast
RT Candida albicans.";
RL Science 285:1271-1275(1999).
RN [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: Acts on phosphatidylinositol (PI) in the first committed step
CC in the production of the second messenger inositol 1,4,5,-
CC trisphosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: The C.albicans mating-type-like (MTL) locus contains, in
CC addition to the genes for the regulatory proteins (MTLA1, MTLA2,
CC MTLALPHA1 and MTLALPHA2), a and alpha idiomorphs of a
CC phosphatidylinositol kinase (PIKA and PIKALPHA), a poly(A) polymerase
CC (PAPA and PAPALPHA) and an oxysterol binding protein-like protein (OBPA
CC and OBPALPHA).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AF167162; AAD51405.1; -; Genomic_DNA.
DR EMBL; CP017627; AOW29607.1; -; Genomic_DNA.
DR RefSeq; XP_714615.1; XM_709522.1.
DR AlphaFoldDB; Q9UW24; -.
DR STRING; 237561.Q9UW24; -.
DR PRIDE; Q9UW24; -.
DR GeneID; 3643765; -.
DR KEGG; cal:CAALFM_C501760CA; -.
DR CGD; CAL0000190377; PIKA.
DR VEuPathDB; FungiDB:C5_01760C_A; -.
DR HOGENOM; CLU_002446_2_0_1; -.
DR InParanoid; Q9UW24; -.
DR OMA; CGLIETI; -.
DR OrthoDB; 1147978at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IGI:CGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IGI:CGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021601; Phosphatidylino_kinase_fungi.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11522; Pik1; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..956
FT /note="Phosphatidylinositol 4-kinase PIK1a"
FT /id="PRO_0000088833"
FT DOMAIN 1..120
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 658..939
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 545..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..670
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 805..813
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 824..848
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 956 AA; 109252 MW; 940777ECF976C68B CRC64;
MPVAPHELRD TIKSRDLGLF QCIDLLKQHN DNIGVHHQLV QKLYSYSYDE LEFFIPQFIQ
LLVNFETDSM ALEDFLLHYC NQFPHFSLIV FWYLQAFLFE LRNEPKSYSF QTVRKFINKL
QNILFNVETS FHIRGPEFRE NMQPALILCG SVASAFSSPL VNEYALPIVR SQGKQQKSFV
FKLASFQKSL TRNLTMKNQR LSADAITPVI SDDDSKVSNR IQESQRLKTK YSKKKISAAL
QLDDSENYTT DEEELGYVQT LSRPKIREMK YTEVEENLKI NTIIRSKKNR SKTTVNSISF
FSDTDQSASM EEYNRSAQSL PELVRTRSRL DLYSSESEAA LGTSRNSAEL IISKKKFMGS
EVKTRPYKEL LKILQVNYSK KETSFIMSLQ NISLRLSSVP KVARLSALRA ELSIINESIL
PSEIDIPQLL PVTSNKNKKF HKILKLNINE ACVLNSAERV PYLLLIEYLS DEIDFNPFSD
QNQKIINDCV RKPEVKPNDQ ISGDDDTSVV SSIQEEMFLD NNASENYNED GDLGEISLLH
SRSSSRDWAK STPGSPVARS SQEDEKFYGN VSSTTGGTIE SSVLADQMRI ASLMLQQLES
SGQSNTQQFV SIRNRIIESM ISLQDQFDFI DYETLKELKT DEQDAGKRKL ENDFKLAEDW
NEKKHRIRKS SIYGHLENWD LCSVIVKNGD DLPQEAFACQ LISLISNIWK KHKVDFWTKR
MKILITSANA GLVETITNAM SIHSIKKSLT ELSIENGENA KGRIFTLKDY FQKLYGSVDS
SKYVKAQENF AISLASYSII CYVLQIKDRH NGNIMLDHEG HIIHIDFGFL LSNSPGSVGF
EAAPFKLTSE YVEVLGGLES KAYLKFVDTC KNCFKALRKE WGQIVSIVEL MQKGSSLPCF
NNGDNTSVLL QQRLQLHLSD EEIDSFIEVY LIEKSVGSMY TRLYDQFQMI TQGIYS
