GIN4_CANAL
ID GIN4_CANAL Reviewed; 1349 AA.
AC Q59W62; A0A1D8PF85;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Serine/threonine-protein kinase GIN4;
DE EC=2.7.11.1;
DE AltName: Full=Growth inhibitory protein 4;
GN Name=GIN4; OrderedLocusNames=CAALFM_C111400CA;
GN ORFNames=CaO19.663, CaO19.8280;
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, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14769857; DOI=10.1083/jcb.200307176;
RA Wightman R., Bates S., Amornrrattanapan P., Sudbery P.;
RT "In Candida albicans, the Nim1 kinases Gin4 and Hsl1 negatively regulate
RT pseudohypha formation and Gin4 also controls septin organization.";
RL J. Cell Biol. 164:581-591(2004).
RN [5]
RP FUNCTION IN CDC11 PHOSPHORYLATION, AND ASSOCIATION WITH THE SEPTIN COMPLEX.
RX PubMed=17765684; DOI=10.1016/j.devcel.2007.06.011;
RA Sinha I., Wang Y.M., Philp R., Li C.R., Yap W.H., Wang Y.;
RT "Cyclin-dependent kinases control septin phosphorylation in Candida
RT albicans hyphal development.";
RL Dev. Cell 13:421-432(2007).
RN [6]
RP FUNCTION.
RX PubMed=17504812; DOI=10.1242/jcs.002931;
RA Li C.R., Lee R.T., Wang Y.M., Zheng X.D., Wang Y.;
RT "Candida albicans hyphal morphogenesis occurs in Sec3p-independent and
RT Sec3p-dependent phases separated by septin ring formation.";
RL J. Cell Sci. 120:1898-1907(2007).
RN [7]
RP PHOSPHORYLATION AT SER-10; SER-11; SER-12; SER-15; THR-69; THR-191;
RP SER-294; SER-300; SER-303; SER-388; SER-390; SER-393; THR-397; SER-407;
RP SER-409; THR-412; SER-413; SER-455; SER-469; SER-473; SER-477; SER-485;
RP SER-556; SER-634; SER-720; SER-746; THR-778; THR-869; THR-876; SER-891;
RP THR-941; SER-973; THR-990; THR-992; SER-999; THR-1056; SER-1059; SER-1074;
RP SER-1077; SER-1078; SER-1080; SER-1094; THR-1095; SER-1097; SER-1098;
RP THR-1106; SER-1154 AND SER-1218, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, AND INTERACTION WITH SEP7.
RX PubMed=22366454; DOI=10.1242/jcs.104497;
RA Li C.R., Yong J.Y., Wang Y.M., Wang Y.;
RT "CDK regulates septin organization through cell-cycle-dependent
RT phosphorylation of the Nim1-related kinase Gin4.";
RL J. Cell Sci. 125:2533-2543(2012).
CC -!- FUNCTION: Serine/threonine-protein kinase which regulates the
CC localization and the function of the septins during mitosis. Involved
CC in the formation of the septin ring but not the basal septin band.
CC Phosphorylates septins CDC11 and SEP7. Required for the transition from
CC pseudohyphae to hyphae. Acts upstream of IRS4 and INP51 in regulating
CC cell wall integrity responses. Involved in propolis-induced cell death.
CC {ECO:0000269|PubMed:14769857, ECO:0000269|PubMed:17504812,
CC ECO:0000269|PubMed:17765684, ECO:0000269|PubMed:22366454}.
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 -!- SUBUNIT: Associates with the septin complex which consists of CDC3,
CC CDC10, CDC11, CDC12, and SEP7.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14769857}. Bud neck
CC {ECO:0000269|PubMed:14769857}.
CC -!- PTM: Hyperphosphorylated during mitosis at dozens of sites. Among
CC these, 7 have perfect or minimal CDK consensus sites and are CDC28
CC targets.
CC -!- DISRUPTION PHENOTYPE: Leads to hyperinvasive cells.
CC {ECO:0000269|PubMed:14769857}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR EMBL; CP017623; AOW26765.1; -; Genomic_DNA.
DR RefSeq; XP_713796.1; XM_708703.2.
DR AlphaFoldDB; Q59W62; -.
DR SMR; Q59W62; -.
DR BioGRID; 1227618; 15.
DR STRING; 237561.Q59W62; -.
DR iPTMnet; Q59W62; -.
DR PRIDE; Q59W62; -.
DR GeneID; 3644543; -.
DR KEGG; cal:CAALFM_C111400CA; -.
DR CGD; CAL0000191817; GIN4.
DR VEuPathDB; FungiDB:C1_11400C_A; -.
DR eggNOG; KOG0588; Eukaryota.
DR HOGENOM; CLU_005306_0_0_1; -.
DR InParanoid; Q59W62; -.
DR OMA; IFRKLSW; -.
DR OrthoDB; 1127668at2759; -.
DR PRO; PR:Q59W62; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:CGD.
DR GO; GO:0005730; C:nucleolus; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IDA:CGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IDA:CGD.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0001558; P:regulation of cell growth; IMP:CGD.
DR GO; GO:0000921; P:septin ring assembly; IMP:CGD.
DR Gene3D; 3.30.310.220; -; 1.
DR InterPro; IPR031850; Fungal_KA1_dom.
DR InterPro; IPR043024; KA1_sf_fungal.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF16797; Fungal_KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Coiled coil; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1349
FT /note="Serine/threonine-protein kinase GIN4"
FT /id="PRO_0000424368"
FT DOMAIN 28..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 661..701
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 778
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 869
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 876
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 941
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 990
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 992
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1056
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1095
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22366454"
SQ SEQUENCE 1349 AA; 152951 MW; 6E4D7B7D9F961644 CRC64;
MPHSRQPSIS SSIMSQSNHN HPQKIGPWKL GKTLGRGATG RVLLATHQTT GQKAAVKVVS
KSELQDEETE KNGDGLPYGI EREIIIMKLL THPNVLRLYD VWETSKALYL VLEYVEGGEL
FDLLVERGPL PEVEAIKYFR QIILGTAYCH ALGICHRDLK PENLLLDSQL NVKLADFGMA
ALESNGKLLE TSCGSPHYAA PEIVSGLKYH GAASDVWSCG VILFALLTGR LPFDDENIRN
LLLKVQAGNF EMPVDEVSRE ARDLIARMLE VDPMRRISTE KILRHPLLTK YPMSNEDLIS
EKSLPHPQTG YKSLGSVRNI DKQILSNLTI LWNDRPEEEI VDCLLKDGSN PEKTFYALLM
RYKHNQEDNT NNNSPKKSTS FNNKVVRSGS KYSLNGTPRR KRASHISVSR PTSFQYKSNP
GAGATANRNS VARHSVASSA NNSPRKSPYK SPYRSPYRSP YKSPSKRYSY NQSPTKSPYG
RRSNSQRQFE NEPLKAKPRN IYNEIVDAQS NFSLPPSLPP SLPSKDSRYM IDEPNQPQLQ
QPALSQVPEN PIVDESPDLM QSAKISSGKR NSIIGKNNNN SNSNKRMSKR KSIRASMTTG
LKRNSITMKL LSTYAKLSGD DDWEYMDKQT KRTSATFAAL CDKIFNQEDY DEEDEQLVDP
EEKEAKEYER LMELERKKHE AELKARRELE KKKRRQKRRS ILSSKKLSII VKNDADPNNS
EQELVDEGIK QPKRQSKNLT ALRALSEGNH ASEELTLEDV ENLKRRSASQ PVPKRRQTPV
LTRRPVSRLD PLWQAHENEQ LDRAKDALEQ EWRDSQKRSS TVSRKKVNRE SMISVMDDIV
EEDQGRVNRR STRNTYYERE RDYELPEPTV EDSNLTDDYM TEIRKSRLLN SQLNVRDPLN
EKRKSEPKTL ISNVQIPSVT RKSRNFTTSN KRLSVLSMYS TKESYRDLNS IINSPDENPE
QHQNMNKPAL RTSIADRLDK AGLAEPEYET ETDGEDKVSV IDLDDHLADR RTSYYDGSGK
RASRASTTKR YNVHSSSGQR PKSKVPDLPK NDYDDTFVSN SDEVHKRQYK SMVSDESSAS
DDVFDKIKLP DGKSTKSSID ELANGTSTSG HRKPKIRHSQ PGPEMLIPHL NGGIESSQPM
SKVRGNNSSG HDDSVPPPPP AHKVNKKPLD DKTNFPPPEV DPKRKGSFFR KLSWGSKKTI
ENNTNAATNT TTQQQLPSPA ESKEEKPKSS FFRWFSSSNT PSAAEIRKFN TILPKHEMST
ALFALLNSWS NFGLKDLRND QVGYYITGAI SKHNSFNLKS CKFRIKINQR DFNQKSEIVC
VRVKGSKVTT DTLFSEIEKV LLKEGVLDK
