SLN1_CANAL
ID SLN1_CANAL Reviewed; 1373 AA.
AC Q5A872; A0A1D8PRV5;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Histidine protein kinase SLN1;
DE EC=2.7.13.3;
GN Name=SLN1; OrderedLocusNames=CAALFM_CR01000CA;
GN ORFNames=CaO19.10766, CaO19.3256;
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.
RX PubMed=9493379; DOI=10.1099/00221287-144-2-425;
RA Nagahashi S., Mio T., Ono N., Yamada-Okabe T., Arisawa M., Bussey H.,
RA Yamada-Okabe H.;
RT "Isolation of CaSLN1 and CaNIK1, the genes for osmosensing histidine kinase
RT homologues, from the pathogenic fungus Candida albicans.";
RL Microbiology 144:425-432(1998).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND AUTOPHOSPHORYLATION.
RX PubMed=10572127; DOI=10.1128/jb.181.23.7243-7247.1999;
RA Yamada-Okabe T., Mio T., Ono N., Kashima Y., Matsui M., Arisawa M.,
RA Yamada-Okabe H.;
RT "Roles of three histidine kinase genes in hyphal development and virulence
RT of the pathogenic fungus Candida albicans.";
RL J. Bacteriol. 181:7243-7247(1999).
RN [6]
RP FUNCTION.
RX PubMed=11368790; DOI=10.1042/0264-6021:3560595;
RA Huh W.-K., Kang S.-O.;
RT "Characterization of the gene family encoding alternative oxidase from
RT Candida albicans.";
RL Biochem. J. 356:595-604(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14734021; DOI=10.1016/s1567-1356(03)00201-0;
RA Kruppa M., Jabra-Rizk M.A., Meiller T.F., Calderone R.;
RT "The histidine kinases of Candida albicans: regulation of cell wall mannan
RT biosynthesis.";
RL FEMS Yeast Res. 4:409-416(2004).
RN [8]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=17038117; DOI=10.1111/j.1365-2958.2006.05438.x;
RA Menon V., Li D., Chauhan N., Rajnarayanan R., Dubrovska A., West A.H.,
RA Calderone R.;
RT "Functional studies of the Ssk1p response regulator protein of Candida
RT albicans as determined by phenotypic analysis of receiver domain point
RT mutants.";
RL Mol. Microbiol. 62:997-1013(2006).
CC -!- FUNCTION: Histidine kinase involved in a two-component signaling
CC pathway that regulates cell wall mannan biosynthesis. Part of the
CC bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which
CC controls activity of the HOG1 pathway and gene expression in response
CC to oxidative stress and probably also to changes in the osmolarity of
CC the extracellular environment. Plays a role in the regulation of
CC alternative oxidase (AOX) gene family expression. Required for hyphal
CC formation and virulence. {ECO:0000269|PubMed:10572127,
CC ECO:0000269|PubMed:11368790, ECO:0000269|PubMed:14734021,
CC ECO:0000269|PubMed:17038117, ECO:0000269|PubMed:9493379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC phosphate group from His-515 (H1) in the histidine kinase domain
CC (transmitter domain) to Asp-1300 (D1) of the response regulatory domain
CC (receiver domain). This transfer probably occurs between two SLN1
CC molecules, rather than intramolecularly (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impairs the hyphal formation and attenuates the
CC virulence in a mouse systemic candidiasis model.
CC {ECO:0000269|PubMed:10572127, ECO:0000269|PubMed:14734021}.
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DR EMBL; CP017630; AOW30862.1; -; Genomic_DNA.
DR RefSeq; XP_717946.1; XM_712853.1.
DR AlphaFoldDB; Q5A872; -.
DR SMR; Q5A872; -.
DR STRING; 237561.Q5A872; -.
DR PRIDE; Q5A872; -.
DR GeneID; 3640422; -.
DR KEGG; cal:CAALFM_CR01000CA; -.
DR CGD; CAL0000175114; SLN1.
DR VEuPathDB; FungiDB:CR_01000C_A; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_003731_0_0_1; -.
DR InParanoid; Q5A872; -.
DR OMA; MRIPIRE; -.
DR OrthoDB; 27870at2759; -.
DR PRO; PR:Q5A872; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:CGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0097308; P:cellular response to farnesol; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IGI:CGD.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell wall biogenesis/degradation; Coiled coil;
KW Glycoprotein; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..1373
FT /note="Histidine protein kinase SLN1"
FT /id="PRO_0000425800"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..1373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 512..1044
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1245..1366
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 387..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 456..493
FT /evidence="ECO:0000255"
FT COMPBIAS 680..703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 515
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1300
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1373 AA; 150742 MW; 4D14F2474D6640C9 CRC64;
MRRLKIGIRP QLIIIVCFAS LFSLLILGIV TGIYFSANLK NLRLERLLVI SQLKRTQVQQ
AIQYIAYQVM TVSEVDSLTV PLSNYRAGNN SKAVFSEAQN YLQQYVLTTD SFTAARLYDL
DLQVVASSFD NMTLISESAQ DVVYPLQPNR SMPPVLGTPS GLYFTGPIAN NSDNFNSRYF
MGITVPVLSN SSIILSQPSI SGYLTIVAAA ESIRSALNST SEDDYQAMAV QPVYGDPQKG
IDNLSQNAYN GDNEVIGFKL VFPVENSLLE AGTIYNINSS SSMKTALASN SGTATGVKSF
FGKKVAIGFS RISVQDNLNW SIVIVQSNSV FNGPANKLRK ITIGVVIGIG AFMCFVTFPL
AVWFIRPITK LKEATEAITK YKKEKLNSVN SNSPTSGSGS GSGSGSGSRA NSDSSADQSL
SLDTGKRNSI NSSSFSSSYS TGIRLPARIP RSKKIFKDEL TELSEAFNIM TEELDKQYTH
LEDRVKLRTK ELEASKIQAE AANEAKTVFI ANISHELRTP LNGILGMTSI AMEEEDPNVI
HDSLKLIHRS GELLLHILTE LLTYSKNTLN RSKLEKSNFQ ILEIVYQVRS IFNKLAHDQR
VNFKILVKPN IFRKLIIYGD SNRIIQIVMN LVSNSLKFTP VDGSVSVSFK LLGEYDHERS
KKLDYKKVCI LNDSSSSTVA VPPPTPPSDT KPNPKPKSTP TPKPDPTRSH LVDHNNRSAN
TTSPLTPVRK PTNQTKNKSI TNNVTKQNMK IRKKKKTNKN LHNNNNNNKN DNSDFLMNRR
LSGSHKFNNT NDEELSPTAI EKNIDKYLTS SADSDNISVT TLSTVQYETT IFESQFKSKP
LPALPVDAKP QVSGKIDEND VNDEDPSGGS IKDDDSEDTI NEKQGISSSP SSSSSSNEKQ
ENSPRSNDST TVTVTRPRHN MMPSAQDFKS YPTFDKKPEY DSNMSNNEIV KNNRVYRIRN
MYQPKVWVIQ IEVTDTGPGI EPALQEKVFE PFVQGDQTLS RSYGGTGLGL SICRQLATMM
HGTLTLKSTI GKGSTFTLTL PLPQTGEIMV PPEDMAEFCE DEFNPAAKIN RKVAFEDGDI
DTESQQQENP SSEEDTQGDR NVQSSTSSSP PNSSSTDSAL PASDSSDIGG TNKSKTTSHG
NNKNINAKKR IITNSSASST KGTKRHTNND GGGGVNGNHS DDNKDLTLTI DKPSLFTRGS
TGTANSGTTS SHSDKKILYP TPTTTTTTTT TTDHTTVLDD ISHLRVLVAE DNSVNQEVIS
RMLKQEGITN LTMACNGAKA IDFVKESIEN NENFDLIFMD VQMPEVDGLK ATKMIRKNLQ
YNKPIIALTA FADESNVKEC LNSGMSGFIT KPISKTNIKK VLVEFLSNEV VTS
