MOB2_CANAL
ID MOB2_CANAL Reviewed; 313 AA.
AC Q5ABC6; A0A1D8PC95;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=CBK1 kinase activator protein MOB2;
GN Name=MOB2; OrderedLocusNames=CAALFM_C100620WA;
GN ORFNames=CaO19.13465, CaO19.6044;
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, INTERACTION WITH CBK1, AND DISRUPTION PHENOTYPE.
RX PubMed=18843050; DOI=10.1091/mbc.e08-03-0272;
RA Song Y., Cheon S.A., Lee K.E., Lee S.Y., Lee B.K., Oh D.B., Kang H.A.,
RA Kim J.Y.;
RT "Role of the RAM network in cell polarity and hyphal morphogenesis in
RT Candida albicans.";
RL Mol. Biol. Cell 19:5456-5477(2008).
RN [5]
RP SUBCELLULAR LOCATION, FUNCTION, AND PHOSPHORYLATION AT SER-44; SER-51;
RP SER-67 AND SER-97.
RX PubMed=21593210; DOI=10.1091/mbc.e11-03-0205;
RA Gutierrez-Escribano P., Gonzalez-Novo A., Suarez M.B., Li C.R., Wang Y.,
RA de Aldana C.R., Correa-Bordes J.;
RT "CDK-dependent phosphorylation of Mob2 is essential for hyphal development
RT in Candida albicans.";
RL Mol. Biol. Cell 22:2458-2469(2011).
RN [6]
RP FUNCTION.
RX PubMed=22589718; DOI=10.1371/journal.ppat.1002683;
RA Gutierrez-Escribano P., Zeidler U., Suarez M.B., Bachellier-Bassi S.,
RA Clemente-Blanco A., Bonhomme J., Vazquez de Aldana C.R., d'Enfert C.,
RA Correa-Bordes J.;
RT "The NDR/LATS kinase Cbk1 controls the activity of the transcriptional
RT regulator Bcr1 during biofilm formation in Candida albicans.";
RL PLoS Pathog. 8:E1002683-E1002683(2012).
CC -!- FUNCTION: Functions as an activator subunit for the CBK1 protein
CC kinase. Part of the regulation of ACE2 activity and cellular
CC morphogenesis (RAM) signaling network. The RAM network is critically
CC required for hyphal growth as well as normal vegetative growth, and for
CC polarization of lipid rafts and the actin cytoskeleton. It play an
CC essential role in biofilm formation. The RAM network also plays a role
CC in serum- and antifungal azoles-induced activation of ergosterol
CC biosynthesis genes, especially those involved in the late steps of
CC ergosterol biosynthesis. {ECO:0000269|PubMed:18843050,
CC ECO:0000269|PubMed:21593210, ECO:0000269|PubMed:22589718}.
CC -!- SUBUNIT: Interacts with protein kinase CBK1 to form the RAM CBK1-MOB2
CC kinase complex. {ECO:0000269|PubMed:18843050}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=localizes to sites of polarized growth in both yeast and hyphal
CC cells. {ECO:0000269|PubMed:21593210}.
CC -!- PTM: Phosphorylated by CDC28 at Ser-44, Ser-51, Ser-67, and Ser-97.
CC Phosphorylation occurs during bud emergence and is maintained until the
CC G2/M transition. Dephosphorylated at the end of mitosis.
CC Phosphorylation is required for the maintenance of polarisome
CC components in hyphae. {ECO:0000269|PubMed:21593210}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to cell-wall- or
CC membrane-perturbing agents, cell-separation defects, a multinucleate
CC phenotype, and loss of cell polarity. {ECO:0000269|PubMed:18843050}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; CP017623; AOW25760.1; -; Genomic_DNA.
DR RefSeq; XP_719006.1; XM_713913.1.
DR AlphaFoldDB; Q5ABC6; -.
DR SMR; Q5ABC6; -.
DR BioGRID; 1222475; 2.
DR STRING; 237561.Q5ABC6; -.
DR iPTMnet; Q5ABC6; -.
DR PRIDE; Q5ABC6; -.
DR GeneID; 3639381; -.
DR KEGG; cal:CAALFM_C100620WA; -.
DR CGD; CAL0000186024; MOB2.
DR VEuPathDB; FungiDB:C1_00620W_A; -.
DR eggNOG; KOG0440; Eukaryota.
DR HOGENOM; CLU_038321_2_1_1; -.
DR InParanoid; Q5ABC6; -.
DR OMA; LNTACAK; -.
DR OrthoDB; 1127941at2759; -.
DR PRO; PR:Q5ABC6; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005938; C:cell cortex; IDA:CGD.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR GO; GO:0030428; C:cell septum; IDA:CGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030295; F:protein kinase activator activity; IGI:CGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:CGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; 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:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0031579; P:membrane raft organization; IMP: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:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:1900233; P:positive regulation of single-species biofilm formation on inanimate substrate; IMP:CGD.
DR GO; GO:0062200; P:RAM/MOR signaling pathway; IEA:EnsemblFungi.
DR GO; GO:2000100; P:regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:CGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR Gene3D; 1.20.140.30; -; 1.
DR InterPro; IPR005301; MOB_kinase_act_fam.
DR InterPro; IPR036703; MOB_kinase_act_sf.
DR PANTHER; PTHR22599; PTHR22599; 1.
DR Pfam; PF03637; Mob1_phocein; 1.
DR SMART; SM01388; Mob1_phocein; 1.
DR SUPFAM; SSF101152; SSF101152; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..313
FT /note="CBK1 kinase activator protein MOB2"
FT /id="PRO_0000424372"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:21593210"
FT MOD_RES 51
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:21593210"
FT MOD_RES 67
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:21593210"
FT MOD_RES 97
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:21593210"
SQ SEQUENCE 313 AA; 35384 MW; 8554555198B9AAA8 CRC64;
MSFLNTIRGL GRGSKKNKKD LEPSNNAIYS HSNLSGNGLR RTQSPTKFSP SKLSSKGAQG
SAAYTSSPTK RSRTGQSLQH QDSQSSLQYQ QQSGSVSPSK RSSIQTTKST TVNADPPLFL
CEPYVKTALV KGSFKTIVQL PKYVDYCEWL ALNIFELFNH LNRFYGVIQE YATPEAYPTM
NAGPNTNYLW VNSSGQAVNL PACQYIEYVI TWVTNKLNDQ SVFPTKNGGA FPPNFIKDCK
NISRQMFRIF AHIYHNHFDK IIHLSLEAHW NSFFAHFISF VKEFNLIDRT EMEPLLPLIE
NFEQQGKITQ ASK
