PAR4_CAEBR
ID PAR4_CAEBR Reviewed; 649 AA.
AC A8X0C4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Serine/threonine-protein kinase par-4 {ECO:0000250|UniProtKB:Q15831, ECO:0000312|EMBL:CAP26084.2};
DE EC=2.7.11.1;
GN Name=par-4 {ECO:0000312|EMBL:CAP26084.2}; ORFNames=CBG05647;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP26084.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP26084.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Required for cytoplasmic partitioning and asymmetric cell
CC division in early embryogenesis. Phosphorylates and restricts the
CC asymmetry effectors mex-5 and mex-6 to the anterior cytoplasm of the
CC zygote and maintains these phosphorylations until fertilization.
CC Phosphorylates and regulates aak-2 in response to oxidative stress. May
CC also play a role in motility, behavioral response, regulation of
CC lifespan and dauer formation through this pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q9GN62}.
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 Evidence={ECO:0000250|UniProtKB:Q15831};
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; Evidence={ECO:0000250|UniProtKB:Q15831};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q15831};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q15831};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9GN62}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. LKB1 subfamily. {ECO:0000255}.
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DR EMBL; HE601419; CAP26084.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X0C4; -.
DR SMR; A8X0C4; -.
DR STRING; 6238.CBG05647; -.
DR WormBase; CBG05647; CBP15405; WBGene00028053; Cbr-par-4.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_030910_0_0_1; -.
DR InParanoid; A8X0C4; -.
DR OMA; RIMERMR; -.
DR OrthoDB; 856506at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IEA:InterPro.
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:0030010; P:establishment of cell polarity; IEA:InterPro.
DR GO; GO:0042593; P:glucose homeostasis; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR CDD; cd14119; STKc_LKB1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039154; LKB1_c.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Developmental protein; Kinase; Magnesium;
KW Manganese; Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..649
FT /note="Serine/threonine-protein kinase par-4"
FT /id="PRO_0000383652"
FT DOMAIN 197..460
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 203..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 649 AA; 72676 MW; A29428BC59EF095A CRC64;
MEGPSSSSVP TASDAPSKYL LPSDSDDGIA TSSAANVGAR NHVTNTEKME KEKKPSPMVL
NVDPDYDYDE EDGGSCEEDQ RGPPAPISRE IVDGAIARRS RDRQISPGVK MSIGNYDDME
DDDEEAETPE EQKQRFLASM KRIRNQPQEA FDPPEDTEAM REFINRQVND AMMFNRDNHI
DYSPVNKPKE AKIIEGYLWG GIIGTGSYGK VKEVIDIYTI TRRAAKIMKY EKLRKIPNGW
DNIRSEMSIL RRLNHRNIVK LIEVFNLPEK GKVYMIFEYC IGSVQNLIDM EPAHRLSIGE
SHAIFLELCH GLNYLHSKRV SHKDIKPGNL LLSIDMTVKI CDFGVAEQIC LFQSDGRCTK
VNGTPKFQPP ECVYGNHEYF DGYKVDMWSA GVTLYNMVSG KYPFEQQVLL RLYESIGTNP
VEMPTNVELS KDLQDIIKRL LDKDFNTRPN ISDVMQHPWF QTGFPEDQGL GRIMERMRTG
DRPFTMYPSL QAMYDGAGSE VILDEDGNEL VLPPPDLVKR GLKFFLELKI LENLPGTLSL
SSFPGFQTLE KRPGDGPPPS SDSGVVAAPD SASGDPLRRP SSRSMPTSAP PRPPSGAVEV
VEAVAAPEAV VEDPVVEEAP AQQQEAPDRR RRGKRSLFSC IFRSRTDSS
