ID PAR1_CAEBR Reviewed; 1088 AA.
AC A8WYE4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Serine/threonine-protein kinase par-1 {ECO:0000250|UniProtKB:Q9TW45, ECO:0000312|EMBL:CAP25402.1};
DE EC=2.7.11.1;
GN Name=par-1; ORFNames=CBG04756;
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:CAP25402.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP25402.1};
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 effector mex-5 (and possibly also mex-6) to the anterior
CC cytoplasm of the zygote. Regulates mes-1 expression during early
CC embryogenesis. Critical role in postembryonic vulval morphogenesis.
CC {ECO:0000250|UniProtKB:Q9TW45}.
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:Q7KZI7};
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:Q7KZI7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7KZI7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}.
CC Note=Colocalizes with germ granules (P granules).
CC {ECO:0000250|UniProtKB:Q9TW45}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; HE601135; CAP25402.1; -; Genomic_DNA.
DR RefSeq; XP_002637943.1; XM_002637897.1.
DR AlphaFoldDB; A8WYE4; -.
DR SMR; A8WYE4; -.
DR STRING; 6238.A8WYE4; -.
DR GeneID; 8579940; -.
DR KEGG; cbr:CBG_04756; -.
DR CTD; 8579940; -.
DR WormBase; CBG04756a; CBP47106; WBGene00027371; Cbr-par-1.
DR eggNOG; KOG0586; Eukaryota.
DR HOGENOM; CLU_000288_157_2_1; -.
DR InParanoid; A8WYE4; -.
DR OMA; YDEVMAC; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0050321; F:tau-protein kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12196; MARK1-3_C; 1.
DR CDD; cd14072; STKc_MARK; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR049508; MARK1-4_cat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR PANTHER; PTHR24346:SF93; KP78A-RELATED; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Developmental protein; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1088
FT /note="Serine/threonine-protein kinase par-1"
FT /id="PRO_0000383321"
FT DOMAIN 128..379
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 398..440
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1039..1088
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 134..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1088 AA; 116525 MW; 805A332FC0C22850 CRC64;
MSTVSSYFMG ISSKKNGSSA TANKQSTRPQ ESHHHRRQQP TSQQSTEMNG TTTAPSGGTS
SGTTTTSSGV PTASTGGGSA RYSSSSSGRS HPTTGGGSSS HARSSGQSGM SSRSAARRND
QDVHVGKYKL LKTIGKGNFA KVKLAKHVIT GHEVAIKIID KTALNPSSLQ KLFREVKIMK
QLDHPNIVKL YQVMETEQTL YLVLEYASGG EVFDYLVAHG RMKEKEARAK FRQIVSAVQY
LHSKNIIHRD LKAENLLLDQ DMNIKIADFG FSNTFSLGNK LDTFCGSPPY AAPELFSGKK
YDGPEVDVWS LGVILYTLVS GSLPFDGQNL KELRERVLRG KYRIPFYMST DCENLLKKFL
VINPQRRSSL DNIMKDRWMN VGYEDDELKP FIEPPKDQID EQRIEKLIQI FQLGFNKATI
LESVEKEKFE DIHATYLLLG ERKSDPSRYS RSSATATGPS ITSGAALASA ANAQKHQSSA
APASGSSSSR RSSQNDAAAS GAGGTVVMSG TRHGGVQMRA QPTSRQAAIS LLQPPSYKPS
SNTTQIAQIP PLFNRNSTAT SSTNQPSSGI TAGTRKIDPK GRIPLNSAAV QSHRTATGAV
AANTGGIPSQ RDHSQQQQQY MNQLTSSSMM SKLINKTPAA GGANATTSAT SAAAAPLQKS
GSQISHAPTE PVIREDDDES NSEHQNGNVP LIGGVGPQTS PVVAPSEDVT SSEQQKQEKA
SSEAPKETKP SMIHQSPSMP PSQMMTAMES LKLSESGGKS PSNSQQPPQR ATSQQMSRSA
TTNSAANMAS NQQSSGAPQQ SGASSQQCHT KPSSTSSSSS SSTTAPTSSG QPHHQHQLTH
NASFSVTPSA YQMPTTTTIT SGAPTSSSAF PRNTRNRQTF HGKTEKDKGG DDGSDEIGDT
PANVSIGATG ASANNTEGTI WSKLSKLTRR DHNRESMTQP VSSRAGTIGA AQGQQTAAAL
AAIREQSSGP LTPGTPPVAQ AMTQEGDVKP RSLRFTWSMK TTSSLAPDDM MREIRKVLDA
NGCDYEQRER YMILCVHGDP NTDSLVQWEM EVCKLPRLSL NGVRFKRISG TSIGFKNIAS
KIAQELNL
//
