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PAR1_CAEBR
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   03-AUG-2022, entry version 91.
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.CBG04756; -.
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; DWVIFED; -.
DR   OrthoDB; 1127668at2759; -.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR001772; KA1_dom.
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   InterPro; IPR015940; UBA.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; SSF103243; 1.
DR   SUPFAM; SSF56112; SSF56112; 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
 
 
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