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KC1D_XENLA
ID   KC1D_XENLA              Reviewed;         415 AA.
AC   Q5BP74; Q7ZXL6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Casein kinase I isoform delta;
DE            Short=CKI-delta;
DE            Short=CKId;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:15893604};
DE   AltName: Full=Tau-protein kinase CSNK1D;
DE            EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730};
GN   Name=csnk1d;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, PHOSPHORYLATION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND CATALYTIC
RP   ACTIVITY.
RC   TISSUE=Embryo;
RX   PubMed=15893604; DOI=10.1016/j.molbrainres.2005.02.009;
RA   Constance C.M., Fan J.-Y., Preuss F., Green C.B., Price J.L.;
RT   "The circadian clock-containing photoreceptor cells in Xenopus laevis
RT   express several isoforms of casein kinase I.";
RL   Brain Res. Mol. Brain Res. 136:199-211(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: [Isoform 1]: Casein kinases are operationally defined by
CC       their preferential utilization of acidic proteins such as caseins as
CC       substrates. Can phosphorylate a large number of proteins
CC       (PubMed:15893604). Central component of the circadian clock. May act as
CC       a negative regulator of circadian rhythmicity by phosphorylating per1
CC       and per2, which may lead to their degradation. Participates in wnt
CC       signaling (By similarity). {ECO:0000250|UniProtKB:P48730,
CC       ECO:0000269|PubMed:15893604}.
CC   -!- FUNCTION: [Isoform 2]: Has no kinase activity.
CC       {ECO:0000269|PubMed:15893604}.
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:0000269|PubMed:15893604};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC         Evidence={ECO:0000305|PubMed:15893604};
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:0000269|PubMed:15893604};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC         Evidence={ECO:0000305|PubMed:15893604};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P48730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC   -!- ACTIVITY REGULATION: Exhibits substrate-dependent heparin activation.
CC       {ECO:0000250|UniProtKB:P48730}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with per1 and per2.
CC       Component of the circadian core oscillator (By similarity).
CC       {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC       {ECO:0000269|PubMed:15893604}. Nucleus {ECO:0000269|PubMed:15893604}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:15893604}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5BP74-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5BP74-2; Sequence=VSP_035782;
CC   -!- TISSUE SPECIFICITY: Detected in retina photoreceptor cells.
CC       {ECO:0000269|PubMed:15893604}.
CC   -!- INDUCTION: Constitutively expressed in retina.
CC       {ECO:0000269|PubMed:15893604}.
CC   -!- PTM: Autophosphorylated on serine and threonine residues.
CC       {ECO:0000269|PubMed:15893604}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR   EMBL; AY926534; AAX22002.1; -; mRNA.
DR   EMBL; AY926535; AAX22003.1; -; mRNA.
DR   EMBL; BC044700; AAH44700.1; -; mRNA.
DR   RefSeq; NP_001080669.1; NM_001087200.1.
DR   RefSeq; XP_018096015.1; XM_018240526.1. [Q5BP74-2]
DR   AlphaFoldDB; Q5BP74; -.
DR   SMR; Q5BP74; -.
DR   DNASU; 380361; -.
DR   GeneID; 380361; -.
DR   KEGG; xla:380361; -.
DR   CTD; 380361; -.
DR   Xenbase; XB-GENE-5734033; csnk1d.S.
DR   OrthoDB; 1097975at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 380361; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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   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   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Wnt signaling pathway.
FT   CHAIN           1..415
FT                   /note="Casein kinase I isoform delta"
FT                   /id="PRO_0000354089"
FT   DOMAIN          9..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          301..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..342
FT                   /note="Autoinhibitory"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        301..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VAR_SEQ         189..246
FT                   /note="EQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
FT                   CKGYPS -> A (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15893604, ECO:0000303|Ref.2"
FT                   /id="VSP_035782"
FT   CONFLICT        57
FT                   /note="K -> N (in Ref. 1; AAX22003)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   415 AA;  47439 MW;  B8B8765DB29EC9B5 CRC64;
     MELRVGNRYR LGRKIGSGSF GDIYLGTDIA ASEEVAIKLE CVKTKHPQLH IESKIYKMMQ
     GGVGIPTIKW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
     SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
     SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
     CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA
     AEDAERERRE REERLRHTRN PAVRGLPSTA SGRLRGTQEV TPSTPLTPTS HTANTSPRPV
     SGMERERKVS MRLHRGAPVN VSSSDLTSRQ DTSRMSTSQI PSRVTSSGLP STVHR
 
 
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