ID G3H4B2_CRIGR Unreviewed; 824 AA.
AC G3H4B2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Microtubule-associated serine/threonine-protein kinase 3 {ECO:0000313|EMBL:EGV97454.1};
GN ORFNames=I79_005112 {ECO:0000313|EMBL:EGV97454.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV97454.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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DR EMBL; JH000137; EGV97454.1; -; Genomic_DNA.
DR AlphaFoldDB; G3H4B2; -.
DR STRING; 10029.G3H4B2; -.
DR PaxDb; 10029-XP_007611093-1; -.
DR eggNOG; KOG0606; Eukaryota.
DR InParanoid; G3H4B2; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR24356:SF140; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 3; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGV97454.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..163
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 164..235
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 469..557
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 247..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..587
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..728
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 88580 MW; 97C3AB264995E075 CRC64;
MQGSGLPTQP ECPGPAHSLL ITSLGHIKLT DFGLSKIGLM SMATNLYEGH IEKDAREFVD
KQVCGTPEYI APEVIFRQGY GKPVDWWAMG IILYEFLVGC VPFFGDTPEE LFGQVVSDEI
LWPEGDEALP ADAQDLITRL LRQSPMERLG TGGTHEVKQH PFFLALDWAG LLRHKAEFVP
QLEAEDDTSY FDTRSERYRH LGSEDEETND EESSTEIPQF SSCSHRFSKV YSSSEFLAVQ
PTPTFAERSF SEDREDGWER NSEGDSGRRL SIDLRLRSWA CASSCLPSSP LPDRGPNPSL
NTISLDTMPK FAFSSEDEGA GSGPADPKKP VFILGEPDPP PPTTPVTPKP CNLSADTAVL
SHARLRSNST GARHSTPRPL DGGRGRRLGG PRDPGPEKPR ASPGGGGGGS RVPKSASVSA
LSLIITADDG SGGPLMSPLS PRSLSSNPSS RDSSPSRDPS PVCGSLRPPI VIHSSGKKYG
FSLRAIRVYM GDSDVYTVHH VVWSVEEGSP AQEAGLRAGD LITHINGESV LGLVHMDVVE
LLLKSGNKIS LRTTALENTS IKVGPARKNT AKGRMARRNK RSRRRETQDR RKSLFKRISK
PSSVLHTSRS FSSGLHHSLS SSESLPGSPT HSLSPSPTTP CRSPAPDAPT DTASPPSVSP
SSSSPDSPAT GHTRPSSLHG LAAKLGPPRH KSGRRKSTSS IPPSPLACPP VPTPPPRSPS
PLPGHIPIPV RSPRLRRGQS ADKLGLGTSE RLEGDGGWRG RGTEAELVVM RRLHLSERRD
SFKKQEAVQE VSFDEEPGPP RAVPKIAVQG AEATPGTPGP ATKD
//
