ID A0A2I3TF01_PANTR Unreviewed; 1696 AA.
AC A0A2I3TF01;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=CDC42BPA {ECO:0000313|Ensembl:ENSPTRP00000087832.1,
GN ECO:0000313|VGNC:VGNC:57563};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000087832.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000087832.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000087832.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR EMBL; AACZ04040722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04040723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04040724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPTRT00000083255.1; ENSPTRP00000087832.1; ENSPTRG00000042934.1.
DR VGNC; VGNC:57563; CDC42BPA.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000042934; Expressed in colon and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20864; C1_MRCKalpha; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR CDD; cd05623; STKc_MRCK_alpha; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR026611; MRCK_alpha_cat.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE_THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 77..343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 344..414
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 976..1026
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1046..1165
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1191..1463
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1535..1548
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 940..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 441..669
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 715..820
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1566..1613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1696 AA; 193286 MW; F9A58C149E690C56 CRC64;
MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
CFREERDVLV NGDNKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEDMARF
YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP
EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA
GPTSLDLDVN VQRTLDNNLA TEAYERRIKR LEQEKLELSR KLQESTQTVQ ALQYSTVDGP
LTASKDLEIK NLKEEIEKLR KQVTESSHLE QQLEEANAVR QELDDAFRQI KAYEKQIKTL
QQEREDLNKE LVQASERLKY QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
RDKEEEVDLV MQKVESLRQE LRRTERAKKE LEVHTEALAA EASKDRKLRE QSEHYSKQLE
NELEGLKQKQ ISYSPGVCSI EHQQEITKLK TDLEKKSIFY EEELSKREGI HANEIKNLKK
ELHDSEGQQL ALNKEIMILK DKLEKTRRES QSEREEFESE FKQQYEREKV LLTEENKKLT
SELDKLTTLY ENLSIHNQQL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
NKVKASNIIT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGMGTVDST PLSVHTPTLR
KKGCPGSTGF PPKRKTHQFF VKSFTTPTKC HQCTSLMVGL IRQGCSCEVC GFSCHITCVN
KAPTACPVPP EQTKGPLGID PQKGIGTAYE GHVRIPKPAG VKKGWQRALA IVCDFKLFLY
DIAEGKASQP SVVISQVIDM RDEEFSVSSV LASDVIHASR KDIPCIFRVT ASQLSASNNK
CSILMLADTE NEKNKWVGVL SELHKILKKN KFRDRSVYVP KEAYDSTLPL IKTTQAAAII
DHERIALGNE EGLFVVHVTK DEIIRVGDNK KIHQIELIPN DQLVAVISGR NRHVRLFPMS
ALDGRETDFY KLSETKGCQT ITSGKVRHGA LTCLCVAMKR QVLCYELFQS KTRHRKFKEI
QVPYNVQWMA IFSEQLCVGF QSGFLRYPLN GEGNPYSMLH SNDHTLSFIA HQPMDAICAV
EISSKEYLLC FNSIGIYTDC QGRRSRQQEL MWPANPSSCC YNAPYLSVYS ENAVDIFDVN
SMEWIQTLPL KKVRPLNNEG SLNLLGLETI RLIYFKNKMA EGDELVVPET SDNSRKQMVR
NINNKRRYSF RVPEEERMQQ RREMLRDPEM RNKLISNPTN FNHIAHMGPG DGIQILKDLP
MNPRPQESRT VFSGSVSIPS ITKSRPEPGR SMSASSGLSA RSSAQNGSAL KREFSGGSYS
AKRQPMPSPS EGSLSSGGMD QGSDAPARDF DGEDSDSPRH STASNSSNLS SPPSPVSPRK
TKSLSLESTD RGSWDP
//
