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Database: UniProt
Entry: A0A2R9AEX3_PANPA
LinkDB: A0A2R9AEX3_PANPA
Original site: A0A2R9AEX3_PANPA 
ID   A0A2R9AEX3_PANPA        Unreviewed;      1691 AA.
AC   A0A2R9AEX3;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:ENSPPAP00000015867.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000015867.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000015867.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000015867.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; AJFE02049239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02049248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008966062.1; XM_008967814.2.
DR   Ensembl; ENSPPAT00000038560.1; ENSPPAP00000015867.1; ENSPPAG00000030700.1.
DR   GeneID; 100976328; -.
DR   CTD; 8476; -.
DR   GeneTree; ENSGT01030000234517; -.
DR   OrthoDB; 988261at2759; -.
DR   Proteomes; UP000240080; Chromosome 1.
DR   Bgee; ENSPPAG00000030700; Expressed in cerebellum and 6 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:UP000240080};
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          971..1021
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1041..1160
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1186..1458
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   DOMAIN          1530..1543
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   REGION          1551..1691
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   COILED          886..941
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1561..1608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1616..1635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1654..1691
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   1691 AA;  193073 MW;  52D829B08A20BCD9 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 LVQASERLKN 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 EKGIEHQDSQ HSFLAFLNTP
     TDALDQFERK THQFFVKSFT TPTKCHQCTS LMVGLIRQGC SCEVCGFSCH ITCVNKAPTT
     CPVPPEQTKG PLGIDPQKGI GTAYEGHVRI PKPAGVKKGW QRALAIVCDF KLFLYDIAEG
     KASQPSVVIS QVIDMRDEEF SVSSVLASDV IHASRKDIPC IFRVTASQLS ASNNKCSILM
     LADTENEKNK WVGVLSELHK ILKKNKFRDR SVYVPKEAYD STLPLIKTTQ AAAIIDHERI
     ALGNEEGLFV VHVTKDEIIR VGDNKKIHQI ELIPNDQLVA VISGRNRHVR LFPMSALDGR
     ETDFYKLSET KGCQTITSGK VRHGALTCLC VAMKRQVLCY ELFQSKTRHR KFKEIQVPYN
     VQWMAIFSEQ LCVGFQSGFL RYPLNGEGNP YSMLHSNDHT LSFIAHQPMD AICAVEISSK
     EYLLCFNSIG IYTDCQGRRS RQQELMWPAN PSSCCYNAPY LSVYSENAVD IFDVNSMEWI
     QTLPLKKVRP LNNEGSLNLL GLETIRLIYF KNKMAEGDEL VVPETSDNSR KQMVRNINNK
     RRYSFRVPEE ERMQQRREML RDPEMRNKLI SNPTNFNHIA HMGPGDGIQI LKDLPMNPRP
     QESRTVFSGS VSIPSITKSR PEPGRSMSAS SGLSARSSAQ NGSALKREFS GGSYSAKRQP
     MPSPSEGSLS SGGMDQGSDA PARDFDGEDS DSPRHSTASN SSNLSSPPSP VSPRKTKSLS
     LESTDRGSWD P
//
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