ID F1SAM8_PIG Unreviewed; 1644 AA.
AC F1SAM8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 91.
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=CDC42BPB {ECO:0000313|Ensembl:ENSSSCP00000002731.3,
GN ECO:0000313|VGNC:VGNC:86453};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000002731.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000002731.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000002731.3};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000002731.3}
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 RefSeq; XP_013833873.1; XM_013978419.1.
DR PeptideAtlas; F1SAM8; -.
DR Ensembl; ENSSSCT00000002802.5; ENSSSCP00000002731.3; ENSSSCG00000002523.5.
DR VGNC; VGNC:86453; CDC42BPB.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_3_1; -.
DR TreeFam; TF313551; -.
DR Proteomes; UP000008227; Unplaced.
DR Bgee; ENSSSCG00000002523; Expressed in endocardial endothelium and 43 other cell types or tissues.
DR ExpressionAtlas; F1SAM8; baseline and differential.
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: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; cd20865; C1_MRCKbeta; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 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; IPR020454; DAG/PE-bd.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 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:SF34; SERINE_THREONINE-PROTEIN KINASE MRCK BETA; 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 PRINTS; PR00008; DAGPEDOMAIN.
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 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 1: Evidence at protein level;
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1SAM8};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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 8..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 275..345
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 958..1008
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1028..1147
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1173..1446
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1516..1529
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 901..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 372..578
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 691..739
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 836..870
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1548..1571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1593..1607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1644 AA; 185937 MW; 395B27D975A91BF0 CRC64;
MQLHREDFEI IKVIGRGAFG EVAVVRMKST ERIYAMKILN KWEMLKRAET ACFREERDVL
VNGDSQWLTT LHYAFQDENY LYLVMDYYVG GDLLTLLSKF EDRLPEDMAR FYIGEMVLAI
DSIHQLHYVH RDIKPDNVLL DVNGHIRLAD FGSCLKMNDD GTVQSSVAVG TPDYISPEIL
QAMEDGMGRY GPECDWWSLG VCMYEMLYGE TPFYAESLVE TYGKIMNHEE RFQFPSHVTD
VSEEAKDLIQ RLICSRERRL GQNGVEDFKK HAFFQGLNWE TIRNLEAPYI PDVSSPSDTS
NFDVDDDVLR NVEILPPASH TGFSGLHLPF IGFTFTTESC FSDRGSLKSI MQSSTLTKDE
GLQRDLENSL QVEAYERRIR RLEQERLELS RKLQEATQTV QSFHGAARTL GSAARDKEIK
KLNEEIERLK NKIAESNKLE RQLEDTVTLR QEQEDSTHRL KGLEKQYRAV RQEKEDFHKQ
LIEASERLKS QARELKDAHQ QRKLALQEFS ELNERMAELR SQKQKVSRQL RDREEEVEAA
LQKIDALRQE VRRADKCRKE LEAQLEDAVA EASKERKLRE HSENFSKQIE SELEALKMKQ
GGRGPGAALE HQQEISRIKS ELEKKVLFYE EELVRREASH VLELKTVKKE VHDSEGHQLA
LQKEVLVLKD KLEKSKRERH SELEEAVGTV KDKYERERAV LSEENKKLTA ENEKLCAFVD
KLTAQNRQLE DELQDLAAKK ESVAHWEAQI AEIIQWVSDE KDARGYLQAL ASKMTEELEA
LRSSSLGSRT LDPLWKVRRS QKLDMSARLE LQSALEAEIR AKQLVQEELR KVKDMNLSFE
SKLKDSEAKN RELLEEMEIL KKKMEEKFRT DAGLKLPDFQ DSIFEYFNTA PLAHDLTFRA
SSASEQETQA AKPEAMPPSS VAASTEQQED VARAPQRPPT VPLPSTQALA LAGPKPKAHQ
FSIKSFSSPT QCSHCTSLMV GLIRQGYACD VCSFACHVSC RDSAPQVCPI PPEQSKRPLG
VDVQRGIGTA YKGYVKVPKP TGVKKGWQRA YAVVCDCKLF LYDLPEGKST QPGVVASQVL
DLRDEEFSVS SVLASDVIHA SRRDIPCIFR VTASLLGTPS KTSSLLILTE NENEKRKWVG
ILEGLQSILQ KNRLRSQVVH SPQEAYDSSL PLIKAVLAAA ILDADRIAVG LEEGLYVVEV
TRDVIVRVAD YKKVYQIELA PKEKVAALLC GRNHHVHLCP WSSFDGAEGT VDIKLPETKG
CQLIATGAPK KSSPTCLFVA VKRLVLCYEM QRTKPFHRKL SELAAPGPVQ WMAVLKDKLC
VGYPSGFSLL SPQGEGQALN LVNPNDPSLT FLSQQSFDAL CAVELQSEEY LLCFSHMGLY
VDPQGRRSRM QELMWPAAPV ACSCSPSHVT VYSDYGVDVF DARSMEWVQT IGLRRIRPLN
SEGSLNLLNC EPPRLIYFKS KFAGPALNVP DTSDNSKKQM LRTRSKRRFV FKVPEEERLQ
QRREMLRDPE LRSRMISNPT NFNHVAHMGP GDGMQVLMDL PLSAVPPSQE ERPGPAPASL
SRQPPPRNKP YVSWPSSGGS EPGVAVPLRS MSDPDQDFDK EPDSDSTKHS TPSNSSNPSG
PPSPNSPHRS QLPLEGLEQP SYDA
//
