ID A0A2K5P6K3_CERAT Unreviewed; 725 AA.
AC A0A2K5P6K3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-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=MARK4 {ECO:0000313|Ensembl:ENSCATP00000045329.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000045329.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000045329.1}
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR AlphaFoldDB; A0A2K5P6K3; -.
DR Ensembl; ENSCATT00000069774.1; ENSCATP00000045329.1; ENSCATG00000045079.1.
DR GeneTree; ENSGT00940000159555; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000045079; Expressed in skeletal muscle tissue and 11 other cell types or tissues.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12197; MARK4_C; 1.
DR CDD; cd14407; UBA_MARK3_4; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF28; MAP_MICROTUBULE AFFINITY-REGULATING KINASE 4; 1.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 37..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 297..341
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 676..725
FT /note="KA1"
FT /evidence="ECO:0000259|PROSITE:PS50032"
FT REGION 358..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 79519 MW; 89585AC38446C322 CRC64;
SGRSSDKGPS WSSRSLGARC RNSIASCPEE QPHVGNYRLL RTIGKGNFAK VKLARHILTG
REVSMGTGWG SGQFPLFREV RIMKGLNHPN IVKLFEVIET EKTLYLVMEY ASAGEVFDYL
VSHGRMKEKE ARAKFRQIVS AVHYCHQKNI VHRDLKAENL LLDAEANIKI ADFGFSNEFT
LGSKLDTFCG SPPYAAPELF QGKKYDGPEV DIWSLGVILY TLVSGSLPFD GHNLKELRER
VLRGKYRVPF YMSTDCESIL RRFLVLNPAK RCTLEQIMKD KWINIGYEGE ELKPYTEPEE
DFGDTKRIEV MVGMGYTREE IKEALTSQKY NEVTATYLLL GRKTEEGGDR GAPGLALARV
RAPSDTTNGT SSSKGTSHSK GQRSSSSTYH RQRRHSDFCG PSPAPLHPKR SPTSTGEAEL
KEERLPGRKA SCSAAGSGSR GLPPSSPMVS SAHNPNKAEI PERRKDSTST PNNLPPSMMT
RRNTYVCTER PGAERPSLLP NGKENSSGTP RVPPASPSSH SLAPPSGERS RLARGSTIRS
TFHGGQVRDR RAGGGGGGGV QNGPPASPTL AHEAAPLPAG RPRPTTNLFT KLTSKLTRRV
ADEPERIGGP EVTSCHLPWD QTETAPRLLR FPWSVKLTSS RPPEALMAAL RQATAAARCR
CRQPQPFLLA CLHGGAGGPE PLSHFEVEVC QLPRPGLRGV LFRRVAGTAL AFRTLVTRIS
NDLEL
//
