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Database: UniProt
Entry: A0A2K5TNN8_MACFA
LinkDB: A0A2K5TNN8_MACFA
Original site: A0A2K5TNN8_MACFA 
ID   A0A2K5TNN8_MACFA        Unreviewed;       510 AA.
AC   A0A2K5TNN8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Acetyl-CoA carboxylase kinase {ECO:0000256|ARBA:ARBA00032270};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.31 {ECO:0000256|ARBA:ARBA00012403};
DE   AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase {ECO:0000256|ARBA:ARBA00032865};
GN   Name=PRKAA1 {ECO:0000313|Ensembl:ENSMFAP00000001653.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000001653.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000001653.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000001653.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A
CC         reductase] = ADP + H(+) + O-phospho-L-seryl-[3-hydroxy-3-
CC         methylglutaryl-coenzyme A reductase]; Xref=Rhea:RHEA:23172,
CC         Rhea:RHEA-COMP:13692, Rhea:RHEA-COMP:13693, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00023941};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[acetyl-CoA carboxylase] = ADP + H(+) + O-
CC         phospho-L-seryl-[acetyl-CoA carboxylase]; Xref=Rhea:RHEA:20333,
CC         Rhea:RHEA-COMP:13722, Rhea:RHEA-COMP:13723, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036863};
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; A0A2K5TNN8; -.
DR   STRING; 9541.ENSMFAP00000001653; -.
DR   Ensembl; ENSMFAT00000000180.2; ENSMFAP00000001653.2; ENSMFAG00000036296.2.
DR   VEuPathDB; HostDB:ENSMFAG00000036296; -.
DR   GeneTree; ENSGT00940000158865; -.
DR   Proteomes; UP000233100; Chromosome 6.
DR   Bgee; ENSMFAG00000036296; Expressed in adult mammalian kidney and 13 other cell types or tissues.
DR   GO; GO:0050405; F:[acetyl-CoA carboxylase] kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0031331; P:positive regulation of cellular catabolic process; IEA:UniProt.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd14079; STKc_AMPK_alpha; 1.
DR   CDD; cd14403; UBA_AID_AAPK1; 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; IPR032270; AMPK_C.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR049020; PRKAA1/2_AID.
DR   InterPro; IPR028797; PRKAA1_UBA.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF21147; AMPK_alpha_AID; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; KA1-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022955};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          27..279
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   510 AA;  59149 MW;  07F775834F88A996 CRC64;
     MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR
     QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG
     RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF
     LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG
     IFYTPQYLNP SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
     DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS
     FLDDHHLSRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI
     MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTYSKMSL QLYQVDSRTY LLDFRSIDEW
     LPLGGRGKLV RRSQRSLPSS LKLKLLMRRM
//
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