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Database: UniProt
Entry: U3IVJ2_ANAPP
LinkDB: U3IVJ2_ANAPP
Original site: U3IVJ2_ANAPP 
ID   U3IVJ2_ANAPP            Unreviewed;       479 AA.
AC   U3IVJ2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 2.
DT   27-MAR-2024, entry version 69.
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=AKT3 {ECO:0000313|Ensembl:ENSAPLP00000011266.2};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000011266.2, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000011266.2, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000011266.2}
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. AGC Ser/Thr
CC       protein kinase family. RAC subfamily. {ECO:0000256|ARBA:ARBA00006935}.
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DR   AlphaFoldDB; U3IVJ2; -.
DR   SMR; U3IVJ2; -.
DR   STRING; 8840.ENSAPLP00000011266; -.
DR   Ensembl; ENSAPLT00000011990.2; ENSAPLP00000011266.2; ENSAPLG00000011477.2.
DR   GeneTree; ENSGT00940000157060; -.
DR   HOGENOM; CLU_000288_11_0_1; -.
DR   OMA; RGCQIMA; -.
DR   Proteomes; UP000016666; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0048854; P:brain morphogenesis; IEA:Ensembl.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:Ensembl.
DR   GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:1905653; P:positive regulation of artery morphogenesis; IEA:Ensembl.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
DR   GO; GO:0032008; P:positive regulation of TOR signaling; IEA:Ensembl.
DR   GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:Ensembl.
DR   CDD; cd01241; PH_PKB; 1.
DR   CDD; cd05593; STKc_PKB_gamma; 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; IPR034675; Akt3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039026; PH_PKB.
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; PTHR24351:SF199; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..107
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          148..405
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          406..479
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          458..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   479 AA;  55743 MW;  509D0EC3B143CF4D CRC64;
     MSDVTIVKEG WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ
     LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS
     PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK
     KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE
     RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA
     ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM
     EDIKFPRTLS ADAKSLLSGL LIKDPNKRLG GGPDDAKEIM RHSFFAGVNW QDVYDKKLVP
     PFKPQVTSET DTRYFDEEFT AQTITITPPE KYDEDGMDCM DNERRPHFPQ FSYSASGRE
//
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