AKT2A_XENLA
ID AKT2A_XENLA Reviewed; 486 AA.
AC Q7ZX15;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RAC-beta serine/threonine-protein kinase A;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase Akt-2-A;
DE AltName: Full=Protein kinase B, beta-A;
DE Short=PKB beta-A;
DE AltName: Full=RAC-PK-beta-A;
GN Name=akt2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH46261.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH46261.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Akt2-a is one of several closely related serine/threonine-
CC protein kinases known as the AKT kinase, and which regulate many
CC processes including metabolism, proliferation, cell survival, growth
CC and angiogenesis. This is mediated through serine and/or threonine
CC phosphorylation of a range of downstream substrates. Over 100 substrate
CC candidates have been reported so far, but for most of them, no isoform
CC specificity has been reported (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q60823};
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:0000250|UniProtKB:Q60823};
CC -!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain (Thr-
CC 314) and the other in the C-terminal regulatory region (Ser-479), need
CC to be phosphorylated for its full activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000305}.
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DR EMBL; BC046261; AAH46261.1; -; mRNA.
DR RefSeq; NP_001080091.1; NM_001086622.1.
DR RefSeq; XP_018084111.1; XM_018228622.1.
DR AlphaFoldDB; Q7ZX15; -.
DR SMR; Q7ZX15; -.
DR GeneID; 379783; -.
DR KEGG; xla:379783; -.
DR CTD; 379783; -.
DR Xenbase; XB-GENE-484172; akt2.L.
DR OMA; EVMSHRF; -.
DR OrthoDB; 614710at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 379783; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
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-KW.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd01241; PH_PKB; 1.
DR CDD; cd05595; STKc_PKB_beta; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR034677; Akt2.
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 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; SSF56112; SSF56112; 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 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..486
FT /note="RAC-beta serine/threonine-protein kinase A"
FT /id="PRO_0000223508"
FT DOMAIN 5..110
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 157..414
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 415..486
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 455..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 163..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 136
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 311
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 318
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 486 AA; 56310 MW; F124CAE30758016B CRC64;
MNEVMVIKEG WLQKRGEYIK TWRPRYFLLK SDGSFIGYKE KPESTEHNVV LPPLNNFSVA
ECQLMKTERP RPNTFVIRCL QWTTVIERTF HVDTPEEREE WIIAIQTVAN GLKNQVPEDE
EEEAMEVKYG SPSDVSSAEQ MDVAMSKGHP KVTMNDFDYL KLLGKGTFGK VILVREKATG
RYYAMKILRK EVIIAKDEVA HTLTESRVLQ NTKHPFLTAL KYAFQTSDRL CFVMEYANGG
ELFFHLSRER VFTEDRARFY GAEIVSALEY LHSRNVVYRD IKLENLMLDK DGHVKITDFG
LCKEGITDGA TMRTFCGTPE YLAPEVLEDN DYGRAVDWWG LGVVMYEMMC GRLPFYNQDH
ERLFELILME EIRFPRTLSP EAKSLLAGLL KKDPKQRLGG GPNDAQEVMS HRFFVSINWQ
DVTERKLTPP FKPQVTSEID TRYFDDEFTA QSITLTPPDR YDNLDALESD QRPHFPQFSY
SASIRE
