AKT2B_XENLA
ID AKT2B_XENLA Reviewed; 485 AA.
AC Q6IP76;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=RAC-beta serine/threonine-protein kinase B;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase Akt-2-B;
DE AltName: Full=Protein kinase B, beta-B;
DE Short=PKB beta-B;
DE AltName: Full=RAC-PK-beta-B;
GN Name=akt2-b;
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:AAH72041.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH72041.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Akt2-b 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 313) and the other in the C-terminal regulatory region (Ser-478), 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; BC072041; AAH72041.1; -; mRNA.
DR RefSeq; NP_001085101.1; NM_001091632.1.
DR AlphaFoldDB; Q6IP76; -.
DR SMR; Q6IP76; -.
DR DNASU; 432172; -.
DR GeneID; 432172; -.
DR KEGG; xla:432172; -.
DR CTD; 432172; -.
DR Xenbase; XB-GENE-17345542; akt2.S.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 432172; Expressed in blastula 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..485
FT /note="RAC-beta serine/threonine-protein kinase B"
FT /id="PRO_0000223509"
FT DOMAIN 5..109
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 156..413
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 414..485
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 454..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 162..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 310
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 317
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 485 AA; 56024 MW; 27D584109098CC56 CRC64;
MNEVMVIKEG WLQKRGEYIK TWRPRYFLLK SDGSFIGYKE KPDSTEHSLL PPLNNFSVAE
CQLMKTERPR PNTFVIRCLQ WTTVIERTFH VDTPEEREEW IIAIQTVANG LKNQVPEDEE
EEAMEVKYGS PSDVSSAEQM DVAMSKGRPK VTMNDFDYLK LLGKGTFGKV ILVREKATGL
YYAMKILRKE VIIAKDEVAH TLTESRVLQN TKHPFLTGLK YAFQTSDRLC FVMEYANGGE
LFFHLSRERV FTEDRARFYG AEIVSALEYL HSRNVVYRDI KLENLMLDKD GHVKITDFGL
CKEGITDGAT MRTFCGTPEY LAPEVLEDND YGRAVDWWGL GVVMYEMMCG RLPFYNQDHE
RLFELILMEE TRFPRTLSPE AKSLLAGLLK KDPKQRLGGG PDDAQEVMSH GFFASINWQD
VTERKLSPPF KPQVTSEIDT RYFDDEFTAQ SITLTPPDRY DNLDALESEQ RPHFPQFSYS
SSIRE
