STRAA_PONAB
ID STRAA_PONAB Reviewed; 431 AA.
AC Q5RBJ6;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=STE20-related kinase adapter protein alpha;
DE Short=STRAD alpha;
DE AltName: Full=STE20-related adapter protein;
GN Name=STRADA; Synonyms=STRAD;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH90864.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH90864.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pseudokinase which, in complex with CAB39/MO25
CC (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates
CC STK11/LKB1. Adopts a closed conformation typical of active protein
CC kinases and binds STK11/LKB1 as a pseudosubstrate, promoting
CC conformational change of STK11/LKB1 in an active conformation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a trimeric complex composed of STK11/LKB1, STRAD
CC (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta):
CC the complex tethers STK11/LKB1 in the cytoplasm and stimulates its
CC catalytic activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7RTN6}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; CR858650; CAH90864.1; -; mRNA.
DR RefSeq; NP_001125494.1; NM_001132022.1.
DR AlphaFoldDB; Q5RBJ6; -.
DR SMR; Q5RBJ6; -.
DR STRING; 9601.ENSPPYP00000009579; -.
DR GeneID; 100172403; -.
DR KEGG; pon:100172403; -.
DR CTD; 92335; -.
DR eggNOG; KOG0582; Eukaryota.
DR InParanoid; Q5RBJ6; -.
DR OrthoDB; 995563at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..431
FT /note="STE20-related kinase adapter protein alpha"
FT /id="PRO_0000260038"
FT DOMAIN 69..379
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 310..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTN6"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTN6"
FT MOD_RES 329
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000250|UniProtKB:Q7RTN6"
FT MOD_RES 401
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000250"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTN6"
SQ SEQUENCE 431 AA; 48333 MW; 1ED2CB33DC47A9D6 CRC64;
MSFLVSKPER IRRWVSEKFI VEGLRDLELF GEQPPGDTRR KTNDASSESI APFSKQEVMG
SFLPEGGCYE LLTVIGKGFE DLMTVNLARY KPTGEYVTVR RINLEACSNE MVTFLQGELH
VSKLFNHPNI VPYRATFIAD NELWVVTSFM AYGSAKDLIC THFMDGMNEL AIAYILQGVL
KALDYIHHMG YVHRSVKASH ILISVDGKVY LSGLRSNLSM ISHGQRQRVV HDFPKYSIKV
LPWLSPEVLQ QNLQGYDAKS DIYSVGITAC ELANGHVPFK DMPATQTLLE KLNGTVPCLL
DTSTIPAEEL TMSPSRSVAN SGLSDSLTTS TPRPSNGDSP SHPYHRTFSP HFHHFVEQCL
QRNPDARPSA STLLNHSFFK QIKRRASEAL PELLRPVTPI TNFEGSQSQD HSGIFGLVTN
LEELEVDDWE F