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STRAA_RAT
ID   STRAA_RAT               Reviewed;         393 AA.
AC   Q7TNZ6; Q66HD4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=STE20-related kinase adapter protein alpha;
DE            Short=STRAD alpha;
DE   AltName: Full=STE20-related adapter protein;
GN   Name=Strada;
GN   Synonyms=Lyk5 {ECO:0000312|EMBL:AAP92801.1, ECO:0000312|RGD:727905}, Strad;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAP92801.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAP92801.1};
RA   Shan Y.X., Yu L.;
RT   "Cloning and characterization of human, mouse and rat Lyk5 gene.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH81911.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis {ECO:0000312|EMBL:AAH81911.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND INTERACTION WITH CAB39 AND STK11.
RX   PubMed=14511394; DOI=10.1186/1475-4924-2-28;
RA   Hawley S.A., Boudeau J., Reid J.L., Mustard K.J., Udd L., Makela T.P.,
RA   Alessi D.R., Hardie D.G.;
RT   "Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25
RT   alpha/beta are upstream kinases in the AMP-activated protein kinase
RT   cascade.";
RL   J. Biol. 2:28.1-28.16(2003).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|Ref.1};
CC         IsoId=Q7TNZ6-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15489334};
CC         IsoId=Q7TNZ6-2; Sequence=VSP_052216;
CC   -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:14511394}.
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; AY327409; AAP92801.1; -; mRNA.
DR   EMBL; BC081911; AAH81911.1; -; mRNA.
DR   RefSeq; NP_877972.1; NM_182820.1. [Q7TNZ6-1]
DR   AlphaFoldDB; Q7TNZ6; -.
DR   SMR; Q7TNZ6; -.
DR   IntAct; Q7TNZ6; 2.
DR   STRING; 10116.ENSRNOP00000011894; -.
DR   iPTMnet; Q7TNZ6; -.
DR   PhosphoSitePlus; Q7TNZ6; -.
DR   PaxDb; Q7TNZ6; -.
DR   PRIDE; Q7TNZ6; -.
DR   DNASU; 303605; -.
DR   GeneID; 303605; -.
DR   KEGG; rno:303605; -.
DR   UCSC; RGD:727905; rat. [Q7TNZ6-1]
DR   CTD; 92335; -.
DR   RGD; 727905; Strada.
DR   eggNOG; KOG0582; Eukaryota.
DR   InParanoid; Q7TNZ6; -.
DR   OrthoDB; 995563at2759; -.
DR   Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   PRO; PR:Q7TNZ6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0140535; C:intracellular protein-containing complex; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:1902554; C:serine/threonine protein kinase complex; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0019900; F:kinase binding; ISO:RGD.
DR   GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0070314; P:G1 to G0 transition; ISO:RGD.
DR   GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..393
FT                   /note="STE20-related kinase adapter protein alpha"
FT                   /id="PRO_0000260039"
FT   DOMAIN          32..341
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7RTN6"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7RTN6"
FT   MOD_RES         381
FT                   /note="Phosphothreonine; by LKB1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7RTN6"
FT   VAR_SEQ         1..21
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052216"
FT   CONFLICT        50
FT                   /note="S -> LA (in Ref. 2; AAH81911)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="A -> V (in Ref. 2; AAH81911)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  43553 MW;  B92AB012E2A8AD34 CRC64;
     MSFLANEASS ESIASFSKPE IMSSFLPEGG CYELLSVIGK GFEDLMTVNS RYKPTGEYVT
     VRRINLEACS NEMVTFLQGE LHVSKLFSHP NIVPYRATFI ADNELWAVTS FMAYGSAKDL
     IGTHFMDGMS ELAIAYILQG VLKALDYIHH MGYVHRSVKA SHILISTDGK VYLSGLRSNL
     SMISHGQRQR AVHDFPKYSI KVLPWLSPEV LQQNLQGYDA KSDIYSVGIT ACELANGHVP
     FKDMPATQML LEKLNGTVPC LLDTSTIPAE ELTMSPSRSI ANPGLNDSLA AGSLRPANGD
     SPSHPYHRTF SPHFHNFVEQ CLQRNPDARP NASTLLNHSF FKQIKRRASE ALPELLRPVT
     PITSFEGSQS QDHSGILGLV TNLEDLEVDD WEF
 
 
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