STRAA_MOUSE
ID STRAA_MOUSE Reviewed; 431 AA.
AC Q3UUJ4; Q6VEU7; Q9D0G8;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=STE20-related kinase adapter protein alpha;
DE Short=STRAD alpha;
DE AltName: Full=STE20-related adapter protein;
GN Name=Strada; Synonyms=Lyk5, Strad;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ24162.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAQ24162.1};
RA Zhou G., Wang J., Zhang Y.;
RT "Cloning of mouse protein kinase LYK5.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE23631.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23631.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB27626.1}, and
RC Hypothalamus {ECO:0000312|EMBL:BAE23631.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH58517.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58517.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH58517.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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=3;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3UUJ4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.1};
CC IsoId=Q3UUJ4-2; Sequence=VSP_052217, VSP_052218;
CC Name=3 {ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1};
CC IsoId=Q3UUJ4-3; Sequence=VSP_052217;
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; AY341872; AAQ24157.1; -; mRNA.
DR EMBL; AY341878; AAQ24162.1; -; mRNA.
DR EMBL; AK011451; BAB27626.1; -; mRNA.
DR EMBL; AK138358; BAE23631.1; -; mRNA.
DR EMBL; BC058517; AAH58517.1; -; mRNA.
DR CCDS; CCDS25550.1; -. [Q3UUJ4-3]
DR CCDS; CCDS56816.1; -. [Q3UUJ4-1]
DR RefSeq; NP_001239377.1; NM_001252448.1. [Q3UUJ4-1]
DR RefSeq; NP_001239378.1; NM_001252449.1. [Q3UUJ4-2]
DR RefSeq; NP_082402.1; NM_028126.3. [Q3UUJ4-3]
DR RefSeq; XP_006534358.1; XM_006534295.1. [Q3UUJ4-3]
DR RefSeq; XP_011247572.1; XM_011249270.1. [Q3UUJ4-1]
DR AlphaFoldDB; Q3UUJ4; -.
DR SMR; Q3UUJ4; -.
DR IntAct; Q3UUJ4; 1.
DR STRING; 10090.ENSMUSP00000099361; -.
DR iPTMnet; Q3UUJ4; -.
DR PhosphoSitePlus; Q3UUJ4; -.
DR EPD; Q3UUJ4; -.
DR MaxQB; Q3UUJ4; -.
DR PaxDb; Q3UUJ4; -.
DR PeptideAtlas; Q3UUJ4; -.
DR PRIDE; Q3UUJ4; -.
DR ProteomicsDB; 254596; -. [Q3UUJ4-1]
DR ProteomicsDB; 254597; -. [Q3UUJ4-2]
DR ProteomicsDB; 254598; -. [Q3UUJ4-3]
DR Antibodypedia; 64277; 340 antibodies from 31 providers.
DR DNASU; 72149; -.
DR Ensembl; ENSMUST00000007444; ENSMUSP00000007444; ENSMUSG00000069631. [Q3UUJ4-1]
DR Ensembl; ENSMUST00000103072; ENSMUSP00000099361; ENSMUSG00000069631. [Q3UUJ4-3]
DR GeneID; 72149; -.
DR KEGG; mmu:72149; -.
DR UCSC; uc007lyf.2; mouse. [Q3UUJ4-3]
DR UCSC; uc007lyg.2; mouse. [Q3UUJ4-1]
DR UCSC; uc011ygi.2; mouse. [Q3UUJ4-2]
DR CTD; 92335; -.
DR MGI; MGI:1919399; Strada.
DR VEuPathDB; HostDB:ENSMUSG00000069631; -.
DR eggNOG; KOG0582; Eukaryota.
DR GeneTree; ENSGT00940000158827; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q3UUJ4; -.
DR OMA; QRDPENR; -.
DR OrthoDB; 995563at2759; -.
DR PhylomeDB; Q3UUJ4; -.
DR TreeFam; TF319817; -.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR BioGRID-ORCS; 72149; 8 hits in 77 CRISPR screens.
DR ChiTaRS; Strada; mouse.
DR PRO; PR:Q3UUJ4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UUJ4; protein.
DR Bgee; ENSMUSG00000069631; Expressed in spermatocyte and 184 other tissues.
DR ExpressionAtlas; Q3UUJ4; baseline and differential.
DR Genevisible; Q3UUJ4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0140535; C:intracellular protein-containing complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:MGI.
DR GO; GO:0070314; P:G1 to G0 transition; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..431
FT /note="STE20-related kinase adapter protein alpha"
FT /id="PRO_0000260037"
FT DOMAIN 69..379
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 32..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..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 419
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000250|UniProtKB:Q7RTN6"
FT VAR_SEQ 5..41
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_052217"
FT VAR_SEQ 370..381
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052218"
SQ SEQUENCE 431 AA; 48236 MW; 6E4B14CC9B2B1D7D CRC64;
MSFLVSKPER IRRWVSEKFI VEGLRDLELF GEQPPGDTRR KANEASSESI ASFSKPEMMS
SFLPEGGCYE LLTIIGKGFE DLMTVNLARY KPTGEYVTVR RINLEACSNE MVTFLQGELH
VSKLFSHPNI VPYRATFIAD NELWVVTSFM AYGSAKDLIG THFMDGMNEL AIAYILQGVL
KALDYIHHMG YVHRSVKASH ILISTDGKVY LSGLRSNLSM ISHGQRQRAV HDFPKYSIKV
LPWLSPEVLQ QNLQGYDAKS DIYSVGITAC ELANGHVPFK DMPATQMLLE KLNGTVPCLL
DTSTIPAEEL TMSPSRSIAN PGLNDSLAAG SLRPSNGDSP SHPYHRTFSP HFHNFVEQCL
QRNPDARPNA STLLNHSFFK QIKRRASEAL PELLRPVTPI TNFEGSQSQD HSGIFGLVTN
LEDLEVDDWE F
