CAB39_MOUSE
ID CAB39_MOUSE Reviewed; 341 AA.
AC Q06138; Q8VDZ8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Calcium-binding protein 39;
DE AltName: Full=MO25alpha;
DE AltName: Full=Protein Mo25;
GN Name=Cab39; Synonyms=Mo25;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8418809; DOI=10.1002/mrd.1080340102;
RA Miyamoto H., Matsushiro A., Nozaki M.;
RT "Molecular cloning of a novel mRNA sequence expressed in cleavage stage
RT mouse embryos.";
RL Mol. Reprod. Dev. 34:1-7(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 97-107; 197-209 AND 269-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Component of a complex that binds and activates STK11/LKB1.
CC In the complex, required to stabilize the interaction between
CC CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 (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: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Transcribed during early mouse development.
CC Detected at all developmental stages from the egg through the
CC blastocyst, most abundant at the 2-cell stage.
CC -!- SIMILARITY: Belongs to the Mo25 family. {ECO:0000305}.
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DR EMBL; S51858; AAB24801.1; -; mRNA.
DR EMBL; AK144665; BAE25997.1; -; mRNA.
DR EMBL; CH466520; EDL40253.1; -; Genomic_DNA.
DR EMBL; CH466520; EDL40254.1; -; Genomic_DNA.
DR EMBL; CH466520; EDL40256.1; -; Genomic_DNA.
DR EMBL; BC020041; AAH20041.1; -; mRNA.
DR CCDS; CCDS15112.1; -.
DR RefSeq; NP_598542.3; NM_133781.4.
DR RefSeq; XP_006529153.1; XM_006529090.3.
DR RefSeq; XP_006529154.1; XM_006529091.2.
DR RefSeq; XP_011246209.1; XM_011247907.2.
DR RefSeq; XP_017168028.1; XM_017312539.1.
DR AlphaFoldDB; Q06138; -.
DR SMR; Q06138; -.
DR BioGRID; 198428; 2.
DR IntAct; Q06138; 1.
DR MINT; Q06138; -.
DR STRING; 10090.ENSMUSP00000108987; -.
DR iPTMnet; Q06138; -.
DR PhosphoSitePlus; Q06138; -.
DR EPD; Q06138; -.
DR MaxQB; Q06138; -.
DR PaxDb; Q06138; -.
DR PeptideAtlas; Q06138; -.
DR PRIDE; Q06138; -.
DR ProteomicsDB; 273814; -.
DR Antibodypedia; 34407; 149 antibodies from 27 providers.
DR DNASU; 12283; -.
DR Ensembl; ENSMUST00000097666; ENSMUSP00000095270; ENSMUSG00000036707.
DR Ensembl; ENSMUST00000113360; ENSMUSP00000108987; ENSMUSG00000036707.
DR GeneID; 12283; -.
DR KEGG; mmu:12283; -.
DR UCSC; uc007bum.2; mouse.
DR CTD; 51719; -.
DR MGI; MGI:107438; Cab39.
DR VEuPathDB; HostDB:ENSMUSG00000036707; -.
DR eggNOG; KOG1566; Eukaryota.
DR GeneTree; ENSGT00390000004360; -.
DR HOGENOM; CLU_035755_0_0_1; -.
DR InParanoid; Q06138; -.
DR OMA; HLKLCMN; -.
DR OrthoDB; 865327at2759; -.
DR PhylomeDB; Q06138; -.
DR TreeFam; TF314910; -.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 12283; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Cab39; mouse.
DR PRO; PR:Q06138; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q06138; protein.
DR Bgee; ENSMUSG00000036707; Expressed in facial nucleus and 266 other tissues.
DR ExpressionAtlas; Q06138; baseline and differential.
DR Genevisible; Q06138; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
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:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:MGI.
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:0032147; P:activation of protein kinase activity; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013878; Mo25.
DR PANTHER; PTHR10182; PTHR10182; 1.
DR Pfam; PF08569; Mo25; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Reference proteome.
FT CHAIN 1..341
FT /note="Calcium-binding protein 39"
FT /id="PRO_0000209825"
FT CONFLICT 332
FT /note="D -> N (in Ref. 1; AAB24801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 39843 MW; E7FECA529D6FE811 CRC64;
MPFPFGKSHK SPADIVKNLK ESMAVLEKQD ISDKKAEKAT EEVSKNLVAM KEILYGTNEK
EPQTEAVAQL AQELYNSGLL GTLVADLQLI DFEGKKDVAQ IFNNILRRQI GTRTPTVEYI
CTQQNILFML LKGYESPEIA LNCGIMLREC IRHEPLAKII LWSEQFYDFF RYVEMSTFDI
ASDAFATFKD LLTRHKLLSA EFLEQHYDRF FSEYEKLLHS ENYVTKRQSL KLLGELLLDR
HNFTIMTKYI SKPENLKLMM NLLRDKSRNI QFEAFHVFKV FVANPNKTQP ILDILLKNQT
KLIEFLSKFQ NDRTEDEQFN DEKTYLVKQI RDLKRAAQQE A
