CB39L_MOUSE
ID CB39L_MOUSE Reviewed; 337 AA.
AC Q9DB16; Q8BG52; Q91WB8; Q91YL0;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Calcium-binding protein 39-like;
DE AltName: Full=MO25beta;
DE AltName: Full=Mo25-like protein;
GN Name=Cab39l;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, Pituitary, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DB16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DB16-2; Sequence=VSP_007417, VSP_007418;
CC -!- SIMILARITY: Belongs to the Mo25 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16128.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005323; BAB23953.2; -; mRNA.
DR EMBL; AK030474; BAC26978.1; -; mRNA.
DR EMBL; AK053642; BAC35457.1; -; mRNA.
DR EMBL; AK076758; BAC36470.1; -; mRNA.
DR EMBL; AK076867; BAC36513.1; -; mRNA.
DR EMBL; BC016128; AAH16128.1; ALT_INIT; mRNA.
DR EMBL; BC016546; AAH16546.2; -; mRNA.
DR CCDS; CCDS27171.1; -. [Q9DB16-1]
DR RefSeq; NP_081184.3; NM_026908.3. [Q9DB16-1]
DR RefSeq; XP_006519557.1; XM_006519494.2.
DR RefSeq; XP_006519558.1; XM_006519495.2.
DR RefSeq; XP_017171665.1; XM_017316176.1.
DR AlphaFoldDB; Q9DB16; -.
DR SMR; Q9DB16; -.
DR BioGRID; 213169; 10.
DR STRING; 10090.ENSMUSP00000022553; -.
DR iPTMnet; Q9DB16; -.
DR PhosphoSitePlus; Q9DB16; -.
DR EPD; Q9DB16; -.
DR MaxQB; Q9DB16; -.
DR PaxDb; Q9DB16; -.
DR PeptideAtlas; Q9DB16; -.
DR PRIDE; Q9DB16; -.
DR ProteomicsDB; 283687; -. [Q9DB16-1]
DR ProteomicsDB; 283688; -. [Q9DB16-2]
DR Antibodypedia; 23903; 192 antibodies from 30 providers.
DR DNASU; 69008; -.
DR Ensembl; ENSMUST00000022553; ENSMUSP00000022553; ENSMUSG00000021981. [Q9DB16-1]
DR Ensembl; ENSMUST00000225595; ENSMUSP00000153643; ENSMUSG00000021981. [Q9DB16-2]
DR GeneID; 69008; -.
DR KEGG; mmu:69008; -.
DR UCSC; uc007uek.1; mouse. [Q9DB16-1]
DR CTD; 81617; -.
DR MGI; MGI:1914081; Cab39l.
DR VEuPathDB; HostDB:ENSMUSG00000021981; -.
DR eggNOG; KOG1566; Eukaryota.
DR GeneTree; ENSGT00390000004360; -.
DR HOGENOM; CLU_035755_0_0_1; -.
DR InParanoid; Q9DB16; -.
DR OMA; NFAVMTK; -.
DR OrthoDB; 865327at2759; -.
DR PhylomeDB; Q9DB16; -.
DR TreeFam; TF314910; -.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR BioGRID-ORCS; 69008; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cab39l; mouse.
DR PRO; PR:Q9DB16; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9DB16; protein.
DR Bgee; ENSMUSG00000021981; Expressed in choroid plexus epithelium and 259 other tissues.
DR ExpressionAtlas; Q9DB16; baseline and differential.
DR Genevisible; Q9DB16; MM.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
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 Alternative splicing; Reference proteome.
FT CHAIN 1..337
FT /note="Calcium-binding protein 39-like"
FT /id="PRO_0000209827"
FT VAR_SEQ 279..296
FT /note="VFVASPHKTQPIVEILLK -> NSVFITNRIHGLKRWLSS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007417"
FT VAR_SEQ 297..337
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007418"
FT CONFLICT 45
FT /note="S -> P (in Ref. 1; BAB23953)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="L -> R (in Ref. 2; AAH16546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 39106 MW; C62B5B58095A98C8 CRC64;
MKKMPLFSKS HKNPAEIVKI LKDNLAILEK QDKKTDKASE EVSKSLQAMK EILCGTNDKE
PPTEAVAQLA QELYSSGLLV TLIADLQLID FEGKKDVTQI FNNILRRQIG TRCPTVEYIS
SHPHILFMLL KGYEAPQIAL RCGIMLRECI RHEPLAKIIL FSNQFRDFFK YVELSTFDIA
SDAFATFKDL LTRHKVLVAD FLEQNYDTIF EDYEKLLQSE NYVTKRQSLK LLGELILDRH
NFTIMTKYIS KPENLKLMMN LLRDKSPNIQ FEAFHVFKVF VASPHKTQPI VEILLKNQPK
LIEFLSSFQK ERTDDEQFAD EKNYLIKQIR DLKKAAP
