ST38L_MOUSE
ID ST38L_MOUSE Reviewed; 464 AA.
AC Q7TSE6; B2KFR4; Q6P6K6; Q8BWK4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase 38-like;
DE EC=2.7.11.1;
DE AltName: Full=NDR2 protein kinase;
DE AltName: Full=Nuclear Dbf2-related kinase 2;
GN Name=Stk38l {ECO:0000312|EMBL:AAP44998.1};
GN Synonyms=Ndr2 {ECO:0000303|PubMed:15037617};
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:AAP44998.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP44998.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAP44998.1};
RX PubMed=15037617; DOI=10.1074/jbc.m402472200;
RA Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A., Hemmings B.A.;
RT "Regulation of NDR2 protein kinase by multi-site phosphorylation and the
RT S100B calcium-binding protein.";
RL J. Biol. Chem. 279:23806-23812(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAO66474.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO66474.1};
RC TISSUE=Basophil {ECO:0000312|EMBL:AAO66474.1};
RX PubMed=15308672; DOI=10.1074/jbc.m403552200;
RA Stork O., Zhdanov A., Kudersky A., Yoshikawa T., Obata K., Pape H.-C.;
RT "Neuronal functions of the novel serine/threonine kinase Ndr2.";
RL J. Biol. Chem. 279:45773-45781(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetal heart;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|EMBL:AAH62170.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal jaw {ECO:0000312|EMBL:AAH62170.1}, and
RC Fetal limb {ECO:0000312|EMBL:AAH62170.1};
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Pancreas;
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).
RN [8]
RP FUNCTION, AND INTERACTION WITH MICAL1.
RX PubMed=21730291; DOI=10.1128/mcb.01389-10;
RA Zhou Y., Adolfs Y., Pijnappel W.W., Fuller S.J., Van der Schors R.C.,
RA Li K.W., Sugden P.H., Smit A.B., Hergovich A., Pasterkamp R.J.;
RT "MICAL-1 is a negative regulator of MST-NDR kinase signaling and
RT apoptosis.";
RL Mol. Cell. Biol. 31:3603-3615(2011).
CC -!- FUNCTION: Involved in the regulation of structural processes in
CC differentiating and mature neuronal cells.
CC {ECO:0000269|PubMed:15308672, ECO:0000269|PubMed:21730291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by binding of S100B which releases
CC autoinhibitory N-lobe interactions, enabling ATP to bind and the
CC autophosphorylation of Ser-282. Thr-442 then undergoes calcium-
CC dependent phosphorylation by STK24/MST3. Interactions between
CC phosphorylated Thr-442 and the N-lobe promote additional structural
CC changes that complete the activation of the kinase. Autoinhibition is
CC also released by the binding of MOB1/MOBKL1A and MOB2 to the N-terminal
CC of STK38L (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimeric S100B binds two molecules of STK38L. Interacts
CC with MOB1 and MOB2 (By similarity). Interacts with MICAL1; leading to
CC inhibit the protein kinase activity by antagonizing activation by
CC MST1/STK4. {ECO:0000250, ECO:0000269|PubMed:21730291}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15308672}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15308672}. Membrane
CC {ECO:0000269|PubMed:15308672}. Note=Associated with the actin
CC cytoskeleton. Co-localizes with STK24/MST3 in the membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TSE6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSE6-2; Sequence=VSP_012334;
CC -!- TISSUE SPECIFICITY: Highly expressed in the large and small intestine,
CC stomach and testis. High levels also present in the brain, in
CC particular the neurocortex, basal forebrain, hippocampus, the amygdala,
CC cerebellum and brainstem. {ECO:0000269|PubMed:15037617,
CC ECO:0000269|PubMed:15308672}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AY292400; AAP44998.1; -; mRNA.
DR EMBL; AY223819; AAO66474.1; -; mRNA.
DR EMBL; AK052288; BAC34918.1; -; mRNA.
DR EMBL; CU207394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466572; EDL10715.1; -; Genomic_DNA.
DR EMBL; BC062170; AAH62170.1; -; mRNA.
DR CCDS; CCDS39712.1; -. [Q7TSE6-1]
DR RefSeq; NP_001333595.1; NM_001346666.1.
DR RefSeq; NP_766322.1; NM_172734.3. [Q7TSE6-1]
DR RefSeq; XP_006507090.2; XM_006507027.2. [Q7TSE6-2]
DR AlphaFoldDB; Q7TSE6; -.
DR SMR; Q7TSE6; -.
DR BioGRID; 231267; 2.
DR IntAct; Q7TSE6; 1.
DR STRING; 10090.ENSMUSP00000001675; -.
DR iPTMnet; Q7TSE6; -.
DR PhosphoSitePlus; Q7TSE6; -.
DR EPD; Q7TSE6; -.
DR jPOST; Q7TSE6; -.
DR MaxQB; Q7TSE6; -.
DR PaxDb; Q7TSE6; -.
DR PeptideAtlas; Q7TSE6; -.
DR PRIDE; Q7TSE6; -.
DR ProteomicsDB; 257431; -. [Q7TSE6-1]
DR ProteomicsDB; 257432; -. [Q7TSE6-2]
DR Antibodypedia; 24379; 259 antibodies from 28 providers.
DR DNASU; 232533; -.
DR Ensembl; ENSMUST00000001675; ENSMUSP00000001675; ENSMUSG00000001630. [Q7TSE6-1]
DR Ensembl; ENSMUST00000111644; ENSMUSP00000107271; ENSMUSG00000001630. [Q7TSE6-2]
DR GeneID; 232533; -.
DR KEGG; mmu:232533; -.
DR UCSC; uc009esh.2; mouse. [Q7TSE6-1]
DR CTD; 23012; -.
DR MGI; MGI:1922250; Stk38l.
DR VEuPathDB; HostDB:ENSMUSG00000001630; -.
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000153544; -.
DR HOGENOM; CLU_000288_67_0_1; -.
DR InParanoid; Q7TSE6; -.
DR OMA; PERYSEN; -.
DR OrthoDB; 759391at2759; -.
DR TreeFam; TF105337; -.
DR BioGRID-ORCS; 232533; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Stk38l; mouse.
DR PRO; PR:Q7TSE6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TSE6; protein.
DR Bgee; ENSMUSG00000001630; Expressed in ascending aorta and 207 other tissues.
DR ExpressionAtlas; Q7TSE6; baseline and differential.
DR Genevisible; Q7TSE6; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051128; P:regulation of cellular component organization; IDA:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; ATP-binding; Cytoplasm;
KW Cytoskeleton; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2H1"
FT CHAIN 2..464
FT /note="Serine/threonine-protein kinase 38-like"
FT /id="PRO_0000086721"
FT DOMAIN 90..383
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 384..453
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 64..89
FT /note="S100B binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 96..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O95835,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2H1,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2H1"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2H1"
FT MOD_RES 282
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2H1"
FT MOD_RES 442
FT /note="Phosphothreonine; by STK24/MST3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2H1"
FT VAR_SEQ 423
FT /note="V -> VAFFLFLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012334"
FT CONFLICT 97
FT /note="G -> A (in Ref. 1; AAP44998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 53772 MW; BE7E0CECDB63A8FD CRC64;
MAMTAGATTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE VAMEEEGLAD
EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI
LRKADMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM
KKDTLTEEET QFYISETVLA IDAIHQLGFI HRDVKPDNLL LDAKGHVKLS DFGLCTGLKK
AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY
NKLCDWWSLG VIMYEMLIGF PPFCSETPQE TYRKVMSWKE TLAFPPEVPV SEKAKDLILR
FCTDSENRIG NGGVEEIKGH PFFEGVDWGH IRERPAAIPI EIRSIDDTSN FDDFPESDIL
QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT QRGSIPTYMK AGKL
