SNRK_RAT
ID SNRK_RAT Reviewed; 746 AA.
AC Q63553;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=SNF-related serine/threonine-protein kinase;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase;
GN Name=Snrk {ECO:0000312|RGD:69653};
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:CAA61563.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAA61563.1};
RC TISSUE=Ependymocyte {ECO:0000312|EMBL:CAA61563.1};
RX PubMed=8654423; DOI=10.1111/j.1432-1033.1996.00736.x;
RA Becker W., Heukelbach J., Kentrup H., Joost H.G.;
RT "Molecular cloning and characterization of a novel mammalian protein kinase
RT harboring a homology domain that defines a subfamily of serine/threonine
RT kinases.";
RL Eur. J. Biochem. 235:736-743(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10930554; DOI=10.1016/s0006-8993(00)02548-8;
RA Yoshida K., Yamada M., Nishio C., Konishi A., Hatanaka H.;
RT "SNRK, a member of the SNF1 family, is related to low K(+)-induced
RT apoptosis of cultured rat cerebellar granule neurons.";
RL Brain Res. 873:274-282(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-495 AND SER-518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role in hematopoietic cell proliferation or
CC differentiation. Potential mediator of neuronal apoptosis.
CC {ECO:0000250|UniProtKB:Q9NRH2, ECO:0000269|PubMed:10930554,
CC ECO:0000269|PubMed:8654423}.
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 Evidence={ECO:0000269|PubMed:8654423};
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; Evidence={ECO:0000269|PubMed:8654423};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8654423};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-173.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10930554}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined with
CC highest levels in the brain and testis. Strongly expressed in the
CC pyramidal and granule neurons of the hippocampus and also in the
CC cerebellum. {ECO:0000269|PubMed:10930554, ECO:0000269|PubMed:8654423}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed in the cerebellum by E20, levels
CC increase until 28 days after birth. {ECO:0000269|PubMed:10930554}.
CC -!- PTM: Autophosphorylated. Phosphorylation on Thr-173 by STK11/LKB1 in
CC complex with STE20-related adapter-alpha (STRADA) pseudo kinase and
CC CAB39 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; X89383; CAA61563.1; -; mRNA.
DR PIR; S62365; S62365.
DR RefSeq; NP_620188.1; NM_138833.1.
DR RefSeq; XP_006244119.1; XM_006244057.3.
DR RefSeq; XP_006244120.1; XM_006244058.3.
DR RefSeq; XP_006244121.1; XM_006244059.1.
DR RefSeq; XP_006244122.1; XM_006244060.3.
DR RefSeq; XP_006244123.1; XM_006244061.2.
DR RefSeq; XP_006244124.1; XM_006244062.2.
DR RefSeq; XP_017450914.1; XM_017595425.1.
DR RefSeq; XP_017450915.1; XM_017595426.1.
DR AlphaFoldDB; Q63553; -.
DR SMR; Q63553; -.
DR STRING; 10116.ENSRNOP00000005422; -.
DR iPTMnet; Q63553; -.
DR PhosphoSitePlus; Q63553; -.
DR jPOST; Q63553; -.
DR PaxDb; Q63553; -.
DR PRIDE; Q63553; -.
DR Ensembl; ENSRNOT00000079273; ENSRNOP00000071648; ENSRNOG00000004050.
DR GeneID; 170837; -.
DR KEGG; rno:170837; -.
DR UCSC; RGD:69653; rat.
DR CTD; 54861; -.
DR RGD; 69653; Snrk.
DR eggNOG; KOG4717; Eukaryota.
DR GeneTree; ENSGT00940000155365; -.
DR InParanoid; Q63553; -.
DR OMA; VGSIKFF; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q63553; -.
DR PRO; PR:Q63553; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000004050; Expressed in cerebellum and 18 other tissues.
DR Genevisible; Q63553; RN.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; TAS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..746
FT /note="SNF-related serine/threonine-protein kinase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000225607"
FT DOMAIN 16..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 291..334
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 383..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P57059,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P57059,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P57059,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDU5"
FT MOD_RES 173
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRH2"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRH2"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDU5"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 534
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDU5"
SQ SEQUENCE 746 AA; 81627 MW; 57F6A8FC2704BBEC CRC64;
MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT KLDTLATGHL
FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM FDYIMKHEEG LNEDLAKKYF
AQIVHAISYC HKLHVVHRDL KPENVVFFEK QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY
SAPEILLGDE YDAPAVDIWS LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPPRVSA
GCRDLITRML QRDPKRRASL EEIESHPWLQ GVDPSPATKY NIPLVSYKNL SEEEHNSIIQ
RMVLGDIADR DAIVEALETN RYNHITATYF LLAERILREK QEKEIQTRSA SPSNIKAQFR
QSWPTKIDVP QDLEDDLTAT PLSHATVPQS PARAGDSVLN GHRSKGLCDP AKKDELPELA
GPALSTVPPA SLKPAASGRK CLFRVEEDEE EDEEDKKPVS LSTQVVLRRK PSVTNRLTSR
KSAPVLNQIF EEGESDDEFD MDENLPPKLS RLKMNIASPG TVHKRYHRRK SQGRGSSCSS
SETSDDDSES RRRLDKDSGL AYSWHRRDSS EGPPGSEGDG GGQSKPSGGG GVDKASPGEQ
GTGGSGQGGS GGTPSGTAGS SRRCAGPDSS SSSPASAAPR GAELVQSLKL VSLCLGSQLH
GAKYILDPQK ALLSSVKVQE RSTWKMCISA PGPGPSADLD PVRTKKLRNN VLQLPLCEKT
ISVNIQRSRK EGLLCASSPA SCCHVI
