SLK_RAT
ID SLK_RAT Reviewed; 1206 AA.
AC O08815;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=STE20-like serine/threonine-protein kinase;
DE Short=STE20-like kinase;
DE EC=2.7.11.1;
DE AltName: Full=STE20-related serine/threonine-protein kinase;
DE Short=STE20-related kinase;
GN Name=Slk; Synonyms=Sk2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Fukami Y., Yamamoto H., Ichihara T., Mori K., Gomi T., Sato K.;
RT "SK2, a putative rat homologue of yeast protein kinase NRK1.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 156-214.
RX PubMed=2062320; DOI=10.1016/0161-5890(91)90153-b;
RA Yue C.C.;
RT "Novel putative protein kinase clones from a rat large granular lymphocyte
RT tumor cell line.";
RL Mol. Immunol. 28:399-408(1991).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; SER-347; SER-348;
RP SER-645; SER-649 AND SER-778, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Mediates apoptosis and actin stress fiber dissolution.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}.
CC -!- PTM: Autophosphorylated.
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; AB003357; BAA20077.1; -; mRNA.
DR PIR; PT0204; PT0204.
DR PIR; T34021; T34021.
DR RefSeq; NP_062222.2; NM_019349.2.
DR AlphaFoldDB; O08815; -.
DR SMR; O08815; -.
DR IntAct; O08815; 1.
DR STRING; 10116.ENSRNOP00000015496; -.
DR iPTMnet; O08815; -.
DR PhosphoSitePlus; O08815; -.
DR jPOST; O08815; -.
DR PaxDb; O08815; -.
DR PRIDE; O08815; -.
DR GeneID; 54308; -.
DR KEGG; rno:54308; -.
DR UCSC; RGD:3780; rat.
DR CTD; 9748; -.
DR RGD; 3780; Slk.
DR eggNOG; KOG0579; Eukaryota.
DR InParanoid; O08815; -.
DR OrthoDB; 851098at2759; -.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:O08815; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; IMP:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001943; UVR_dom.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
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; PS50151; UVR; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Coiled coil; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1206
FT /note="STE20-like serine/threonine-protein kinase"
FT /id="PRO_0000233241"
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 874..909
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 308..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 468..492
FT /evidence="ECO:0000255"
FT COILED 825..1037
FT /evidence="ECO:0000255"
FT COILED 1077..1151
FT /evidence="ECO:0000255"
FT COMPBIAS 315..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 438..439
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 813
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 1065
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT CONFLICT 165
FT /note="L -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1206 AA; 137888 MW; 8F5C6A19A3501FB9 CRC64;
MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EEFWEIIGEL GDGAFGKVYK AQNKETNVLA
AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM
LELERPLTES QIQVVCKQTL EALNYLHDNK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN
TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP
MRVLLKIAKS EPPTLAQPSR WSSNFKDFLK KCLEKNVDAR WTTSQLLQHP FVTVDSNKPV
RELIAEAKAE VTEEVEDGKE EDDDDETESA LPIPANKRAS SDLSIASSEE DKLSQNACIL
ESVSERTEHN TSGDKFSNKV LSEKPTPEGP EKTVDVDGPA NDVNLETVAE PNDQAVGFHE
NGREKKRPQL ESQPDTEDQQ TVDVNLVGEG NDSNIVILET NTDCLKPEED RNEENQEIIE
NKLTQSEEIK DIHIQTMDLV SQETGEKEAD FQAIDNEVGF TKEETQEKLG KDDKTHKVVI
SDITSEVGTD EPPGDTQKSA EQSQDAEGGA GEEAPEPAQT LTEKATEGPE AHGAEEEPRS
GERVEDKQLE QQSAVCEGEG QVTSTSESTR ATTEEPETDE VDQVSESNSI EELERLGVTG
AEEQALGSKG EAATELDLER EENAQELPVK AEPQAPAASQ ASEPPPVLIP SINIHSENTE
NKGEMGALPK PETILPPEPE NGKGNDTDSG TGSTVENSSS DLNLSISSFL SKTKDSGSVS
LQETRRQKKT LKKTRKFIVD GVEVSVTTSK IVTDSDSKTE ELRFLRRQEL RELRLLQKEE
QKAQQQLNGK LQQQREQIFR RFEQEMLSKK RQYDQEIENL EKQQKQTIER LEQEHTNRLR
DEAKRIKGEQ EKELSKFQNM LRNRKKEEQE FVQKQQQELD GALKKIIQQQ KAELANIERE
CLNNKQQLLR AREAAIWELE ERHLQEKHQL LKQQLKDQYF IQRHQLLKRH EKETEQMQRY
NQRLIEELKN RQTQERARLP KIQRSEAKTR MAMFKKSLRI NSTATPDQDR EKIKQFAAQE
EKRQKNERMA QHQKHESQMR DLQLQCEANV RELHQLQNEK CHLLVEHETQ KLKELDEEHS
QELKEWREKL RPRKKTLEEE FARKLQEQEV FFKMTGESEC LNPSAQSRGC LQTSHPSSTR
APAWAG
