SLK_CAVPO
ID SLK_CAVPO Reviewed; 1231 AA.
AC O55092;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
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;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC STRAIN=Hartley; TISSUE=Liver;
RX PubMed=9143322; DOI=10.1006/abbi.1997.9893;
RA Itoh S., Kameda Y., Yamada E., Tsujikawa K., Mimura T., Kohama Y.;
RT "Molecular cloning and characterization of a novel putative STE20-like
RT kinase in guinea pigs.";
RL Arch. Biochem. Biophys. 340:201-207(1997).
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 -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9143322}.
CC -!- PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:9143322}.
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; D88425; BAA24930.1; -; mRNA.
DR PIR; T18532; T18532.
DR RefSeq; NP_001166491.1; NM_001173020.1.
DR AlphaFoldDB; O55092; -.
DR SMR; O55092; -.
DR STRING; 10141.ENSCPOP00000000892; -.
DR GeneID; 100135621; -.
DR KEGG; cpoc:100135621; -.
DR CTD; 9748; -.
DR eggNOG; KOG0579; Eukaryota.
DR InParanoid; O55092; -.
DR OrthoDB; 851098at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; 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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
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..1231
FT /note="STE20-like serine/threonine-protein kinase"
FT /id="PRO_0000233238"
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 871..906
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 309..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 822..1065
FT /evidence="ECO:0000255"
FT COILED 1105..1179
FT /evidence="ECO:0000255"
FT COMPBIAS 315..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
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 431..432
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 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08815"
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:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
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 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 810
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 1093
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
SQ SEQUENCE 1231 AA; 141082 MW; F5BD2C1850373B01 CRC64;
MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EEFWETIGEL 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 FVTIDSNKPI
RELIAEAKAE VTEEVEDGKE EDDDEEIENS LPIPTNKRAS SDLSIASSEE DKLSQNACIL
ESVSEKTEHN ASGDKFSTKV LNEKPCPGEP ENAVELVGGA VAVLPDRATE LPESGREEKR
PKLDRLPDTE DQEMADINSV SEGEEDHAVT SETNIEHNLK PEKERDQEKQ PVLENKLVKS
EDTTIQTVDL VSQETGEKEV DIHILDSEVV HAVEDTHEKL RKDDTTQKDV ISDTSSVGER
DEEIGAVPKT AESSAEGAQG DGGKETDEGA QILISKATEG PKASGTEEAP PVTEITETND
TDQKLVENTH EKQLPISSET TLDTSEGLGA SEGREVTESG STEEVEVEGA VSETDEEDVQ
SETRGAPMAV TQMDTEKNET PHEAPAQVEV QVPVPPQPSE PPPAPIPSIN INSEAAENKG
EMGASLNTET ILLPESESQK ENDTDSGTGS TADNSSIDLN LSISSFLSKT KDNGSISLQE
TRRQKKTLKK TRKFIVDGVE VSVTTSKIVT DSDSKTEELR FLRRQELREL RFLQKEEQRA
QQQLNGKLQQ QREQIFRRFE QEMMSKKRQY DQEIENLEKQ QKQTIERLEQ EHTNRLRDEA
KRIKGEQEKE LSKFQNILKN RKKEVLNEVE KAPKDLRKEL MKRRKEELAQ SQHVQEQDFV
QKQQQELDGS LKKIIQQQKA ELANIERECL NNKQQLMRAR EAAIWELEER HLQEKHQLLK
QQLKDQYFMQ RHQLLKRHEK ETEQMQRYNQ RLIEELKNRQ TQERARLPKI QRSEAKTRMA
MFKKSLRINS TATPDQDRDK IKQFSAQEEK RQKNERMAQH QKHENQMRDL QLQCEANVRE
LHQLQNEKCH LLVEHETQKL KELDEEHSQE LKEWREKLRP RKKTLEEEFA RKLQEQEVFF
KMTGESECLN PSTQSRISKF YPIPSLHSTG S
