ID H0UV67_CAVPO Unreviewed; 1231 AA.
AC H0UV67;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=SLK {ECO:0000313|Ensembl:ENSCPOP00000000891.2};
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 {ECO:0000313|Ensembl:ENSCPOP00000000891.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000000891.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000000891.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
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DR EMBL; AAKN02016502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0UV67; -.
DR Ensembl; ENSCPOT00000000999.3; ENSCPOP00000000891.2; ENSCPOG00000000992.4.
DR VEuPathDB; HostDB:ENSCPOG00000000992; -.
DR GeneTree; ENSGT00940000156184; -.
DR InParanoid; H0UV67; -.
DR OMA; HEAYFIE; -.
DR OrthoDB; 2880940at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000000992; Expressed in uterine cervix and 12 other cell types or tissues.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IEA:Ensembl.
DR CDD; cd06643; STKc_SLK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR46538:SF1; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 871..906
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
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 823..894
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 937..1002
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1031..1065
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1106..1177
FT /evidence="ECO:0000256|SAM:Coils"
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 BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1231 AA; 141094 MW; 2A755AFF19024237 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 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
//