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Database: UniProt
Entry: I3LU37_PIG
LinkDB: I3LU37_PIG
Original site: I3LU37_PIG 
ID   I3LU37_PIG              Unreviewed;      1442 AA.
AC   I3LU37;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 73.
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=DAPK1 {ECO:0000313|Ensembl:ENSSSCP00000027636.2};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000027636.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000027636.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000027636.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000027636.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   SMR; I3LU37; -.
DR   STRING; 9823.ENSSSCP00000027636; -.
DR   Ensembl; ENSSSCT00000026142.4; ENSSSCP00000027636.2; ENSSSCG00000010949.5.
DR   GeneTree; ENSGT00940000153424; -.
DR   HOGENOM; CLU_1264189_0_0_1; -.
DR   InParanoid; I3LU37; -.
DR   OrthoDB; 4580305at2759; -.
DR   TreeFam; TF314166; -.
DR   Proteomes; UP000008227; Chromosome 10.
DR   Bgee; ENSSSCG00000010949; Expressed in endocardial endothelium and 45 other cell types or tissues.
DR   ExpressionAtlas; I3LU37; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:1990722; C:DAPK1-calmodulin complex; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR   GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
DR   GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR   GO; GO:0002357; P:defense response to tumor cell; IEA:Ensembl.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:1904094; P:positive regulation of autophagic cell death; IEA:Ensembl.
DR   GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR   GO; GO:0002834; P:regulation of response to tumor cell; IEA:Ensembl.
DR   CDD; cd08782; Death_DAPK1; 1.
DR   CDD; cd14194; STKc_DAPK1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 1.20.5.460; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR020676; DAPK1_cat.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24342:SF17; DEATH-ASSOCIATED PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 7.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          378..410
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          444..476
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          477..509
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          510..542
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          543..575
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          576..608
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          609..641
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          681..955
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1312..1396
FT                   /note="Death"
FT                   /evidence="ECO:0000259|PROSITE:PS50017"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1442 AA;  161467 MW;  9700B68A5225A17C CRC64;
     MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK SSRRGVSRED
     IEREVGILKE IQHPNVITLH EVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL
     KQILNGVYYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT
     PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYEFEEEY
     FSNTSALAKD FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA
     ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL
     QHLLGSLSNY DVNQPNKHGT PPLLIAAGCG NIQILQLLIK RGSRIDIQDK GGSNAIYWAS
     RHGHVDTLKF LNENKCPLDV KDKSGETALH VAARYGHADV VQLLCSFGSN PNFQDKEEET
     PLHCAAWHGY YAVAKALCEA GCNVNIKNRE GETPLLTASA RGYHDIVECL SEHGADLNAT
     DKDGHIALHL AVRRCQMEVI QRLISQGCCV DFQDRHGNTP LHVACKDGNV PIVVALCEAN
     CNVDLPNKYG RTPLHLAANN GILDVVRYLC LSGANVEALT LDGKTAEDLA KSEQHEHVAG
     LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK TTLVESLKCG LLRSFFRRRR
     PRLSSTNSTR FPPSPLASKP AVSVSINNLY PGCENVSVRS RSMMFEPGLT KGMLEVFGAP
     AHHPHCSADD QSTKAIDIQN AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHVIVF
     SLEEPYEIQL NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL RVVLVATHAD IMNVPRPAGG
     EFGYDKDISL LKEIRNRFGN DLHISNKLFV LDAGASGSKD MKVLRNHLQE IRSQIVSVCP
     PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN PLASEADLRH IAQQLHSTGE
     INIMQSETVQ DVLLLDPRWL CTNVLGKLLS VETPRALHHY RGRYTMEDVQ RLVPDSDVEE
     LLQILDAMDI CARDLSSGTM VDIPALIKTD NLHRSWTDEE DEVRVYGGVR IVPVEHLTPF
     PCGIFHKVQV NLCRWIHQQS AEGDADIRLW VNGCKIANRG AELLVLLVNH GQGIEVQVRG
     LETEKIKCCL LLDSVCSTIE NVMATTLPGL LTVKHYLSPQ QLREHHEPVM IYQPRDFFRA
     QTLKETSLTN TMGGYKESFS SIMCFGCHDV YVQASLGMDI HASDLNLLTR RKLSRLLDPP
     DPMGKDWCLL AMNLGLPDLV AKYNTNNGAP KEFLPSPVHA LLREWTSYPN STVGVLMSKL
     RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR KNSHVRNPLY
     DL
//
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