ID A0A1S3LED9_SALSA Unreviewed; 686 AA.
AC A0A1S3LED9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Protein kinase C {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551};
GN Name=LOC106565827 {ECO:0000313|RefSeq:XP_013988869.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013988869.1};
RN [1] {ECO:0000313|RefSeq:XP_013988869.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013988869.1};
RG RefSeq;
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=2.7.11.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569,
CC ECO:0000256|PIRNR:PIRNR000551};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490,
CC ECO:0000256|PIRNR:PIRNR000551}.
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DR RefSeq; XP_013988869.1; XM_014133394.1.
DR AlphaFoldDB; A0A1S3LED9; -.
DR STRING; 8030.ENSSSAP00000114409; -.
DR PaxDb; 8030-ENSSSAP00000114409; -.
DR Ensembl; ENSSSAT00000149512; ENSSSAP00000114414; ENSSSAG00000078795.
DR GeneID; 106565827; -.
DR KEGG; sasa:106565827; -.
DR OMA; CTITCYV; -.
DR OrthoDB; 841660at2759; -.
DR Proteomes; UP000087266; Chromosome ssa12.
DR Bgee; ENSSSAG00000078795; Expressed in pharyngeal gill and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019222; P:regulation of metabolic process; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd20834; C1_nPKC_theta-like_rpt1; 1.
DR CDD; cd20837; C1_nPKC_theta-like_rpt2; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF427; PROTEIN KINASE C DELTA TYPE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF21494; PKC_C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000551};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000551};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000551};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000551};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000551};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 161..211
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 233..283
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 359..613
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 614..685
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 298..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT BINDING 365..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT BINDING 388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 686 AA; 78261 MW; 429D10162DB8ECAE CRC64;
MSPFLRIAFN AFDVGVLPPL TDAPFCAIKM KESLSTERGK TLVQRKPTMY PAWKSTFDAH
IYEGRVLQVV LMKTAEEPLA EATVGVSVLA ERCKKGNGCA EFWVDLQPSG KIQMVVQFFV
EDTDTAAFKS NVKGREEEDG AMTLTRRRGA IKQAKVHFIK NHEFTATFFG QPTFCSVCRE
FVWGFNKQGY KCRQCNAAIH KKCIDKIIGR CTGTAANSRD TMFQKERFKI DMPHRFKIHN
YMSPTFCDHC GSMLWGMVKQ GLKCEDCGMN SHHKCEKKVG NLCGINQKLL AEALNQVSQK
STRRSESSNS ESTDIGIYQD FNKSPGADPS EGYEKLWEGG KGPAPASITP KTRLTIDSFV
FHKVLGKGSF GKVLLAELRG RGQYFAVKAL KKDVVLMDDD VECTMVEKRV LALAWDNPFL
THLYSTFQTR EHLFFVMEYL NGGDLMFHIQ DKGRFDLYRA TFYSAEIIIG LQFLHSKGII
YRDLKLDNVM LDRDGHIKIA DFGMCKENVF GDNRATTFCG TPDYIAPEIL LGQKYTFSVD
WWSFGVLVYE MLIGQSPFQG DDEDELFESI RMDVPHYPRW ITKEAKDLLE KLFERDPSRR
LGVVDNIRSH SFFKTLNWPA LEKRQVDPPF KPKVKGPNDC NNFDREFLSE KPRLSHTDKN
LIDSMDQTAF AGFSFINPKM ERIMDK
//
