ID A0A1S3L396_SALSA Unreviewed; 481 AA.
AC A0A1S3L396;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Protein kinase C beta type-like {ECO:0000313|RefSeq:XP_013985431.1};
GN Name=LOC106563994 {ECO:0000313|RefSeq:XP_013985431.1};
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_013985431.1};
RN [1] {ECO:0000313|RefSeq:XP_013985431.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_013985431.1; XM_014129956.1.
DR AlphaFoldDB; A0A1S3L396; -.
DR STRING; 8030.ENSSSAP00000015820; -.
DR KEGG; sasa:106563994; -.
DR Proteomes; UP000087266; Chromosome ssa12.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20833; C1_cPKC_rpt1; 1.
DR CDD; cd20836; C1_cPKC_rpt2; 1.
DR CDD; cd04026; C2_PKC_alpha_gamma; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR PANTHER; PTHR45729:SF10; PROTEIN KINASE C; 1.
DR PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 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; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|RefSeq:XP_013985431.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000313|RefSeq:XP_013985431.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 132..182
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 196..246
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 253..370
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 436..481
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 481
FT /evidence="ECO:0000313|RefSeq:XP_013985431.1"
SQ SEQUENCE 481 AA; 53823 MW; 0CACDC6EE18281BF CRC64;
MRRSAHTPAA RRHSCSSAAQ SPSEQGSRAH GESGTRQCEA WQESGHSHRA NTGGKPTPTE
EEGREAPAEK APTLSFLLIS KHFRVKMADR EQGSSDGESS STGGSERRES GAARGFARQG
ALRQKNVHEV KDHKFIARFF KQPTFCSHCT DFIWGFGKQG FQCQVCCFVV HKRCHEFVTF
SCPGADKNAS DDPRSKHKFK VHTYSSPTFC DHCGSLLYGL IHQGMKCDHC MMNIHKRCVS
NVPSLCGTDH TERRGRIQIT ADIKDNKLTV YIQEACNLVP MDPNGLSDPY VKLKLIPDPK
SDTKQKTKTI KCNLNPTWNE TFTFPLKDSD KDRRLSVEIW DWDLTSRNDF MGALSFGVSE
LQKQGVDGWF KLLSQEEGEY FNVPVQPDGE DGNEELRQKF ERAKIGPGKN TDGSSSNSTS
KYDSNGNQDR VKLTDFNFIM VLGKGSFGKV MLAERKGADE LYAVKILKKD VVIQDDDVEC
T
//
