ID A0A2D0PJB2_ICTPU Unreviewed; 633 AA.
AC A0A2D0PJB2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RAF proto-oncogene serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00040839};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Raf-1 {ECO:0000256|ARBA:ARBA00042977};
GN Name=raf1b {ECO:0000313|RefSeq:XP_017306072.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017306072.1};
RN [1] {ECO:0000313|RefSeq:XP_017306072.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017306072.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000256|ARBA:ARBA00010507}.
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DR RefSeq; XP_017306072.1; XM_017450583.3.
DR AlphaFoldDB; A0A2D0PJB2; -.
DR GeneID; 108255012; -.
DR CTD; 557109; -.
DR OrthoDB; 4560496at2759; -.
DR Proteomes; UP000221080; Chromosome 21.
DR GO; GO:0005886; C:plasma membrane; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20870; C1_A_C-Raf; 1.
DR CDD; cd17135; RBD_CRAF; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_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; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23257:SF763; RAF PROTO-ONCOGENE SERINE_THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02196; RBD; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-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; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_017306072.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 73..149
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 156..202
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 335..595
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 239..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 633 AA; 71575 MW; D587319ABD036963 CRC64;
MISLTRRLNR LLRLSPSSLM EHIQGTWKTL SNGFGFRDSV FEDSSMTPTI TKSFPYRRRS
SDDEKITNTS KANTIRVYLP NQQRTVVNVR PGMTLHSCLI KALKVRGLQP ECCAVFRLHP
EQPRSKKSRM DWNTDSTSLI GEELLVEVLD HVPLTTHNFV RKTFLKLAFC DICQKFLLHG
FRCQTCGYKF HEHCSTKVPT MCVDWSNIRQ LLLFPTPGES GTPSLPPLSS RRMRDSLSRL
PASGSLSQKQ RSTSTPNVHM VSSSLPGGGA SCEDASKNQD SGRHPNLSPT GWSQPKTPGP
VHREKASSNT QDKNRIRPRE KRDSCYYWEI DASEVVLHSC IGSGSFGTVF KGKWHGDVAV
KILKVKDPTP EQFQAFRNEV AVLRKTRHVN ILLFMGYMTK DNLAIVTQWC EGSSLYKHLH
VQDTKLQLFQ LIDIARQTAQ GMDYLHAKNI IHRDMKSNNI FLHEGLTVKI GDFGLATVKT
RWSGSQQVEQ PSGSILWMAP EVIRMQDSNP YSFQSDVYAY GIVLYELMTG ELPYSMVANR
DQIIFMVGRG YLSPDLSKLY KSCPKAMKRL VADCIKKSKD DRPLFPQILA SIELLQHSLP
KINRSASEPS LHRAAHTDDI SICTLTSTRL PVF
//
