ID V8NBW1_OPHHA Unreviewed; 370 AA.
AC V8NBW1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
DE Flags: Fragment;
GN Name=V-CBL {ECO:0000313|EMBL:ETE59565.1};
GN ORFNames=L345_14700 {ECO:0000313|EMBL:ETE59565.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE59565.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE59565.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE59565.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC specific E2 ubiquitin-conjugating enzymes, and transfers it to
CC substrates, generally promoting their degradation by the proteasome.
CC {ECO:0000256|RuleBase:RU367001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU367001};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU367001}.
CC -!- DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB)
CC domain, a short linker region and the RING-type zinc finger. The PTB
CC domain, which is also called TKB (tyrosine kinase binding) domain, is
CC composed of three different subdomains: a four-helix bundle (4H), a
CC calcium-binding EF hand and a divergent SH2 domain.
CC {ECO:0000256|RuleBase:RU367001}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE59565.1}.
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DR EMBL; AZIM01005479; ETE59565.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NBW1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR024162; Adaptor_Cbl.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR003153; Adaptor_Cbl_N_hlx.
DR InterPro; IPR014742; Adaptor_Cbl_SH2-like.
DR InterPro; IPR024159; Cbl_PTB.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR23007; CBL; 1.
DR PANTHER; PTHR23007:SF13; E3 UBIQUITIN-PROTEIN LIGASE CBL; 1.
DR Pfam; PF02262; Cbl_N; 1.
DR Pfam; PF02762; Cbl_N3; 1.
DR SUPFAM; SSF47668; N-terminal domain of cbl (N-cbl); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51506; CBL_PTB; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|RuleBase:RU367001};
KW Metal-binding {ECO:0000256|RuleBase:RU367001};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Transferase {ECO:0000256|RuleBase:RU367001};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367001};
KW Zinc {ECO:0000256|RuleBase:RU367001};
KW Zinc-finger {ECO:0000256|RuleBase:RU367001}.
FT DOMAIN 9..289
FT /note="Cbl-PTB"
FT /evidence="ECO:0000259|PROSITE:PS51506"
FT REGION 338..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE59565.1"
SQ SEQUENCE 370 AA; 41811 MW; 598780F1766B9DF8 CRC64;
MAMAPGPAWM PRRTGAHRSL EKTLQGLTKL QQLACQPQVA LRNSAPHLPS LLPLIYQHLK
LIREHYGAGL AEVWESDFFR IFLLNLLEKI KQATQLFKRG KDKEEILLEG SAASHMLAEL
QAVFPNGEDQ GSTYQLSKQE AQVFWRGTWR ERFFLAKSCW LCNVNLMAFS TICFASPSNS
FPVFSSQPWP TLLKNWTYLA VTHPGYMAFL TYDEVKARLQ AYVNKPGSYI FRLSCTRLGQ
WAIGYVTADR NILQTIPQKK SLFQALVDGH KEGLNSLSST ARWNPPSSFA KSAPRTTRMF
KSVRAGIFSA GNALSHGSFQ NLPPAPFVAR RSGAMKMWRS AHTAPRRAAP PPRTRATRGT
WRMWTWCCNS
//
