GenomeNet

Database: UniProt
Entry: W6V060_ECHGR
LinkDB: W6V060_ECHGR
Original site: W6V060_ECHGR 
ID   W6V060_ECHGR            Unreviewed;       540 AA.
AC   W6V060;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
GN   ORFNames=EGR_00761 {ECO:0000313|EMBL:EUB64217.1};
OS   Echinococcus granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB64217.1, ECO:0000313|Proteomes:UP000019149};
RN   [1] {ECO:0000313|EMBL:EUB64217.1, ECO:0000313|Proteomes:UP000019149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24013640; DOI=10.1038/ng.2757;
RA   Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA   Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA   Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA   Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT   "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL   Nat. Genet. 45:1168-1175(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:EUB64217.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APAU02000003; EUB64217.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6V060; -.
DR   STRING; 6210.W6V060; -.
DR   EnsemblMetazoa; XM_024490010.1; XP_024355413.1; GeneID_36336476.
DR   OMA; LHRQHEP; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000019149; 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   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR024162; Adaptor_Cbl.
DR   InterPro; IPR014741; Adaptor_Cbl_EF_hand-like.
DR   InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR   InterPro; IPR014742; Adaptor_Cbl_SH2-like.
DR   InterPro; IPR024159; Cbl_PTB.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23007; CBL; 1.
DR   PANTHER; PTHR23007:SF11; E3 UBIQUITIN-PROTEIN LIGASE CBL; 1.
DR   Pfam; PF02761; Cbl_N2; 1.
DR   Pfam; PF02762; Cbl_N3; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF47668; N-terminal domain of cbl (N-cbl); 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS51506; CBL_PTB; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367001};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW   Transferase {ECO:0000256|RuleBase:RU367001};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU367001};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367001};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          109..415
FT                   /note="Cbl-PTB"
FT                   /evidence="ECO:0000259|PROSITE:PS51506"
FT   DOMAIN          438..475
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   540 AA;  61958 MW;  CEC4B0A4886DB6DD CRC64;
     MEKLHHFASS FVIFFNVAKL AAELQKYIMD MHNYMEDVGI TWRPSCQAEA PFVEILMLAL
     PKASDPSEPN PTDLDYLGID CGLTFVIVTG DLNRLLFVCI DRGNHNMELQ NSFFMNAHAI
     TKGTLKMAEA QITSSGLKSR LHRQHEPVKC EKHLKDTIEQ LEQLTKLFLE IQTPSEKSGL
     HTQFIEYWDK FSTSLTKLLK QFESRLSTGS KNFDMETFSK YTFFFYHMAE EIKFLFPSGK
     FATNQVFGRK DAQNWWERNF NPRVAVASAE FLARFRNEFP DVNEDGDALI DTMGFSSLDY
     ISKYDLDIFT RLFGAWPFVT RIWRRLVNHP GYQKYGTFNT TFDVLNRCRT TPGSYTFRIS
     MSRNGYWSIG YVSAEGKITQ VLCFTSPMTD YLCSGKEQGC FKYPKGQACS DDLSDVSNMR
     TKVELYSHPG DAEDLLKCKI CGTNPNDAQL EPCGHFICVH CCRKIQSSAS CYQCNSKILC
     TTPIEIKLEM ANAVVKLIGW HSERALRFRR KIPPVVPNFC YLMEITKDDA TSIQSLENQH
//
DBGET integrated database retrieval system