ID   CBLBA_XENLA             Reviewed;         918 AA.
AC   Q6GQL0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 111.
DE   RecName: Full=E3 ubiquitin-protein ligase CBL-B-A;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13191};
DE   AltName: Full=RING-type E3 ubiquitin transferase CBL-B-A {ECO:0000305};
DE   AltName: Full=SH3-binding protein CBL-B-A;
DE   AltName: Full=Signal transduction protein CBL-B-A;
GN   Name=cblb-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q13191}.
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:0000250|UniProtKB:Q13191};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with several SH3 domain-containing proteins and with
CC       poly-ubiquitinated proteins. {ECO:0000250|UniProtKB:Q13191}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13191}.
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   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250|UniProtKB:Q13191}.
CC   -!- MISCELLANEOUS: This protein has one functional calcium-binding site.
CC       {ECO:0000250}.
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; BC072732; AAH72732.1; -; mRNA.
DR   RefSeq; NP_001085428.1; NM_001091959.1.
DR   AlphaFoldDB; Q6GQL0; -.
DR   SMR; Q6GQL0; -.
DR   DNASU; 443854; -.
DR   GeneID; 443854; -.
DR   KEGG; xla:443854; -.
DR   AGR; Xenbase:XB-GENE-6251733; -.
DR   CTD; 443854; -.
DR   Xenbase; XB-GENE-6251733; cblb.L.
DR   OrthoDB; 7237699at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 443854; Expressed in testis and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:InterPro.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:TreeGrafter.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0050868; P:negative regulation of T cell activation; ISS:UniProtKB.
DR   GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:2000583; P:regulation of platelet-derived growth factor receptor-alpha signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd16708; RING-HC_Cbl; 1.
DR   CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR   FunFam; 1.10.238.10:FF:000022; E3 ubiquitin-protein ligase CBL; 1.
DR   FunFam; 1.20.930.20:FF:000001; E3 ubiquitin-protein ligase CBL; 1.
DR   FunFam; 3.30.40.10:FF:000015; E3 ubiquitin-protein ligase CBL; 1.
DR   FunFam; 3.30.505.10:FF:000154; E3 ubiquitin-protein ligase CBL; 1.
DR   Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
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; IPR003153; Adaptor_Cbl_N_hlx.
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; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23007; CBL; 1.
DR   PANTHER; PTHR23007:SF3; E3 UBIQUITIN-PROTEIN LIGASE CBL-B; 1.
DR   Pfam; PF02262; Cbl_N; 1.
DR   Pfam; PF02761; Cbl_N2; 1.
DR   Pfam; PF02762; Cbl_N3; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 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; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cytoplasm; Immunity; Metal-binding; Reference proteome; Repeat;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..918
FT                   /note="E3 ubiquitin-protein ligase CBL-B-A"
FT                   /id="PRO_0000055863"
FT   DOMAIN          46..354
FT                   /note="Cbl-PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00839"
FT   ZN_FING         384..423
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..178
FT                   /note="4H"
FT   REGION          179..251
FT                   /note="EF-hand-like"
FT   REGION          252..354
FT                   /note="SH2-like"
FT   REGION          355..383
FT                   /note="Linker"
FT   REGION          481..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..576
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..830
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         236
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         238
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         243
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         297
FT                   /ligand="4-O-phospho-L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:62338"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   918 AA;  102831 MW;  5CEB1FDCBCE9D572 CRC64;
     MASGSGSSSS TSSSALSGRL PGSRSANPRK ARILGLFDAI QDAVGPPKQA AADRRTVEKT
     WKLMDKVVRL CQNPKLQLKN SPPYILDILP DTYQHLRLIL SKYDDNQKLA QLSENEYFKI
     YIDSLIKKSK RAMRLFKEGK ERMYEEQSQE RRNLTKLSLI FSHMLAEIKA IFPSGQFQGD
     NFRITKADAA EFWRKFFGER TIVPWKIFRQ CLHEVHQISS GLEAMALKST IDLTCNDYIS
     VFEFDIFTRL FQPWGSILRN WNFLAVTHPG YMAFLTYDEV KARLQKYSLK PGSYIFRLSC
     TRLGQWAIGY VTADGNILQT IPHNKPLFQA LIDGSREGFY LYPDGRSYNP DLTGLCEPTP
     HDHIKVTQEQ YELYCEMGST FQLCKICAEN DKDVKIEPCG HLMCTSCLTS WQESDGQGCP
     FCRCEIKGME PIIVDPFDPR DESRCFSFSD SLCTPMLDFD DDDLREECLI MNRLAALRKM
     NERQNSPVTS PGSSPLSQRR KTPPEPLQIP HLNLPPVPPR LDLIQKGLAR SPCASPTGSP
     KSSPCMVRKQ DKPLPAPPPL LREPPPPPER PPPIPPDSRT CRHLHHADNV PCRDQSTPHE
     AWCTRDLSGG NPASVCRVTH DGSPKLGVPS SSVLNGRHSR MSTEAGFMRH KHHKRRESPL
     ETLRVYNGLS GNEEYDVPPR LSPPTITIHP IVKCPVLVNS VSDKVRNSAE EDDCEYKIPS
     SHPVSSRLPL HCHSIKHFPR LCENGQCLSN GTHNGISEIK KLKPPDQGDV IATSTVPIHF
     PPARTSAREN HPHGSSLTRT PSDYDLLVPH PGEESFDISP PSQPPPPPPA RTCVTEHVMP
     TALGSRPNSD VDLFLPHSDP CPEAPLPPAR RGPGEVKSNR LSQEYDQLPS CPGKGQEKAS
     NTKGELLLPN QNLIMRPT
//