ID   CBL_MLVCN               Reviewed;         390 AA.
AC   P23092;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   22-FEB-2023, entry version 101.
DE   RecName: Full=Transforming protein cbl;
GN   Name=V-CBL;
OS   Cas-NS-1 murine leukemia virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Murine leukemia virus.
OX   NCBI_TaxID=11793;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2784003; DOI=10.1073/pnas.86.4.1168;
RA   Langdon W.Y., Hartley J.W., Klinken S.P., Ruscetti S.K., Morse H.C. III;
RT   "v-cbl, an oncogene from a dual-recombinant murine retrovirus that induces
RT   early B-lineage lymphomas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1168-1172(1989).
CC   -!- FUNCTION: Induces early B-lineage lymphomas.
CC   -!- DOMAIN: Is composed of the phosphotyrosine binding (PTB) domain, a
CC       short linker region and the RING-type zinc finger. The PTB domain,
CC       which is also called TKB (tyrosine kinase binding) domain, is composed
CC       of three different subdomains: a four-helix bundle (4H), a calcium-
CC       binding EF hand and a divergent SH2 domain (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Cbl polyprotein.
CC   -!- MISCELLANEOUS: This protein has one functional calcium-binding site.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; J04169; AAA42885.1; ALT_INIT; Genomic_DNA.
DR   SMR; P23092; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:InterPro.
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: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; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 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   PANTHER; PTHR23007; CBL; 1.
DR   PANTHER; PTHR23007:SF5; E3 UBIQUITIN-PROTEIN LIGASE CBL; 1.
DR   Pfam; PF02262; Cbl_N; 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; SSF55550; SH2 domain; 1.
DR   PROSITE; PS51506; CBL_PTB; 1.
PE   3: Inferred from homology;
KW   Calcium; Metal-binding; Oncogene; Repeat.
FT   CHAIN           1..390
FT                   /note="Transforming protein cbl"
FT                   /id="PRO_0000055868"
FT   DOMAIN          77..381
FT                   /note="Cbl-PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00839"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..205
FT                   /note="4H"
FT   REGION          206..278
FT                   /note="EF-hand-like"
FT   REGION          279..381
FT                   /note="SH2-like"
FT   BINDING         259
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         261
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         263
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         265
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         270
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22681"
FT   BINDING         324
FT                   /ligand="4-O-phospho-L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:62338"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  43692 MW;  EB72483746827AB0 CRC64;
     ASAGGGCRRG PSFSPGSIPS LAAERAPDPP LAMAGNVKKS SGAGGGGSGG SGAGGLIGLM
     KDAFQPHHHH HHLSPHPPCT VDKKMVEKCW KLMDKVVRLC QNPNVALKNS PPYILDLLPD
     TYQHLRTVLS RYEGKMETLG ENEYFRVFME NLMKKTKQTI SLFKEGKERM YEENSQPRRN
     LTKLSLIFSH MLAELKGIFP SGLFQGDTFR ITKADAAEFW RKAFGEKTIV PWKSFRQALH
     EVHPISSGLE AMALKSTIDL TCNDYISVFE FDIFTRLFQP WSSLLRNWNS LAVTHPGYMA
     FLTYDEVKAR LQKFIHKPGS YIFRLSCTRL GQWAIGYVTA DGNILQTIPH NKPLFQALID
     GFREGFYLFP DGRNQNPDLT GLCEPTPHFS
//