ID   A9JRD3_DANRE            Unreviewed;       499 AA.
AC   A9JRD3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
GN   Name=cblc {ECO:0000313|ZFIN:ZDB-GENE-080220-20};
GN   ORFNames=zgc:172162 {ECO:0000313|EMBL:AAI55617.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI55617.1};
RN   [1] {ECO:0000313|EMBL:AAI55617.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:AAI55617.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2007) 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: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}.
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DR   EMBL; BC155616; AAI55617.1; -; mRNA.
DR   RefSeq; NP_001121724.2; NM_001128252.1.
DR   AlphaFoldDB; A9JRD3; -.
DR   GeneID; 565383; -.
DR   KEGG; dre:565383; -.
DR   AGR; ZFIN:ZDB-GENE-080220-20; -.
DR   ZFIN; ZDB-GENE-080220-20; cblc.
DR   OrthoDB; 1123734at2759; -.
DR   PhylomeDB; A9JRD3; -.
DR   TreeFam; TF314210; -.
DR   UniPathway; UPA00143; -.
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:UniProtKB-UniRule.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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   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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23007; CBL; 1.
DR   PANTHER; PTHR23007:SF13; 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   Pfam; PF13920; zf-C3HC4_3; 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 {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367001};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367001};
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          23..330
FT                   /note="Cbl-PTB"
FT                   /evidence="ECO:0000259|PROSITE:PS51506"
FT   DOMAIN          360..399
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..440
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..481
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  57763 MW;  BA33A6D7BCC5FC7D CRC64;
     MARRPGTAGR SQISDTSETP SQPPTSADRK LLEKVLKRLD KLHKLSVDPR LALKNSPPYL
     PELLSETAIH LTEVWAPYRG SAMAVPRWDE GDYMRIHIRH LLDKTDRAVL LFKEGKEKMF
     EETSNYRRNL TKLSLLFSHM LNELRTIFPG GRFQGDTYRV TKTEAKEFWR KTFGHKCIVQ
     WNVFKQQLKR VHYFEEGMEA MALKSTVDLT CNDHISIFEF DIFTRLFQPW STLIRNWNHL
     AVTHPGYMAF LTYDQVKARL EHYRHRPGSY IFRLSCTQMG QWAIGHVTSD GSIVQTIPQN
     TPLYQALIQG FREGCYLYPD GRDVNPDLSS LCSPVHKGRV KVTEEQYELY CEIGSTFQLC
     KICTERDKDT RIQPCGHLLC QPCLTGWQKS DGHTCPYCRC DIRGTESILI EPYLPIRDKR
     AEEEEEDDED DDDDEEEDHE DIELVMKKLA CMKKISQEEY QIPRSSLSPP PLPPKRNSSS
     PCPSPKPQTH RSFSLGAQK
//