ID A0A087VIL4_BALRE Unreviewed; 854 AA.
AC A0A087VIL4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=N312_07156 {ECO:0000313|EMBL:KFO12456.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO12456.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO12456.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO12456.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367001};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, 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; KL494796; KFO12456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087VIL4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053309; 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; cd16708; RING-HC_Cbl; 1.
DR CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR CDD; cd14393; UBA_c-Cbl; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-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; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_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: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 Pfam; PF00627; UBA; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00165; UBA; 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 SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51506; CBL_PTB; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00518; ZF_RING_1; 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:UP000053309};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU367001};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW 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 1..286
FT /note="Cbl-PTB"
FT /evidence="ECO:0000259|PROSITE:PS51506"
FT DOMAIN 316..355
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 804..843
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 365..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO12456.1"
FT NON_TER 854
FT /evidence="ECO:0000313|EMBL:KFO12456.1"
SQ SEQUENCE 854 AA; 94242 MW; AD48CB3A4FA5DBD5 CRC64;
VVRLCQNPKL ALKNSPPYIL DLLPDTYQHL RTILSRYEGK METLGENEYF RVFMENLMKK
TKQTISLFKE GKERMYEENS QPRRNLTKLS LIFSHMLAEL KGIFPSGLFQ GDTFRITKAD
AAEFWRKAFG EKTIVPWKSF RQALHEVHPI SSGLEAMALK STIDLTCNDY ISVFEFDIFT
RLFQPWSSLL RNWNSLAVTH PGYMAFLTYD EVKARLQKFI HKPGSYIFRL SCTRLGQWAI
GYVTADGNIL QTIPHNKPLF QALIDGFREG FYLFPDGRNQ NPDLTGLCEP TPQDHIKVTQ
EQYELYCEMG STFQLCKICA ENDKDVKIEP CGHLMCTSCL TAWQESEGQG CPFCRCEIKG
TEPIVVDPFD PRGGGGLSRQ GAEGTPSPNY DDDDDDRADD SLFMMKELAG TKVERPPSPF
SVAPQATLPP VPPRLDLLQQ RVSNPPGASS PGTTSKAAPG TLHKDKPLPI PPTLRDLPPP
PPPDRPHSIG AEGRPQRRPL PCTPGDCPSR DKPPPVPSNR QADLWPSRPI PKAPSVALSP
GDPWAGRELS NRHSLPFSLP SQMDSRADSH RLGSTLSLDN PMSLNSGPTT TSECEHSKIK
PSSSANAIYS LAARPLPVPK LPPGEQSESD EDTEYMSPSS LPVVPPGPAV QNPEIKMPLE
MTQSLRVLDR DQQTDGCMYE AMYNIHSQAA SSAFEIVNTS DEGDLAAATA SNGPEESENE
EDGYDIPKPP LPVAIARRTL SDISNATPAF SRMSLENDPV TGFSDGSQVP ERPPKPLPRR
INSERKAGSC QTGGASSGTS ASLQLSSEIE NLMSQGYSYQ DIQKALVIAH NNIEMAKNIL
REFVSISSPA HVAT
//
