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Database: UniProt
Entry: A0A1U7RFW3_MESAU
LinkDB: A0A1U7RFW3_MESAU
Original site: A0A1U7RFW3_MESAU 
ID   A0A1U7RFW3_MESAU        Unreviewed;       494 AA.
AC   A0A1U7RFW3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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|RefSeq:XP_005086382.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005086382.1};
RN   [1] {ECO:0000313|RefSeq:XP_005086382.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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|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   RefSeq; XP_005086382.1; XM_005086325.3.
DR   AlphaFoldDB; A0A1U7RFW3; -.
DR   STRING; 10036.ENSMAUP00000022828; -.
DR   GeneID; 101840606; -.
DR   KEGG; maua:101840606; -.
DR   CTD; 23624; -.
DR   eggNOG; KOG1785; Eukaryota.
DR   OrthoDB; 1123734at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000189706; Unplaced.
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; 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:SF12; E3 UBIQUITIN-PROTEIN LIGASE CBL-C; 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   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:UP000189706};
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          7..320
FT                   /note="Cbl-PTB"
FT                   /evidence="ECO:0000259|PROSITE:PS51506"
FT   DOMAIN          350..389
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          411..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  55549 MW;  25CE9577AE8C6BBC CRC64;
     MAAAASPRGR QWGEPRALGR AVKLLQRLEE QCRDPRLAMG PPSLRHLLPR TAQLIREVAK
     ARREAPGGPE GPGGAADFLV VYLANLEAKG RKVAELLPPR GRKDANEEVF REGSRFRRQL
     AKLALIFSHM HAELNALFPG GKYCGHLYQL SKAAAHSFWR ERCGVRCVLP WAEFQSLLCA
     CHPVDPGPTL QALRSTMDLT CNGHVSVFEF DIFTRLFQPW PTLLRNWQLL AVNHPGYMAF
     LTYDEVQTRL QACRDKPGSY IFRPSCTRLG QWAIGYVSPD GSILQTIPLN KPLFQVLLKG
     QRDGIYLYPD GKNHNPDLTE LCQAEPYQRI EVSEEQLQLY EAINSTFELC KICAERDKDV
     RLEPCGHLLC SRCLATWQQS DGQTCPFCRR QIEGFQAVSI CQAQERSAEV RATAEDSGEH
     CHQKTARREL EPVTPSGPPL PPEDPSPRRP QDKGWLSVAP ITMPRLRAPL PLPKMASVLW
     EVTDRPQARQ GATE
//
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