ID H2Z2P4_CIOSA Unreviewed; 401 AA.
AC H2Z2P4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000011856.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000011856.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|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}.
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 AlphaFoldDB; H2Z2P4; -.
DR STRING; 51511.ENSCSAVP00000011856; -.
DR Ensembl; ENSCSAVT00000011994.1; ENSCSAVP00000011856.1; ENSCSAVG00000006956.1.
DR eggNOG; KOG1785; Eukaryota.
DR GeneTree; ENSGT00940000168289; -.
DR HOGENOM; CLU_013535_2_0_1; -.
DR InParanoid; H2Z2P4; -.
DR OMA; RQSWPPR; -.
DR TreeFam; TF314210; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007875; 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; 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:SF11; 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 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:UP000007875};
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 1..308
FT /note="Cbl-PTB"
FT /evidence="ECO:0000259|PROSITE:PS51506"
FT DOMAIN 340..382
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 401 AA; 46927 MW; 2A14D85A1E01CD16 CRC64;
RVTIDKKYIE KSSKLMDKVA KFCQQSKMNL KNSPPYILDI LPDTYNHLRL IMLRYEDRLQ
VLNECEYFRI FLDNLMKKCK EAIKLFREGR ERMFDENSQH RRSLTKLSLV FSHMLAELKA
EFPDGRFIGE EYRITKSEAA NFWRTTFRHK VSAGTIIQWS IFRQELDKVH PISSGLECIA
LKSTIDLVCN NYISNFEFDV FSRLFQPWTN LLKNWNMLAV THPGYMAFLT YDEVKARLHK
YIHKPGSYIF RLSCTRLGQW AVGYVTMGGE ILQTIPQNKS LCQALIDGWK EGFYLFPDGR
QVNPDLSGLL EQSEDDEERI TVSQEQYELY CEMGSTFQLC KICAENNKDV RIEPCGHLIC
KSCLESWQEM DNSTSPTCPW CRCEIKGTET VVIEPYEGDK K
//
