ID W5MAZ4_LEPOC Unreviewed; 787 AA.
AC W5MAZ4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005553.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005553.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR EMBL; AHAT01013452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01013453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MAZ4; -.
DR STRING; 7918.ENSLOCP00000005553; -.
DR Ensembl; ENSLOCT00000005561.1; ENSLOCP00000005553.1; ENSLOCG00000004637.1.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000158690; -.
DR InParanoid; W5MAZ4; -.
DR OMA; QWDRPRH; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000018468; Linkage group LG13.
DR Bgee; ENSLOCG00000004637; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd08382; C2_Smurf-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF293; E3 UBIQUITIN-PROTEIN LIGASE SMURF1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 2.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 4.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..120
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 276..309
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 322..355
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 450..787
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 230..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 787 AA; 89954 MW; 8AF4CD9E73ED2486 CRC64;
MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKV VVDGSGQCHS TDTVKSTLDP
KWNQHYDLYI GKTDSITISV WNHKKIHKKQ GAGFLGCVRL LSNAISRLKD TGYQRLDLCK
LNPTDSDTVR GQIVVSLQTR DRIGSGGPVV DCRGLLENEG TPHICWHNNY IYITGYTHSR
ISISHQQVHM NMSCIKILTD FPRPVYEDSG PGRPLSCFME EPLPYTDSTG AAGGGSCRFL
ESPSQEQRLQ AQRIRNQEPR GHAHTPQNRP HGHQSPELPE GYEQRTTVQG QVYFLHTQTG
VSTWHDPRIP RDLNSVSCED LGPLPPGWEV RSTVSGRIYF VDHNNRTTQF TDPRLHHIMR
LIFDAQLSAS IFSYQSQVKE SSQTLPTQTE VSVEEGEGEV PVRYERDLVQ KLKVLRHELS
LQQPQAGHCR IEVSREEIFE ESYRQIMKMR PKDLKKRLMV KFRGEEGLDY GGVAREWLYL
LCHEMLNPYY GLFQYSTDNI YTLQINPDSS INPDHLSYFH FVGRIMGLAV FHGHYINGGF
TLPFYKQLLG KPIQLSDLET VDPELHKSLV WILENDITPV LDHTFCVEHN AFGKFLQHEL
KPNGRNIPVT EENKKEYVRL YVNWRFMRGI EAQFLALQKG FNELIPQHLL KPFDNKELEL
IIGGLGKIDL NDWKANTRLK HCVADSNIVK WFWQAVESFD EERRGRLLQF VTGSTRVPLQ
GFKALQGSTG SAGPRLFTIH LIDANTDNLP KAHTCFNRID IPPYESYEKL FEKLLTAVEE
TCGFAVE
//
