ID SMUF2_DANRE Reviewed; 765 AA.
AC A9JRZ0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=E3 ubiquitin-protein ligase SMURF2;
DE EC=2.3.2.26 {ECO:0000250|UniProtKB:Q9HAU4};
DE AltName: Full=HECT-type E3 ubiquitin transferase SMURF2;
DE AltName: Full=SMAD ubiquitination regulatory factor 2;
DE AltName: Full=SMAD-specific E3 ubiquitin-protein ligase 2;
GN Name=smurf2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates.
CC {ECO:0000250|UniProtKB:Q9HAU4}.
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:0000250|UniProtKB:Q9HAU4};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAU4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HAU4}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9HAU4}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9HAU4}.
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DR EMBL; BC155849; AAI55850.1; -; mRNA.
DR RefSeq; NP_001107898.1; NM_001114426.1.
DR AlphaFoldDB; A9JRZ0; -.
DR SMR; A9JRZ0; -.
DR STRING; 7955.ENSDARP00000055490; -.
DR PaxDb; 7955-ENSDARP00000055490; -.
DR PeptideAtlas; A9JRZ0; -.
DR GeneID; 563633; -.
DR KEGG; dre:563633; -.
DR AGR; ZFIN:ZDB-GENE-030131-1830; -.
DR CTD; 64750; -.
DR ZFIN; ZDB-GENE-030131-1830; smurf2.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_1_1_1; -.
DR InParanoid; A9JRZ0; -.
DR OMA; LIFLICE; -.
DR OrthoDB; 5480520at2759; -.
DR PhylomeDB; A9JRZ0; -.
DR TreeFam; TF323658; -.
DR Reactome; R-DRE-201451; Signaling by BMP.
DR Reactome; R-DRE-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-DRE-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-DRE-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-DRE-4641257; Degradation of AXIN.
DR Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:A9JRZ0; -.
DR Proteomes; UP000000437; Chromosome 3.
DR Bgee; ENSDARG00000038067; Expressed in somite and 24 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 3.
DR Gene3D; 2.20.70.10; -; 2.
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:SF300; E3 UBIQUITIN-PROTEIN LIGASE SMURF2; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
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; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Membrane; Nucleus; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..765
FT /note="E3 ubiquitin-protein ligase SMURF2"
FT /id="PRO_0000358319"
FT DOMAIN 1..117
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 157..190
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 251..284
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 297..330
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 431..765
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 341..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 733
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 765 AA; 87464 MW; 7CE5429A1479B892 CRC64;
MSNQGVRRNG PVKLRLTVLC AKNLVKKDFF RLPDPFAKVV VDGSGQCHST DTVRNTLDPK
WNQHYDLYIG KSDSITISVW NHKKIHKKQG AGFLGCVRLL SNSINRLKDT GYQRLDLNKL
GPNDSDTVRG QIVVSLQSRD RIGSGGPVVD CSRLFDNDLP DGWEERRTAS GRIQYLNHIT
RSTQWERPTR PASEYSSPGR PLSCLVDENT PIMTPNGAAG VPADDPRVQE RRVRSQRHRN
YMSRTHLHTP PDLPEGYEQR TTQQGQVYFL HTQTGVSTWH DPRVPRDLSN VNCEELGPLP
PGWEIRNTAT GRVYFVDHNN RTTQFTDPRL SANLHLVLNP SPNGSRAAVE AQSSSRPGQL
KEQAQSVVSP GNLPEDPECL TVPKYKRDLV QKLKILRQEL SQQQPQAGHC RIEVSREEIF
EESYRQVMKM RPKDLWKRLM VKFRGEEGLD YGGVAREWLY LLSHEMLNPY YGLFQYSRDD
IYTLQINPDS AVNPEHLSYF HFVGRIMGMA VFHGHYIDGG FTLPFYKQLL GKPITLDDME
SVDPDLHNSL VWILDNDITG VLDHTFCVEH NAYGEIIQHE LKPNGKSIPV TQDTKKEYVR
LYVNWRFLRG IEAQFLALQK GFNEVIPQHL LKAFDEKELE LIVCGLGKID INDWKSNTRL
KHCTPDSNIV KWFWRAVESY DEERRARLLQ FVTGSSRVPL QGFKALQGAA GPRLFTIHQI
DASTNNLPKA HTCFNRIDIP PYESYDKLYD KLLTAIEETC GFAVE
//
