ID   SMUF2_XENLA             Reviewed;         751 AA.
AC   Q2TAS2;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2005) 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}.
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   EMBL; BC110749; AAI10750.1; -; mRNA.
DR   RefSeq; NP_001082282.1; NM_001088813.1.
DR   AlphaFoldDB; Q2TAS2; -.
DR   BMRB; Q2TAS2; -.
DR   SMR; Q2TAS2; -.
DR   DNASU; 398372; -.
DR   GeneID; 398372; -.
DR   KEGG; xla:398372; -.
DR   CTD; 398372; -.
DR   Xenbase; XB-GENE-865123; smurf2.S.
DR   OMA; MEEICHP; -.
DR   OrthoDB; 167687at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 398372; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 3.
DR   Gene3D; 2.60.40.150; -; 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   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; SSF49562; 1.
DR   SUPFAM; SSF51045; SSF51045; 3.
DR   SUPFAM; SSF56204; SSF56204; 1.
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..751
FT                   /note="E3 ubiquitin-protein ligase SMURF2"
FT                   /id="PRO_0000358320"
FT   DOMAIN          1..119
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          417..751
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          214..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        719
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   751 AA;  86325 MW;  A8933EAF4992B99C CRC64;
     MSNQGSRRNG PVKLRLTVLC AKNLVKKDFF RLPDSFAKVV VDGSGQCHST DTVKNTLDPK
     WNQHYDLYIG KSDSITISVW NHKKIHKKQG AGFLGCVRLL SNAINRLKDT GYQRLDLCKL
     GPNDNDTVRG QIVVSLQSRD RIGSGGQVVD CSRLFDNDLP DGWEERRTAS GRIQYLNHIT
     RTTQWERPTR PASEYSSPGR PLSCFVDENT PITGTNGASC GQTSDPRISE RRVRSQRHRN
     YMSRTHLHTP PDLPEGYEQR TTQQGQVYFL HTQTGVSTWH DPRVPRDLGN VNCEELGPLP
     PGWEIRNTAT GRVYFVDHNN RTTQFTDPRL SANLHLVLNR QNQQLKEQQP PQVVSLCQLP
     DEVECLTVPR YKRDLVHKLK SLRQELSQQQ PQAGHCRIEV SREEIFEESY RQVMKMRPKD
     LWKRLMIKFR GEEGLDYGGV AREWLYLLSH DMLNPYYGLF QYSRDDIYTL QINPDSAVNP
     EHLSYFHFVG RIMGMAVFHG HYIDGGFTLP FYKQLLGKPI TLDDMESVDP DLHNSLVWIL
     ENDITGVLDH TFCVEHNAYG ELIQHELKPS GKSIPVTEDT KKEYVRLYVN WRFLRGIEAQ
     FLALQKGFNE VIPQHLLKAF DEKELELIIC GLGKIDVSDW KSNTRLKHCT TDSNIVKWFW
     KAVESFDEER RARLLQFVTG SSRVPLQGFK ALQGAAGPRL FTIHQIDAST NNLPKAHTCF
     NRIDIPPYET YEKLYEKLLT AIEETCGFAV E