ID   SMUF1_XENLA             Reviewed;         731 AA.
AC   Q9PUN2; Q6GPK6;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=E3 ubiquitin-protein ligase SMURF1;
DE            Short=xSMURF1;
DE            EC=2.3.2.26 {ECO:0000250|UniProtKB:Q9HCE7};
DE   AltName: Full=HECT-type E3 ubiquitin transferase SMURF1;
DE   AltName: Full=SMAD ubiquitination regulatory factor 1;
DE   AltName: Full=SMAD-specific E3 ubiquitin-protein ligase 1;
GN   Name=smurf1;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Blastula;
RX   PubMed=10458166; DOI=10.1038/23293;
RA   Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H.;
RT   "A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic
RT   pattern formation.";
RL   Nature 400:687-693(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator
CC       of BMP signaling pathway. Mediates ubiquitination and degradation of
CC       smad1 and smad5, 2 receptor-regulated SMADs specific for the BMP
CC       pathway. Promotes ubiquitination and subsequent proteasomal degradation
CC       of TRAF family members and rhoa. May play a role in dendrite formation
CC       by melanocytes. {ECO:0000250|UniProtKB:Q9HCE7}.
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:Q9HCE7};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from the egg stage to the swimming
CC       tadpole, with maximum levels observed in the stages from egg to
CC       gastrula. At gastrulation distributed uniformly in embryonic ectoderm
CC       and involuting mesoderm, and expression gradually localizes to the
CC       nervous system. At early tadpole stages expressed in the CNS, eye,
CC       branchial arches, kidney and somites. {ECO:0000269|PubMed:10458166}.
CC   -!- DOMAIN: The C2 domain mediates membrane localization and substrate
CC       selection. {ECO:0000250}.
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DR   EMBL; AF169310; AAD52564.1; -; mRNA.
DR   EMBL; BC073111; AAH73111.1; -; mRNA.
DR   RefSeq; NP_001081939.1; NM_001088470.1.
DR   AlphaFoldDB; Q9PUN2; -.
DR   BMRB; Q9PUN2; -.
DR   SMR; Q9PUN2; -.
DR   BioGRID; 99466; 1.
DR   DNASU; 398131; -.
DR   GeneID; 398131; -.
DR   KEGG; xla:398131; -.
DR   CTD; 398131; -.
DR   Xenbase; XB-GENE-479050; smurf1.L.
DR   OrthoDB; 167687at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR   GO; GO:0007398; P:ectoderm development; TAS:UniProtKB.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; TAS:UniProtKB.
DR   GO; GO:0036211; P:protein modification process; TAS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
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; 1.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF51045; SSF51045; 2.
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; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Differentiation; Membrane; Reference proteome;
KW   Repeat; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..731
FT                   /note="E3 ubiquitin-protein ligase SMURF1"
FT                   /id="PRO_0000120328"
FT   DOMAIN          1..120
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          233..266
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          279..312
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          394..731
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          210..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        699
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   731 AA;  83259 MW;  3CE88E512A42CE2C CRC64;
     MSNVVTRRGG SSIRVRLTVL CAKNLAKRDF FRLPDPFAKI VVDGSGQCHS TDTVKNTLDP
     KWNQHYDLYV GKMDSITISI WNHKKIHKKQ GAGFLGCVRL LSNAISRLKD TGYQRLDLCK
     LNPTDNDAVR GQIVVSLQTR DRIGTLGSVV DCRGLLDNEG ALLEDTGPGR PLSCFMDEPA
     PYTDGPGAAG GGPGRLVESP GQEQRLQAQR VRGPEVREHV QTPQNRSHGF QSQDLPEGYE
     QRTTVQGQVY FLHTQTGVST WHDPRIPRDL NSVNCDDLGS LPAGWEVRTT VSGRIYFVDH
     NNRTTQFTDP RLHHIINHQS QLKEPNHAIP VQSDGSLEDG DEFPAQRYER DLVQKLKVLR
     HELSLLQPQA GHCRVEVSRE EIFEESYRQI MKMRPKDLKK RLMVKFRGEE GLDYGGVARE
     WLYLLCHEML NPYYGLFQYS TDNIYTLQIN PDSSINPDHL SYFHFVGRIM GLAVFHGHYI
     NGGFTVPFYK QLLGKPIQLS DLESVDPELH KSLVWILEND ITSVLDHTFC VEHNAFGRLL
     QHELKPNGKN LQVTEENKKE YVRLYVNWRF MRGIEAQFLA LQKGFNELIP QHLLKPFEQK
     ELELIIGGLD KIDISDWKAN TRLKHCLANS NIVQWFWQAV ESFDEERRAR LLQFVTGSTR
     VPLQGFKALQ GSTGAAGPRL FTIHLIDANT DNLPKAHTCF NRIDIPPYES YEKLYEKLLT
     AVEETSGFAV E