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E3 ubiquitin-protein ligase SMURF2 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF2) (SMAD ubiquitination regulatory factor 2) (SMAD-specific E3 ubiquitin-protein ligase 2)

 SMUF2_MOUSE             Reviewed;         748 AA.
A2A5Z6; A2A5Z7; Q5IRE6;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
20-JUN-2018, entry version 104.
RecName: Full=E3 ubiquitin-protein ligase SMURF2;
EC=2.3.2.26 {ECO:0000250|UniProtKB:Q9HCE7};
AltName: Full=HECT-type E3 ubiquitin transferase SMURF2;
AltName: Full=SMAD ubiquitination regulatory factor 2;
AltName: Full=SMAD-specific E3 ubiquitin-protein ligase 2;
Name=Smurf2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=129/SvJ;
PubMed=15820682; DOI=10.1016/j.cell.2005.01.035;
Yamashita M., Ying S.X., Zhang G.M., Li C., Cheng S.Y., Deng C.X.,
Zhang Y.E.;
"Ubiquitin ligase Smurf1 controls osteoblast activity and bone
homeostasis by targeting MEKK2 for degradation.";
Cell 121:101-113(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INDUCTION BY TNF SIGNALING PATHWAY ACTIVATION.
PubMed=16373342; DOI=10.1074/jbc.M509430200;
Kaneki H., Guo R., Chen D., Yao Z., Schwarz E.M., Zhang Y.E.,
Boyce B.F., Xing L.;
"Tumor necrosis factor promotes Runx2 degradation through up-
regulation of Smurf1 and Smurf2 in osteoblasts.";
J. Biol. Chem. 281:4326-4333(2006).
[6]
STABILIZATION BY SCYE1.
PubMed=18448069; DOI=10.1016/j.bbrc.2008.04.099;
Lee Y.S., Han J.M., Son S.H., Choi J.W., Jeon E.J., Bae S.-C.,
Park Y.I., Kim S.;
"AIMP1/p43 downregulates TGF-beta signaling via stabilization of
smurf2.";
Biochem. Biophys. Res. Commun. 371:395-400(2008).
-!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
an E2 ubiquitin-conjugating enzyme in the form of a thioester and
then directly transfers the ubiquitin to targeted substrates.
Interacts with SMAD1 and SMAD7 in order to trigger their
ubiquitination and proteasome-dependent degradation. In addition,
interaction with SMAD7 activates autocatalytic degradation, which
is prevented by interaction with SCYE1. Forms a stable complex
with the TGF-beta receptor-mediated phosphorylated SMAD2 and
SMAD3. In this way, SMAD2 may recruit substrates, such as SNON,
for ubiquitin-mediated degradation. Enhances the inhibitory
activity of SMAD7 and reduces the transcriptional activity of
SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable
decrease in steady-state level of SMAD1 protein and a smaller
decrease of SMAD2 level. {ECO:0000250|UniProtKB:Q9HAU4}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:Q9HCE7}.
-!- ENZYME REGULATION: Activated by NDFIP1- and NDFIP2-binding.
{ECO:0000250}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts (via WW domains) with SMAD1. Interacts (via WW
domains) with SMAD2 (via PY-motif). Interacts (via WW domains)
with SMAD3 (via PY-motif). Interacts with SMAD6. Interacts with
SMAD7 (via PY-motif) and TGFBR1; SMAD7 recruits SMURF2 to the TGF-
beta receptor and regulates its degradation. Does not interact
with SMAD4; SMAD4 lacks a PY-motif. Interacts with AIMP1 (By
similarity). Interacts with NDFIP1 and NDFIP2; this interaction
activates the E3 ubiquitin-protein ligase (By similarity).
{ECO:0000250|UniProtKB:Q9HAU4}.
-!- INTERACTION:
O14641:DVL2 (xeno); NbExp=8; IntAct=EBI-2348309, EBI-740850;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAU4}.
Cytoplasm {ECO:0000250|UniProtKB:Q9HAU4}. Cell membrane
{ECO:0000250|UniProtKB:Q9HAU4}. Membrane raft
{ECO:0000250|UniProtKB:Q9HAU4}. Note=Cytoplasmic in the presence
of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in
membrane rafts. Interacts with STAMBP and RNF11. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=A2A5Z6-1; Sequence=Displayed;
Name=2;
IsoId=A2A5Z6-2; Sequence=VSP_036055, VSP_036056;
-!- INDUCTION: Up-regulated about ten-fold by activation of the TNF-
signaling pathway in vitro. {ECO:0000269|PubMed:16373342}.
-!- DOMAIN: The second and third WW domains are responsible for
interaction with the PY-motif of R-SMAD (SMAD1, SMAD2 and SMAD3).
{ECO:0000250}.
-!- DOMAIN: The C2 domain is involved in autoinhibition of the
catalytic activity by interacting with the HECT domain.
{ECO:0000250}.
-!- PTM: Auto-ubiquitinated and ubiquitinated in the presence of RNF11
and UBE2D1. Ubiquitinated by the SCF(FBXL15) complex, leading to
its degradation by the proteasome (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Level decreases under the suppression of SCYE1,
suggesting that SCYE1 stabilizes SMURF2.
-----------------------------------------------------------------------
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EMBL; AY685230; AAV87906.1; -; mRNA.
EMBL; AL593847; CAM16223.1; -; Genomic_DNA.
EMBL; AL593847; CAM16224.1; -; Genomic_DNA.
EMBL; CH466558; EDL34316.1; -; Genomic_DNA.
EMBL; BC138786; AAI38787.1; -; mRNA.
EMBL; BC138788; AAI38789.1; -; mRNA.
CCDS; CCDS25564.1; -. [A2A5Z6-1]
RefSeq; NP_079757.2; NM_025481.2. [A2A5Z6-1]
RefSeq; XP_006533999.1; XM_006533936.3. [A2A5Z6-2]
UniGene; Mm.340955; -.
ProteinModelPortal; A2A5Z6; -.
SMR; A2A5Z6; -.
BioGrid; 211376; 25.
IntAct; A2A5Z6; 16.
STRING; 10090.ENSMUSP00000090177; -.
iPTMnet; A2A5Z6; -.
PhosphoSitePlus; A2A5Z6; -.
MaxQB; A2A5Z6; -.
PaxDb; A2A5Z6; -.
PeptideAtlas; A2A5Z6; -.
PRIDE; A2A5Z6; -.
Ensembl; ENSMUST00000092517; ENSMUSP00000090177; ENSMUSG00000018363. [A2A5Z6-1]
Ensembl; ENSMUST00000103067; ENSMUSP00000099356; ENSMUSG00000018363. [A2A5Z6-2]
Ensembl; ENSMUST00000167787; ENSMUSP00000129269; ENSMUSG00000018363. [A2A5Z6-1]
GeneID; 66313; -.
KEGG; mmu:66313; -.
UCSC; uc007lzx.2; mouse. [A2A5Z6-1]
UCSC; uc007lzy.2; mouse. [A2A5Z6-2]
CTD; 64750; -.
MGI; MGI:1913563; Smurf2.
eggNOG; KOG0940; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00760000118966; -.
HOGENOM; HOG000208451; -.
HOVERGEN; HBG004134; -.
InParanoid; A2A5Z6; -.
KO; K04678; -.
OMA; SCLVDEN; -.
OrthoDB; EOG091G011S; -.
PhylomeDB; A2A5Z6; -.
TreeFam; TF323658; -.
BRENDA; 6.3.2.19; 3474.
Reactome; R-MMU-201451; Signaling by BMP.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
Reactome; R-MMU-4641257; Degradation of AXIN.
Reactome; R-MMU-5632684; Hedgehog 'on' state.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:A2A5Z6; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018363; -.
Genevisible; A2A5Z6; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISO:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; ISO:MGI.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 3.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR024928; E3_ub_ligase_SMURF1.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00168; C2; 1.
Pfam; PF00632; HECT; 1.
Pfam; PF00397; WW; 3.
PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
SMART; SM00239; C2; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00456; WW; 3.
SUPFAM; SSF51045; SSF51045; 3.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 3.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Nucleus; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 748 E3 ubiquitin-protein ligase SMURF2.
/FTId=PRO_0000358318.
DOMAIN 1 98 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 157 190 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 251 284 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 297 330 WW 3. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 414 748 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
COMPBIAS 347 351 Poly-Gln.
ACT_SITE 716 716 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
VAR_SEQ 18 30 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_036055.
VAR_SEQ 31 31 R -> G (in isoform 2). {ECO:0000305}.
/FTId=VSP_036056.
CONFLICT 130 130 G -> V (in Ref. 1; AAV87906).
{ECO:0000305}.
SEQUENCE 748 AA; 86175 MW; 385AFA32D289D33F CRC64;
MSNPGGRRNG PVKLRLTVLC AKNLVKKDFF RLPDPFAKVV VDGSGQCHST DTVKNTLDPK
WNQHYDLYIG KSDSVTISVW NHKKIHKKQG AGFLGCVRLL SNAINRLKDT GYQRLDLCKL
GPNDNDTVRG QIVVSLQSRD RIGTGGQVVD CSRLFDNDLP DGWEERRTAS GRIQYLNHIT
RTTQWERPTR PASEYSSPGR PLSCFVDENT PITGTNGATC GHSSDPRLAE RRVRSQRHRN
YMSRTHLHTP PDLPEGYEQR TTQQGQVYFL HTQTGVSTWH DPRVPRDLSN INCEELGPLP
PGWEIRNTAT GRVYFVDHNN RTTQFTDPRL SANLHLVLNR QNQLKDQQQQ QVVPLCPDDT
ECLTVPRYKR DLVQKLKILR QELSQQQPQA GHCRIEVSRE EIFEESYRQV MKMRPKDLWK
RLMIKFRGEE GLDYGGVARE WLYLLSHEML NPYYGLFQYS RDDIYTLQIN PDSAVNPEHL
SYFHFVGRIM GMAVFHGHYI DGGFTLPFYK QLLGKSITLD DMELVDPDLH NSLVWILEND
ITGVLDHTFC VEHNAYGEII QHELKPNGKS IPVTEENKKE YVRLYVNWRF LRGIEAQFLA
LQKGFNEVIP QHLLKTFDEK ELELIICGLG KIDVSDWKVN TRLKHCTPDS NVVKWFWKAV
EFFDEERRAR LLQFVTGSSR VPLQGFKALQ GAAGPRLFTI HQIDACTNNL PKAHTCFNRI
DIPPYESYEK LYEKLLTAIE ETCGFAVE


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