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Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)

 SMAD3_PIG               Reviewed;         425 AA.
P84024; O09064; O09144; O14510; O35273; Q92940; Q93002; Q9GKR4;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
26-FEB-2020, entry version 132.
RecName: Full=Mothers against decapentaplegic homolog 3;
Short=MAD homolog 3;
Short=Mad3;
Short=Mothers against DPP homolog 3;
AltName: Full=SMAD family member 3;
Short=SMAD 3;
Short=Smad3;
Name=SMAD3; Synonyms=MADH3;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
Yoshiyasu I., Takashi A., Ito Y., Awata T.;
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular
signal transducer and transcriptional modulator activated by TGF-beta
(transforming growth factor) and activin type 1 receptor kinases. Binds
the TRE element in the promoter region of many genes that are regulated
by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates
transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-
1/SMAD site to regulate TGF-beta-mediated transcription. Has an
inhibitory effect on wound healing probably by modulating both growth
and migration of primary keratinocytes and by altering the TGF-mediated
chemotaxis of monocytes. This effect on wound healing appears to be
hormone-sensitive. Regulator of chondrogenesis and osteogenesis and
inhibits early healing of bone fractures. Positively regulates PDPK1
kinase activity by stimulating its dissociation from the 14-3-3 protein
YWHAQ which acts as a negative regulator.
{ECO:0000250|UniProtKB:P84022}.
-!- SUBUNIT: Monomer; in the absence of TGF-beta. Homooligomer; in the
presence of TGF-beta. Heterotrimer; forms a heterotrimer in the
presence of TGF-beta consisting of two molecules of C-terminally
phosphorylated SMAD2 or SMAD3 and one of SMAD4 to form the
transcriptionally active SMAD2/SMAD3-SMAD4 complex. Interacts with
TGFBR1. Interacts (via MH2 domain) with ZFYVE9. Interacts with HDAC1,
TGIF and TGIF2, RUNX3, CREBBP, SKOR1, SKOR2, SNON, ATF2, SMURF2 and
SNW1. Interacts with DACH1; the interaction inhibits the TGF-beta
signaling. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and
SMAD3. Forms a complex with SMAD2 and TRIM33 upon addition of TGF-beta.
Found in a complex with SMAD3, RAN and XPO4. Interacts in the complex
directly with XPO4. Interacts (via MH2 domain) with LEMD3; the
interaction represses SMAD3 transcriptional activity through preventing
the formation of the heteromeric complex with SMAD4 and translocation
to the nucleus. Interacts with RBPMS. Interacts (via MH2 domain) with
MECOM. Interacts with WWTR1 (via its coiled-coil domain). Interacts
(via the linker region) with EP300 (C-terminal); the interaction
promotes SMAD3 acetylation and is enhanced by TGF-beta phosphorylation
in the C-terminal of SMAD3. This interaction can be blocked by
competitive binding of adenovirus oncoprotein E1A to the same C-
terminal site on EP300, which then results in partially inhibited
SMAD3/SMAD4 transcriptional activity. Interacts with SKI; the
interaction represses SMAD3 transcriptional activity. Component of the
multimeric complex SMAD3/SMAD4/JUN/FOS which forms at the AP1 promoter
site; required for synergistic transcriptional activity in response to
TGF-beta. Interacts (via an N-terminal domain) with JUN (via its basic
DNA binding and leucine zipper domains); this interaction is essential
for DNA binding and cooperative transcriptional activity in response to
TGF-beta. Interacts with PPM1A; the interaction dephosphorylates SMAD3
in the C-terminal SXS motif leading to disruption of the SMAD2/3-SMAD4
complex, nuclear export and termination of TGF-beta signaling.
Interacts (dephosphorylated form via the MH1 and MH2 domains) with
RANBP3 (via its C-terminal R domain); the interaction results in the
export of dephosphorylated SMAD3 out of the nucleus and termination of
the TGF-beta signaling. Interacts with AIP1, PML, TGFB1I1, TTRAP,
FOXL2, PRDM16, HGS and WWP1. Interacts with NEDD4L; the interaction
requires TGF-beta stimulation. Interacts with MEN1. Interacts (via MH2
domain) with CITED2 (via C-terminus). Interaction with CSNK1G2.
Interacts with PDPK1 (via PH domain). Interacts with DAB2; the
interactions are enhanced upon TGF-beta stimulation. Interacts with
USP15. Interacts with PPP5C; the interaction decreases SMAD3
phosphorylation and protein levels. Interacts with LDLRAD4 (via the
SMAD interaction motif). Interacts with PMEPA1. Interacts with ZC3H3.
Interacts with ZFHX3. Interacts with ZNF451. Identified in a complex
that contains at least ZNF451, SMAD2, SMAD3 and SMAD4. Interacts weakly
with ZNF8. Interacts (when phosphorylated) with RNF111; RNF111 acts as
an enhancer of the transcriptional responses by mediating
ubiquitination and degradation of SMAD3 inhibitors. Interacts with
STUB1, HSPA1A, HSPA1B, HSP90AA1 and HSP90AB1. Interacts (via MH2
domain) with ZMIZ1 (via SP-RING-type domain); in the TGF-beta signaling
pathway increases the activity of the SMAD3/SMAD4 transcriptional
complex (By similarity). {ECO:0000250|UniProtKB:P84022,
ECO:0000250|UniProtKB:Q8BUN5}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P84022}. Nucleus
{ECO:0000250|UniProtKB:P84022}. Note=Cytoplasmic and nuclear in the
absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus
when complexed with SMAD4. Through the action of the phosphatase PPM1A,
released from the SMAD2/SMAD4 complex, and exported out of the nucleus
by interaction with RANBP1. Co-localizes with LEMD3 at the nucleus
inner membrane. MAPK-mediated phosphorylation appears to have no effect
on nuclear import. PDPK1 prevents its nuclear translocation in response
to TGF-beta. {ECO:0000250|UniProtKB:P84022}.
-!- TISSUE SPECIFICITY: Highly expressed in the brain and ovary. Detected
in the pyramidal cells of the hippocampus, granule cells of the dentate
gyrus, granular cells of the cerebral cortex and the granulosa cells of
the ovary.
-!- DOMAIN: The MH1 domain is required for DNA binding (By similarity).
Also binds zinc ions which are necessary for the DNA binding.
{ECO:0000250}.
-!- DOMAIN: The MH2 domain is required for both homomeric and heteromeric
interactions and for transcriptional regulation. Sufficient for nuclear
import (By similarity). {ECO:0000250}.
-!- DOMAIN: The linker region is required for the TGFbeta-mediated
transcriptional activity and acts synergistically with the MH2 domain.
{ECO:0000250}.
-!- PTM: Phosphorylated on serine and threonine residues. Enhanced
phosphorylation in the linker region on Thr-179, Ser-204 and Ser-208 on
EGF and TGF-beta treatment. Ser-208 is the main site of MAPK-mediated
phosphorylation. CDK-mediated phosphorylation occurs in a cell-cycle
dependent manner and inhibits both the transcriptional activity and
antiproliferative functions of SMAD3. This phosphorylation is inhibited
by flavopiridol. Maximum phosphorylation at the G(1)/S junction. Also
phosphorylated on serine residues in the C-terminal SXS motif by TGFBR1
and ACVR1. TGFBR1-mediated phosphorylation at these C-terminal sites is
required for interaction with SMAD4, nuclear location and
transactivational activity, and appears to be a prerequisite for the
TGF-beta mediated phosphorylation in the linker region.
Dephosphorylated in the C-terminal SXS motif by PPM1A. This
dephosphorylation disrupts the interaction with SMAD4, promotes nuclear
export and terminates TGF-beta-mediated signaling. Phosphorylation at
Ser-418 by CSNK1G2/CK1 promotes ligand-dependent ubiquitination and
subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-
beta responses. Phosphorylated by PDPK1 (By similarity).
{ECO:0000250|UniProtKB:P84022}.
-!- PTM: Acetylation in the nucleus by EP300 in the MH2 domain regulates
positively its transcriptional activity and is enhanced by TGF-beta.
{ECO:0000250|UniProtKB:P84022}.
-!- PTM: Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation
negatively regulates SMAD3 transcriptional responses during the course
of TGF-beta signaling. {ECO:0000250|UniProtKB:P84022}.
-!- PTM: Ubiquitinated. Monoubiquitinated, leading to prevent DNA-binding.
Deubiquitination by USP15 alleviates inhibition and promotes activation
of TGF-beta target genes. Ubiquitinated by RNF111, leading to its
degradation: only SMAD3 proteins that are 'in use' are targeted by
RNF111, RNF111 playing a key role in activating SMAD3 and regulating
its turnover. Undergoes STUB1-mediated ubiquitination and degradation.
{ECO:0000250|UniProtKB:P84022, ECO:0000250|UniProtKB:Q8BUN5}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
---------------------------------------------------------------------------
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---------------------------------------------------------------------------
EMBL; AB052738; BAB19634.1; -; mRNA.
RefSeq; NP_999302.1; NM_214137.1.
SMR; P84024; -.
MINT; P84024; -.
STRING; 9823.ENSSSCP00000005327; -.
PaxDb; P84024; -.
PeptideAtlas; P84024; -.
PRIDE; P84024; -.
Ensembl; ENSSSCT00000005464; ENSSSCP00000005327; ENSSSCG00000004952.
Ensembl; ENSSSCT00005057440; ENSSSCP00005035375; ENSSSCG00005035367.
Ensembl; ENSSSCT00015062164; ENSSSCP00015024943; ENSSSCG00015045925.
Ensembl; ENSSSCT00025043673; ENSSSCP00025018565; ENSSSCG00025032064.
Ensembl; ENSSSCT00030064740; ENSSSCP00030029587; ENSSSCG00030046321.
Ensembl; ENSSSCT00035076339; ENSSSCP00035031189; ENSSSCG00035057061.
Ensembl; ENSSSCT00040041424; ENSSSCP00040017352; ENSSSCG00040030551.
Ensembl; ENSSSCT00045018396; ENSSSCP00045012692; ENSSSCG00045010800.
Ensembl; ENSSSCT00050004607; ENSSSCP00050001837; ENSSSCG00050003377.
Ensembl; ENSSSCT00055059976; ENSSSCP00055048056; ENSSSCG00055030102.
Ensembl; ENSSSCT00060092092; ENSSSCP00060039794; ENSSSCG00060067444.
Ensembl; ENSSSCT00070014919; ENSSSCP00070012342; ENSSSCG00070007681.
GeneID; 397260; -.
KEGG; ssc:397260; -.
CTD; 4088; -.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00940000153499; -.
InParanoid; P84024; -.
KO; K23605; -.
OMA; RHTEIPS; -.
OrthoDB; 608001at2759; -.
Proteomes; UP000008227; Chromosome 1.
Proteomes; UP000314985; Chromosome 1.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036578; SMAD_MH1_sf.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 1.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
2: Evidence at transcript level;
Acetylation; ADP-ribosylation; Cytoplasm; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P84022"
CHAIN 2..425
/note="Mothers against decapentaplegic homolog 3"
/id="PRO_0000090858"
DOMAIN 10..136
/note="MH1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
DOMAIN 232..425
/note="MH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
REGION 137..231
/note="Linker"
REGION 271..324
/note="Sufficient for interaction with XPO4"
/evidence="ECO:0000250"
METAL 64
/note="Zinc"
/evidence="ECO:0000250"
METAL 109
/note="Zinc"
/evidence="ECO:0000250"
METAL 121
/note="Zinc"
/evidence="ECO:0000250"
METAL 126
/note="Zinc"
/evidence="ECO:0000250"
SITE 40
/note="Required for trimerization"
/evidence="ECO:0000250"
SITE 41
/note="Required for interaction with DNA and JUN and for
functional cooperation with JUN"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 8
/note="Phosphothreonine; by CDK2 and CDK4"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 179
/note="Phosphothreonine; by CDK2, CDK4 and MAPK"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 204
/note="Phosphoserine; by GSK3 and MAPK"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 208
/note="Phosphoserine; by MAPK"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 213
/note="Phosphoserine; by CDK2 and CDK4"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 378
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P84022"
MOD_RES 416
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 418
/note="Phosphoserine; by CK1"
/evidence="ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 422
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 423
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439"
MOD_RES 425
/note="Phosphoserine; by TGFBR1"
/evidence="ECO:0000250|UniProtKB:Q8BUN5,
ECO:0000255|PROSITE-ProRule:PRU00439"
CROSSLNK 33
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P84022"
CROSSLNK 81
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P84022"
SEQUENCE 425 AA; 48081 MW; 46DF5E8B371321AC CRC64;
MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE LEKAITTQNV
NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELRAMELCE FAFNMKKDEV
CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF PPLDDYSHSI PENTNFPAGI EPQSNIPETP
PPGYLSEDGE TSDHQMNHSM DAGSPNLSPN PMSPAHNNLD LQPVTYCEPA FWCSISYYEL
NQRVGETFHA SQPSMTVDGF TDPSNSERFC LGLLSNVNRN AAVELTRRHI GRGVRLYYIG
GEVFAECLSD SAIFVQSPNC NQRYGWHPAT VCKIPPGCNL KIFNNQEFAA LLAQSVNQGF
EAVYQLTRMC TIRMSFVKGW GAEYRRQTVT STPCWIELHL NGPLQWLDKV LTQMGSPSIR
CSSVS


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[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
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[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[Smad7 Madh7 Madh8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[Smad1 Madh1 Madr1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[Smad4 Dpc4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[Smad1 Mad1 Madh1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[Smox Dmel\CG2262 DSMAD2 DSmad2 dSMAD2 dSmad2 dsmad2 l(1)G0348 Sad sad Smad SMAD2 Smad2 smad2 SMOX SmoX smox ted tmp CG2262 Dmel_CG2262] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[SMAD4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[ZFYVE9 MADHIP SARA SMADIP] Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)
[Mad CG12399] Protein mothers against dpp
[NFKBIA IKBA MAD3 NFKBI] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3)
[Dsec\GM11208 Dsec_GM11208] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Dper\GL20193 Dper_GL20193] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Dana\GF20979 dana_GLEANR_4213 Dana_GF20979 GF20979] Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member)
[Bcar3] Breast cancer anti-estrogen resistance protein 3 homolog (BCAR3 adapter protein, NSP family member) (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B) (p130Cas-binding protein AND-34)
[Bcar3 And34] Breast cancer anti-estrogen resistance protein 3 homolog (p130Cas-binding protein AND-34)

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