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Database: UniProt
Entry: A0A0V1A427_9BILA
LinkDB: A0A0V1A427_9BILA
Original site: A0A0V1A427_9BILA 
ID   A0A0V1A427_9BILA        Unreviewed;       863 AA.
AC   A0A0V1A427;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Mothers against decapentaplegic homolog {ECO:0000256|RuleBase:RU361195};
DE            Short=MAD homolog {ECO:0000256|RuleBase:RU361195};
DE            Short=Mothers against DPP homolog {ECO:0000256|RuleBase:RU361195};
DE   AltName: Full=SMAD family member {ECO:0000256|RuleBase:RU361195};
GN   Name=Smad4 {ECO:0000313|EMBL:KRY19246.1};
GN   ORFNames=T12_6894 {ECO:0000313|EMBL:KRY19246.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19246.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY19246.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19246.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361195}.
CC       Nucleus {ECO:0000256|RuleBase:RU361195}.
CC   -!- SIMILARITY: Belongs to the dwarfin/SMAD family.
CC       {ECO:0000256|ARBA:ARBA00005545, ECO:0000256|RuleBase:RU361195}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY19246.1}.
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DR   EMBL; JYDQ01000037; KRY19246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1A427; -.
DR   STRING; 990121.A0A0V1A427; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0050793; P:regulation of developmental process; IEA:UniProt.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt.
DR   CDD; cd10492; MH1_SMAD_4; 1.
DR   CDD; cd10498; MH2_SMAD_4; 1.
DR   Gene3D; 2.60.200.10; -; 1.
DR   Gene3D; 3.90.520.10; SMAD MH1 domain; 1.
DR   InterPro; IPR013790; Dwarfin.
DR   InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR   InterPro; IPR013019; MAD_homology_MH1.
DR   InterPro; IPR017855; SMAD-like_dom_sf.
DR   InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR036578; SMAD_MH1_sf.
DR   PANTHER; PTHR13703:SF45; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG; 1.
DR   PANTHER; PTHR13703; SMAD; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF03166; MH2; 1.
DR   SMART; SM00523; DWA; 1.
DR   SMART; SM00524; DWB; 1.
DR   SUPFAM; SSF56366; SMAD MH1 domain; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS51075; MH1; 1.
DR   PROSITE; PS51076; MH2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU361195};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361195};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU361195};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU361195}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          318..445
FT                   /note="MH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51075"
FT   DOMAIN          639..863
FT                   /note="MH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51076"
FT   REGION          241..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..281
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  91745 MW;  D22317814F8B56C9 CRC64;
     MKISPKPNGC QEVPANVSNF CSVNAQHSQT PSGGFPIRAA VGGLGVGVGR IEGRGGGGGS
     GGGGGAAAAA VATVTGGTAA TMATTAPPLP TAAPVAVGAD GRAIYASSAY SAGKIPVNNY
     PNMATLLNSD PLSSNTHEYE TRVTVEAVSS VNDGQQRHKA QLSICTYASP GSIAGGDMET
     PPEITHPISS PCMGALTSGS GGGGTPTAML MQNPCANQGG AMMSTCVSAY HHPVNMNMQQ
     PMHHQQQHTG VQQQQQQQHH HHHQHPPPPP PPPPPPAPPS QHSQHHHQQQ QQQQQQQQQQ
     QQSSSSIIAA SHQSSSSDAC ASIVHSLMCH RQGGDEGFSR RAIESLIKKL KDKRDELDAL
     IQAITTGGSH VTKCVTIQRT LDGRLQVAGR KGFPHVVYAR IWRWPDLHKN ELKSNSYCQY
     AFDLKVDLVC VNPYHYERVV SPGISNLDFS ALRLDATSPS LKTEFGCGLV ESPTGAGVSK
     PPSSESPLSP VAKVDANTDL PPTQNIAHLP QMSQSAGSAY PVVQGAAEIM GPSSVDSGHT
     SVPAPSTTPN WGSQQQQQQQ QQQQQQVSPA SPHQYQRQGF HVLPAPTATL QPSVYGSAIV
     WPLASVDRNP SFFVTSARLS ALEAEMNTPL TTQPMPDFWC SIAYYELDTQ VGETFKTPSS
     HNSVTVDGYV DPSGVNRFCL GALSNVHRTE VSEKARIHIG RGVRLDLKGE GDVWLCCLSE
     YSVFVQSYYL DREAGRAPGD AVHKIYPKAY IKVFDLRQCH RQMLQQAATA HAAAAAQAAA
     VAGLVNDPGV TGLPPAVSLS AAAGIGVDDL RRLCILRLSF VKGWGPDYPR TTIKATPCWI
     EVHLHRALQL LDEVLHTMPG LTG
//
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