ID W5MPK7_LEPOC Unreviewed; 467 AA.
AC W5MPK7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010316.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010316.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
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; AHAT01013971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006628242.1; XM_006628179.2.
DR RefSeq; XP_015197533.1; XM_015342047.1.
DR AlphaFoldDB; W5MPK7; -.
DR STRING; 7918.ENSLOCP00000010316; -.
DR Ensembl; ENSLOCT00000010329.1; ENSLOCP00000010316.1; ENSLOCG00000008478.1.
DR GeneID; 102682759; -.
DR KEGG; loc:102682759; -.
DR CTD; 4093; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000154391; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; W5MPK7; -.
DR OMA; CSASYPH; -.
DR OrthoDB; 2891561at2759; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000008478; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR CDD; cd10490; MH1_SMAD_1_5_9; 1.
DR CDD; cd10497; MH2_SMAD_1_5_9; 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:SF41; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 9; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361195};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
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 16..140
FT /note="MH1"
FT /evidence="ECO:0000259|PROSITE:PS51075"
FT DOMAIN 273..467
FT /note="MH2"
FT /evidence="ECO:0000259|PROSITE:PS51076"
FT REGION 192..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 52671 MW; A811B9F54005911E CRC64;
MHSTTSITSL FSFTSPAVKR LLGWKQGDEE EKWAEKAVDS LVKKLKKKKG AMEELERALS
CPGQPSKCVT IPRSLDGRLQ VSHRKGLPHV IYCRVWRWPD LQSHHELKAL ECCEFPFGSK
QKDICINPYH YRRVETPVLP PVLVPRHSEF NPQHSLLAKF RNASLHNEPL MPQNATYPDS
FQQLPCNAFS SSPTSSFSQS PSTISYPNSP SSTTEPGSPY QLTAETPPPP YSMTETAANE
DVKPMDSSNP NKLILSAPHR DLRPVCYEEP EYWCSVAYYE LNNRVGETFH ASARSVLIDG
FTDPSNNKNR FCLGLLSNVN RNSTIEHTRR HIGKGVHLYY VGGEVYAECL SDSSIFVQSR
NCNYQHGFHA TTVCKIPSGC SLKIFNNQLF AQLLAQSVNH GFEVVYELTK MCTIRMSFVK
GWGAEYHRQD VTSTPCWIEI HLHGPLQWLD KVLTQMGSPH NPISSVS
//
