SMAD5_CHICK
ID SMAD5_CHICK Reviewed; 465 AA.
AC Q56I99;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Mothers against decapentaplegic homolog 5;
DE Short=MAD homolog 5;
DE Short=Mothers against DPP homolog 5;
DE AltName: Full=SMAD family member 5;
DE Short=SMAD 5;
DE Short=Smad5;
GN Name=SMAD5; Synonyms=MADH5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Li J., Wang Y., Hon C., Wong E.W., Leung F.C.;
RT "Cloning of Smad 1, Smad5 and Smad8 from the chicken ovary and
RT characterization of their expression during chicken ovarian development.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional modulator activated by BMP (bone
CC morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-
CC regulated SMAD (R-SMAD) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May form trimers with the co-SMAD SMAD4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when
CC complexed with SMAD4 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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; AY953144; AAX56945.1; -; mRNA.
DR RefSeq; NP_001014968.1; NM_001014968.1.
DR RefSeq; XP_015149452.1; XM_015293966.1.
DR RefSeq; XP_015149453.1; XM_015293967.1.
DR RefSeq; XP_015149454.1; XM_015293968.1.
DR PDB; 6TBZ; X-ray; 1.78 A; A=11-138.
DR PDBsum; 6TBZ; -.
DR AlphaFoldDB; Q56I99; -.
DR SMR; Q56I99; -.
DR STRING; 9031.ENSGALP00000039387; -.
DR PaxDb; Q56I99; -.
DR Ensembl; ENSGALT00000040187; ENSGALP00000039387; ENSGALG00000006309.
DR GeneID; 395679; -.
DR KEGG; gga:395679; -.
DR CTD; 4090; -.
DR VEuPathDB; HostDB:geneid_395679; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000155437; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; Q56I99; -.
DR OMA; PPEEQMG; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; Q56I99; -.
DR Reactome; R-GGA-201451; Signaling by BMP.
DR PRO; PR:Q56I99; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000006309; Expressed in spermatocyte and 13 other 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:0005634; C:nucleus; IDA:AgBase.
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: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 Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 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; PTHR13703; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..465
FT /note="Mothers against decapentaplegic homolog 5"
FT /id="PRO_0000291877"
FT DOMAIN 13..137
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 271..465
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 163..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:6TBZ"
FT HELIX 25..42
FT /evidence="ECO:0007829|PDB:6TBZ"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:6TBZ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6TBZ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6TBZ"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6TBZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6TBZ"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:6TBZ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6TBZ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6TBZ"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6TBZ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6TBZ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6TBZ"
SQ SEQUENCE 465 AA; 52228 MW; FC7FA32ABF016642 CRC64;
MTSMASLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME ELEKALSSPG
QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLDIC EFPFGSKQKE
VCINPYHYKR VESPVLPPVL VPRHSEFNPQ HSLLVQFRNL SHNEPHMPHN ATFPDSFQQP
NSTPFSISPN SPYPPSPASS TYPSSPASSG PSSPFQLPAD TPPPAYMPPD DQMGQDNSQS
MDTSNTMIPQ IMPNISTRDV QPVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
DPSNNKNRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC
NYHHGFHPTT VCKIPSGCSL KIFNNQEFAQ LLAQSVNHGF EAVYELTKMC TIRMSFVKGW
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPLNP ISSVS
