SMAD5_RAT
ID SMAD5_RAT Reviewed; 465 AA.
AC Q9R1V3;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H.,
RA Suto T., Nakagawa K., Nakahara Y., Higashi K.;
RT "Molecular cloning of rat Smad5 gene.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Interacts with PEBP2-
CC alpha subunit and SMURF1. Interacts with SUV39H1 and SUV39H2. Interacts
CC (via MH2 domain) with LEMD3. Interacts with WWP1. Interacts with
CC TMEM119. Interacts with ZNF8. {ECO:0000250|UniProtKB:P97454,
CC ECO:0000250|UniProtKB:Q99717}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=In the cytoplasm in the absence of ligand. Migration to the
CC nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type
CC 1 receptor kinase. {ECO:0000250}.
CC -!- PTM: Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin
CC ligase SMURF1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; AB010955; BAA83093.1; -; mRNA.
DR RefSeq; NP_067724.1; NM_021692.1.
DR RefSeq; XP_006253648.1; XM_006253586.3.
DR RefSeq; XP_006253649.1; XM_006253587.3.
DR RefSeq; XP_006253650.1; XM_006253588.3.
DR RefSeq; XP_008769669.1; XM_008771447.2.
DR RefSeq; XP_008769670.1; XM_008771448.2.
DR RefSeq; XP_017456146.1; XM_017600657.1.
DR RefSeq; XP_017456147.1; XM_017600658.1.
DR RefSeq; XP_017456148.1; XM_017600659.1.
DR AlphaFoldDB; Q9R1V3; -.
DR SMR; Q9R1V3; -.
DR STRING; 10116.ENSRNOP00000016704; -.
DR iPTMnet; Q9R1V3; -.
DR PhosphoSitePlus; Q9R1V3; -.
DR jPOST; Q9R1V3; -.
DR PaxDb; Q9R1V3; -.
DR PRIDE; Q9R1V3; -.
DR Ensembl; ENSRNOT00000016704; ENSRNOP00000016704; ENSRNOG00000022870.
DR GeneID; 59328; -.
DR KEGG; rno:59328; -.
DR UCSC; RGD:620158; rat.
DR CTD; 4090; -.
DR RGD; 620158; Smad5.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000155437; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; Q9R1V3; -.
DR OMA; PPEEQMG; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; Q9R1V3; -.
DR TreeFam; TF314923; -.
DR Reactome; R-RNO-201451; Signaling by BMP.
DR PRO; PR:Q9R1V3; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000022870; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; Q9R1V3; baseline and differential.
DR Genevisible; Q9R1V3; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0007281; P:germ cell development; ISO:RGD.
DR GO; GO:0001880; P:Mullerian duct regression; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0002051; P:osteoblast fate commitment; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0030278; P:regulation of ossification; NAS:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
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 Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99717"
FT CHAIN 2..465
FT /note="Mothers against decapentaplegic homolog 5"
FT /id="PRO_0000090867"
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..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..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 MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99717"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99717,
FT ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 465 AA; 52215 MW; 798F4BC07CC84044 CRC64;
MTSMASLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME ELEKALSSPG
QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLDIC EFPFGSKQKE
VCINPYHYKR VESPVLPPVL VPRHNEFNPQ HSLLVQFRNL SHNEPHMPQN ATFPDSFHQP
NSTPFPLSPN SPYPPSPASS TYPNSPASSG PGSPFQLPAD TPPPAYMPPD DQMGQDNSQP
MDTSNNMIPQ IMPSISSRDV QPVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
DPANNKSRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC
NFHHGFHPTT VCKIPSSCSL KIFNNQEFAQ LLAQSVNHGF EAVYELTKMC TIRMSFVKGW
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPLNP ISSVS
