HDGF_BOVIN
ID HDGF_BOVIN Reviewed; 239 AA.
AC Q9XSK7;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Hepatoma-derived growth factor;
DE Short=HDGF;
GN Name=HDGF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Dietz F., Nakamura H., Gieselmann V.;
RT "HRP-3: a new member of the hepatoma derived growth factor related protein
RT family interacts with HDGF and another HDGF related polypeptide.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a transcriptional repressor (By similarity). Has
CC mitogenic activity for fibroblasts (By similarity). Heparin-binding
CC protein (By similarity). {ECO:0000250|UniProtKB:P51858}.
CC -!- SUBUNIT: Monomer, and domain-swapped homodimer (By similarity).
CC Interacts with nuclear proteins NCL and YBX1/YB1 (By similarity).
CC {ECO:0000250|UniProtKB:P51858}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51858}. Cytoplasm
CC {ECO:0000250|UniProtKB:P51858}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P51858}. Note=Secreted by exosomes and is
CC located inside the exosome (By similarity). May also be secreted as
CC free protein via an as yet unknown pathway (By similarity).
CC {ECO:0000250|UniProtKB:P51858}.
CC -!- DOMAIN: The PWWP domain harbors the heparin-binding sites and is
CC responsible for DNA-binding, while the C-terminal region is essentially
CC unstructured. {ECO:0000250|UniProtKB:P51858}.
CC -!- DOMAIN: The N-terminal region does not contain a typical signal
CC sequence but is required for secretion (By similarity). It also
CC determines exosomal location (By similarity).
CC {ECO:0000250|UniProtKB:P51858, ECO:0000250|UniProtKB:P51859}.
CC -!- PTM: Sumoylated with SUMO1. Sumoylation prevents binding to chromatin.
CC {ECO:0000250|UniProtKB:P51858}.
CC -!- PTM: Phosphorylation at Ser-165 is likely to be required for secretion.
CC {ECO:0000250|UniProtKB:P51859}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; AJ237996; CAB40626.1; -; mRNA.
DR RefSeq; NP_787026.1; NM_175832.2.
DR RefSeq; XP_015317502.1; XM_015462016.1.
DR AlphaFoldDB; Q9XSK7; -.
DR BMRB; Q9XSK7; -.
DR SMR; Q9XSK7; -.
DR STRING; 9913.ENSBTAP00000008609; -.
DR iPTMnet; Q9XSK7; -.
DR PaxDb; Q9XSK7; -.
DR PeptideAtlas; Q9XSK7; -.
DR PRIDE; Q9XSK7; -.
DR Ensembl; ENSBTAT00000008609; ENSBTAP00000008609; ENSBTAG00000039793.
DR GeneID; 327953; -.
DR KEGG; bta:327953; -.
DR CTD; 3068; -.
DR VEuPathDB; HostDB:ENSBTAG00000039793; -.
DR VGNC; VGNC:29787; HDGF.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000157485; -.
DR InParanoid; Q9XSK7; -.
DR OrthoDB; 530959at2759; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000039793; Expressed in esophagus and 105 other tissues.
DR ExpressionAtlas; Q9XSK7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05834; HDGF_related; 1.
DR InterPro; IPR035496; HDGF-rel_PWWP.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Disulfide bond; DNA-binding; Growth factor;
KW Heparin-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Secreted; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..239
FT /note="Hepatoma-derived growth factor"
FT /id="PRO_0000191699"
FT DOMAIN 12..69
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 69..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 75..80
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 155..170
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 69..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK7"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT DISULFID 12..108
FT /evidence="ECO:0000250|UniProtKB:P51859"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P51858"
SQ SEQUENCE 239 AA; 26604 MW; 6EA42D4D2FBDAF9E CRC64;
MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP
KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY QSSQKKSCVE EPEPEPEATE
GDGDKKGNAE GSSDEEGKLV IDEPTKEKNE KGALKRRAGD LLEDSPKRPK EAEDLEGEEK
EGATLEGERP LPVEAEKNST PSEPGSGRGP PQEEEEEEEE EEAAKEDAEA PGLRDHESL
