HDGR2_RAT
ID HDGR2_RAT Reviewed; 669 AA.
AC Q925G1; Q5PPH2; Q68G63;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Hepatoma-derived growth factor-related protein 2;
DE Short=HRP-2;
DE AltName: Full=Hepatoma-derived growth factor 3;
DE Short=HDGF-3;
GN Name=Hdgfl2; Synonyms=Hdgf3, Hdgfrp2;
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] (ISOFORM 1).
RA Yu L., Zhang P.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-450; SER-454;
RP THR-609; SER-659 AND SER-661, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=26252862; DOI=10.3892/mmr.2015.4195;
RA Zhuang Z., Mei G., Liu W., Chen Y., Zeng J., Zhang W., Yao G., Wang X.;
RT "Hepatoma-derived growth factor-2 is highly expressed during development
RT and in spinal cord injury.";
RL Mol. Med. Report. 12:6140-6144(2015).
CC -!- FUNCTION: Acts as an epigenetic regulator of myogenesis in cooperation
CC with DPF3a (isoform 2 of DPF3/BAF45C) (By similarity). Associates with
CC the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a
CC activate myogenic genes by increasing chromatin accessibility through
CC recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex)
CC to myogenic gene promoters (By similarity). Promotes the repair of DNA
CC double-strand breaks (DSBs) through the homologous recombination
CC pathway by facilitating the recruitment of the DNA endonuclease RBBP8
CC to the DSBs (By similarity). Preferentially binds to chromatin regions
CC marked by H3K9me3, H3K27me3 and H3K36me2 (By similarity). Involved in
CC cellular growth control, through the regulation of cyclin D1 expression
CC (By similarity). {ECO:0000250|UniProtKB:Q7Z4V5}.
CC -!- SUBUNIT: Interacts with HDGF (By similarity). Interacts with
CC trimethylated 'Lys-36' of histone H3 (H3K36me3). Interacts with
CC trimethylated 'Lys-79' of histone H3 (H3K79me3), but has higher
CC affinity for H3K36me3 (By similarity). Interacts with IWS1 (By
CC similarity). Interacts with H2AX, POGZ, RBBP8 and CBX1 (By similarity).
CC Interacts with histones H3K9me3, H3K27me3 and H3K36me2 (By similarity).
CC Interacts with DPF3a (isoform 2 of DPF3/BAF45C). Interacts with
CC SMARCA4/BRG1/BAF190A, SMARCC1/BAF155 and SMARCD1/BAF60A in a DPF3a-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:Q3UMU9,
CC ECO:0000250|UniProtKB:Q7Z4V5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26252862}. Cytoplasm
CC {ECO:0000269|PubMed:26252862}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q925G1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q925G1-2; Sequence=VSP_031120;
CC -!- TISSUE SPECIFICITY: Expressed in the spinal cord (at protein level)
CC (PubMed:26252862). Primarily restricted to neurons, astrocytes and
CC oligodendrocytes and is particularly expressed in motor neurons of the
CC anterior horn (at protein level) (PubMed:26252862). Significantly up-
CC regulated in the injured spinal cord (at protein level)
CC (PubMed:26252862). {ECO:0000269|PubMed:26252862}.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels in the spinal cord at
CC embryonic day 9, expression remains high at postnatal day 7 (P7),
CC become weak at P14 and is not detectable at two months (at protein
CC level). {ECO:0000269|PubMed:26252862}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; AF355102; AAK50635.1; -; mRNA.
DR EMBL; BC071178; AAH71178.1; -; mRNA.
DR EMBL; BC087695; AAH87695.1; -; mRNA.
DR RefSeq; NP_598232.1; NM_133548.1.
DR RefSeq; XP_006244353.1; XM_006244291.3. [Q925G1-2]
DR AlphaFoldDB; Q925G1; -.
DR SMR; Q925G1; -.
DR IntAct; Q925G1; 1.
DR STRING; 10116.ENSRNOP00000064555; -.
DR iPTMnet; Q925G1; -.
DR jPOST; Q925G1; -.
DR PaxDb; Q925G1; -.
DR PRIDE; Q925G1; -.
DR GeneID; 171073; -.
DR KEGG; rno:171073; -.
DR CTD; 84717; -.
DR RGD; 621013; Hdgfl2.
DR VEuPathDB; HostDB:ENSRNOG00000049142; -.
DR eggNOG; KOG1904; Eukaryota.
DR HOGENOM; CLU_034054_0_0_1; -.
DR InParanoid; Q925G1; -.
DR OMA; DLEMGNA; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; Q925G1; -.
DR PRO; PR:Q925G1; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000049142; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q925G1; baseline and differential.
DR Genevisible; Q925G1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; ISS:UniProtKB.
DR GO; GO:0062072; F:H3K9me3 modified histone binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0042692; P:muscle cell differentiation; ISO:RGD.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; ISO:RGD.
DR CDD; cd05834; HDGF_related; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035496; HDGF-rel_PWWP.
DR InterPro; IPR036218; HIVI-bd_sf.
DR InterPro; IPR021567; LEDGF_IBD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR Pfam; PF11467; LEDGF; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF140576; SSF140576; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; Isopeptide bond; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..669
FT /note="Hepatoma-derived growth factor-related protein 2"
FT /id="PRO_0000317645"
FT DOMAIN 7..64
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 92..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..548
FT /note="Interaction with DPF3/BAF45C isoform 2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT REGION 558..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMU9"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMU9"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMU9"
FT CROSSLNK 550
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT VAR_SEQ 635
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031120"
FT CONFLICT 257
FT /note="S -> A (in Ref. 1; AAK50635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 74018 MW; 64EEA3192CDEE2A0 CRC64;
MPHAFKPGDL VFAKMKGYPH WPARIDDIAD GAVKPPPNKY PIFFFGTHET AFLGPKDLFP
YDKCKDKYGK PNKRKGFNEG LWEIQNNPHA SYSAPLPVSS SDSEAPEADL GGGSDADKEK
EARRVMTVTA VTTTATSGRT ESDSDSDKNS DHSGLKRKTP VLKMSVSKRA RKASSDLDQA
SVSPSEEDSE SPSESEKTSD QDFTPEKKTI ARAPRRAPLG GRKKKKVPSA SDSDSRADSD
GAKEEPVVTA QPSPSSSSSS SSSSASDSDV SIKKPPRGRK PAEKPPPKPR GRRSKPERPP
STSSSDSDSD SGEVDRISEW KRRDEERRRE LEARRRREQE EELRRLREQE REEKERRKER
AERGGSSGEE LEDEEPVKKR SRKARGRGTP SSSDSEPEGE LGKEGKKLAK KSQLQGSESA
RKPGQKEKRG RPDEKPRARP VKVERTRKRS EGLSLDRKGE KKKEPSVEER LQKLHSEIKF
ALKVDNPDVR RCLSALEELG TLQVTSQILQ KNTDVVATLK KIRRYKANKD VMAKAAEVYT
RLKSRVLGPK VEALQKVNKA GAEKERADGE KVEEQPGEQA PRELAEDEPS TDRSAPVNGE
AASQKGENTE DGAQEDGQDL EDGPRGGSSE ELHDSPQDSS DPARPGNEHQ DHERMQLASE
SADDDDEDS
