ID   HDGR2_XENLA             Reviewed;         642 AA.
AC   Q32N87; Q6INX7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Hepatoma-derived growth factor-related protein 2;
DE            Short=HRP-2;
GN   Name=hdgfl2; Synonyms=hdgfrp2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a regulator of myogenesis (By similarity).
CC       Promotes the repair of DNA double-strand breaks (DSBs) through the
CC       homologous recombination pathway by facilitating the recruitment of the
CC       DNA endonuclease RBBP8 to the DSBs (By similarity).
CC       {ECO:0000250|UniProtKB:Q7Z4V5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UMU9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q925G1}.
CC   -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC072145; AAH72145.1; ALT_INIT; mRNA.
DR   EMBL; BC108775; AAI08776.1; -; mRNA.
DR   RefSeq; NP_001085132.1; NM_001091663.1.
DR   AlphaFoldDB; Q32N87; -.
DR   SMR; Q32N87; -.
DR   DNASU; 432209; -.
DR   GeneID; 432209; -.
DR   KEGG; xla:432209; -.
DR   CTD; 432209; -.
DR   Xenbase; XB-GENE-6255752; hdgfl2.L.
DR   OMA; DLEMGNA; -.
DR   OrthoDB; 530959at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 432209; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   Myogenesis; Nucleus; Reference proteome.
FT   CHAIN           1..642
FT                   /note="Hepatoma-derived growth factor-related protein 2"
FT                   /id="PRO_0000317647"
FT   DOMAIN          7..64
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   REGION          87..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          294..342
FT                   /evidence="ECO:0000255"
FT   COILED          595..624
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        87..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..617
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        375
FT                   /note="K -> N (in Ref. 1; AAH72145)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   642 AA;  72379 MW;  3A40B2904E8D0E94 CRC64;
     MPHNFKPGDL VFAKMKGYPH WPARIDDVKD GAVKPPPNKC PIFFYGTHET AFLAPKDLFP
     YDKYKDKYGK PNKRKGFNEG LWEIQNNPQA SYSLPPASVS SSDSDVPEEK STARSDEEEK
     QEASQPILPT ASVSASDEEG SEKEGLKRKE RITTAPSAKR TKHSSSEQEP DSASSSKEEN
     SDSDQDFTPE KNTPRIQRRI TNVGEKNKVL AESESDSKSE SEDEKKELKK SPSSSSASSP
     SLSSSDSETP VKKTPRGRRP AEKPAPKPRG RGRKAEPIPS SDSSDSDSSV DRISEWKKRD
     EERKRELEER RKKEQEEQLR RLREEEREED EKKKREKAEK GDKSDSDSDS SKSEVTAPPK
     PRKSSSSSDS EEDKKQVKEV KPVASEIKKG KKDKVRAISD DSDSDKKVKK TIKKPRPAES
     ARKTNQKEKR GERPRGRPSK VEKEKKKPEM INSRRVVKKE PTVEERLQKL HSEIKFALKV
     DNPDIKKCLD ALEELGGLQV TSQILQKNTD VVATLKKIRR YKANQRVMDK AAEVYSRIKA
     RILGPKSESQ QKIAEKVNTA EKGPEDENQT GKAGEDMDAS MNGDFLSQRT ETAGDKEQEL
     EGLNLDNKAE METKQNNHAE HNNNPTEETF EPRPISSENQ NS