PSIP1_CHICK
ID PSIP1_CHICK Reviewed; 579 AA.
AC Q5XXA9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Lens epithelium-derived growth factor;
GN Name=PSIP1; Synonyms=LEDGF;
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].
RX PubMed=15371438; DOI=10.1074/jbc.m406307200;
RA Cherepanov P., Devroe E., Silver P.A., Engelman A.;
RT "Identification of an evolutionarily conserved domain in human lens
RT epithelium-derived growth factor/transcriptional co-activator p75
RT (LEDGF/p75) that binds HIV-1 integrase.";
RL J. Biol. Chem. 279:48883-48892(2004).
CC -!- FUNCTION: Transcriptional coactivator involved in neuroepithelial stem
CC cell differentiation and neurogenesis. Involved in particular in lens
CC epithelial cell gene regulation and stress responses. May play an
CC important role in lens epithelial to fiber cell terminal
CC differentiation. May play a protective role during stress-induced
CC apoptosis (By similarity). {ECO:0000250|UniProtKB:O75475}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75475}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; AY728140; AAU44349.1; -; mRNA.
DR RefSeq; NP_001026781.2; NM_001031610.2.
DR AlphaFoldDB; Q5XXA9; -.
DR SMR; Q5XXA9; -.
DR STRING; 9031.ENSGALP00000024326; -.
DR PaxDb; Q5XXA9; -.
DR PRIDE; Q5XXA9; -.
DR GeneID; 431605; -.
DR KEGG; gga:431605; -.
DR CTD; 11168; -.
DR VEuPathDB; HostDB:geneid_431605; -.
DR eggNOG; KOG1904; Eukaryota.
DR InParanoid; Q5XXA9; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; Q5XXA9; -.
DR PRO; PR:Q5XXA9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0097100; F:supercoiled DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; 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; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..579
FT /note="Lens epithelium-derived growth factor"
FT /id="PRO_0000191711"
FT DOMAIN 1..64
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..464
FT /note="Integrase-binding domain (IBD)"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT REGION 492..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 347..442
FT /evidence="ECO:0000255"
FT MOTIF 186..196
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT COMPBIAS 62..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 64927 MW; 817D2037951C1A8D CRC64;
MSRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKM PIFFFGTHET AFLGPKDIFP
YSENKDKYGK PNKRKGFNEG LWEIDNNPKV KFSHQPSHPA VNTSIKETIQ ESSPEAAEGS
EEKSGAKRRK PSIPKLPPKG DNNSPAEAEA EEKEMHSTKE DEEPSEKNSK EGVVKTNDAS
IPKVARRGRK RKAEKQAESE EAAVVATAAV VAAAAAPVTV SPKVSPKRGR PAVSEVKVPK
PRGRPKLVKP SCLSESDPVN EEEKAKKKGP DEKPKKQGKK DEEGQKEEEK PKKEYDKKDG
KKEAEPKRKN AAKLGSASAS DSEDEGGEEE GDKKKKGGRS FQSTHRRNIM RGQHEKEVTE
RKRKQEEQGE SELQNKEEGK KTEVKKMEKK RETSMDSRLQ RIHAEIKNSL KIDNLDVNRC
IEALDELASL QVSMQQAQKH TEMILTLKKI RKFKVSQVIM EKSTMLYNKF KTMFLVGEGD
SVLSQVLNKS LAEQKQHEEA NKTKEQWKKG TNKKNEKEKD QTGSKIVNGG SETQDTNQSQ
HNGENAEEKD KLEVASKKKT CGEESELEKP AKESAFENK
