ID A0A1S3SL31_SALSA Unreviewed; 523 AA.
AC A0A1S3SL31;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Lens epithelium-derived growth factor-like isoform X1 {ECO:0000313|RefSeq:XP_014065055.1, ECO:0000313|RefSeq:XP_014065139.1};
GN Name=LOC106610301 {ECO:0000313|RefSeq:XP_014065055.1};
GN Synonyms=LOC106610346 {ECO:0000313|RefSeq:XP_014065139.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014065055.1};
RN [1] {ECO:0000313|RefSeq:XP_014065055.1, ECO:0000313|RefSeq:XP_014065139.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014065055.1,
RC ECO:0000313|RefSeq:XP_014065139.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the HDGF family.
CC {ECO:0000256|ARBA:ARBA00005309}.
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DR RefSeq; XP_014065055.1; XM_014209580.1.
DR RefSeq; XP_014065139.1; XM_014209664.1.
DR STRING; 8030.ENSSSAP00000044500; -.
DR PaxDb; 8030-ENSSSAP00000044500; -.
DR GeneID; 106610301; -.
DR KEGG; sasa:106610301; -.
DR KEGG; sasa:106610346; -.
DR OMA; XPSSEER; -.
DR OrthoDB; 4271850at2759; -.
DR Proteomes; UP000087266; Chromosome ssa08.
DR Bgee; ENSSSAG00000046604; Expressed in ovary and 15 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd20151; PWWP_PSIP; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR InterPro; IPR036218; HIVI-bd_sf.
DR InterPro; IPR021567; LEDGF_IBD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR PANTHER; PTHR12550; HEPATOMA-DERIVED GROWTH FACTOR-RELATED; 1.
DR PANTHER; PTHR12550:SF49; JIL-1 ANCHORING AND STABILIZING PROTEIN, ISOFORM A; 1.
DR Pfam; PF11467; LEDGF; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF140576; HIV integrase-binding domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 7..64
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 88..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 59416 MW; 3487D1CE64CD3959 CRC64;
MARDYKPGDL IFAKMKGYPH WPARINDYSD GAVKPANMKF PIFFFGTHET AFLGPKDIYP
YLPNKEKYAK PNKRKGFNEG LWEVENNPKV ELNGEKQMML SDNVTEKDSD SNPEGDEEGD
YEKRKKPKVS GAESEAGQEE DDEEEEDGGM QVSEQGQPQG QDDPTPKEST DTPKPKRRRK
KKSDVEADSE KEDAANSPTS SPQGGEGPTP KRRGRKTKAE KMLLLQQQDP QGSGSDMDTA
ESERKRKRTP EDKSKRGEEE KRLDGRRKKE DNKGRELEGK KDPDAKRRRQ TKEESSSDSE
DQEKSKGAAG DRKRQHPTLT ETGDKDDRQR RKQDEQKEQN KDNGNKVDER KGDKKKEIST
ESRLQRLHGE IKISLKIDNP DVKKCLVALD ELGMLQVTTQ HLQKHSDLIA TLKKIRRFKA
SQDIMDKSTM LYNKFKSMFL LGEGDQLLSQ VLNKSIAEQK QQEEARKGAQ RKAERARENN
TDNNMNGDSS PDDKKQESDK EKPAEEASTG DNSNVVKAQE EST
//
