ID W5NAL6_LEPOC Unreviewed; 630 AA.
AC W5NAL6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Hypoxia inducible factor 1 subunit alpha, like {ECO:0000313|Ensembl:ENSLOCP00000017675.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017675.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000017675.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AHAT01029372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01029373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NAL6; -.
DR STRING; 7918.ENSLOCP00000017675; -.
DR Ensembl; ENSLOCT00000017707.1; ENSLOCP00000017675.1; ENSLOCG00000014356.1.
DR eggNOG; KOG3558; Eukaryota.
DR GeneTree; ENSGT00940000166085; -.
DR HOGENOM; CLU_010044_5_0_1; -.
DR InParanoid; W5NAL6; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000014356; Expressed in larva and 13 other cell types or tissues.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR021537; HIF_alpha-like.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR23043; HYPOXIA-INDUCIBLE FACTOR 1 ALPHA; 1.
DR PANTHER; PTHR23043:SF34; HYPOXIA-INDUCIBLE FACTOR 3-ALPHA ISOFORM X1; 1.
DR Pfam; PF11413; HIF-1; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF14598; PAS_11; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 13..66
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 84..148
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 256..303
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 70017 MW; 357B327561A53017 CRC64;
PCGSPPRRPS SELRKVRSRD AARSRRSQET EVFYQLAHTL PLPRRVTSHL DKAAIMRITL
SYMRMSRLFQ AGGLKTDQGE EEEEEEEMDG YLTRALGGFV MVLAPEGDMV YLSESVSKHI
GITQLDLLGQ SVFDFVHPCD QEELRDALTP RAGFSKKQNQ DVPTERSFFI RMKSTLTSRG
RTVNIKSASY KVLHCTGHIH TYKSSGAQEP PADCPALPPQ PLTFLTLLCE PIPHPSNVEF
PLDSSTFLSR HSLDLKFTHC DGRVTELVGY KPEDLIGRSA YEYHHALDSD HLTKSLHTLL
SKGQVTTSHY RFLAKNGGFV WAETQATVIY NGKTSQPEGV VCLNFILRGD QWLSSCSTPF
VFQSSGDESP MDTDSVEKFF AVRKDDDAKP TAAKEVCVQS RHPRVDAGYF LGGSGFTVMT
WDVMSGFAIS HASLPPEKCC KIETRRGSNL YLSCNTLANV ALKDQPGREK MRFLVPNSVF
VLFFPSTGYE ALDLDMLAPY ISMDDDFQLT FLAQLPESEP PTLEPAAPGA RKRTLKMDED
LPLKESSPDK RKRQEEVLLH DVLLGSLVDG DSTDELEQLR LAKSLLNTDD PLVGGERGLC
NSAALMSDLL SRPPDPLTHE LEAGPISPLT
//
