ID F7C9M0_HORSE Unreviewed; 928 AA.
AC F7C9M0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Endothelial PAS domain protein 1 {ECO:0000313|Ensembl:ENSECAP00000012731.4};
GN Name=EPAS1 {ECO:0000313|Ensembl:ENSECAP00000012731.4,
GN ECO:0000313|VGNC:VGNC:17607};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000012731.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000012731.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012731.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000012731.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012731.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; F7C9M0; -.
DR Ensembl; ENSECAT00000015800.4; ENSECAP00000012731.4; ENSECAG00000014594.4.
DR VGNC; VGNC:17607; EPAS1.
DR GeneTree; ENSGT00940000155930; -.
DR HOGENOM; CLU_010044_3_1_1; -.
DR Proteomes; UP000002281; Chromosome 15.
DR Bgee; ENSECAG00000014594; Expressed in chorionic villus and 23 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0002070; P:epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0048625; P:myoblast fate commitment; IEA:Ensembl.
DR GO; GO:0042415; P:norepinephrine metabolic process; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR GO; GO:2000434; P:regulation of protein neddylation; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd19728; bHLH-PAS_HIF2a_PASD2; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR014887; HIF-1_CTAD.
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; 2.
DR PANTHER; PTHR23043:SF8; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR23043; HYPOXIA-INDUCIBLE FACTOR 1 ALPHA; 1.
DR Pfam; PF11413; HIF-1; 1.
DR Pfam; PF08778; HIF-1a_CTAD; 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 Activator {ECO:0000256|ARBA:ARBA00023159};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 71..124
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 149..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 306..357
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 518..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..847
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 462
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
FT MOD_RES 587
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
FT MOD_RES 905
FT /note="(3S)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
SQ SEQUENCE 928 AA; 102877 MW; CBC23C7B86297222 CRC64;
MEIITSCNIH TIISLSKHKE CKNRRNATTG LPHGSANPGF CFWLRAPWDT LGGTIPAVVL
EISPRWSSSE RRKEKSRDAA RCRRSKETEV FYELAHELPL PHSVSSHLDK ASIMRLAISF
LRTHKLLSSV CSENESEAEA DQQMDNLYLK ALEGFIAVVT QDGDMIFLSE NISKFMGLTQ
VELTGHSIFD FTHPCDHEEI RENLSLKNGS GFGKKSKDMS TERDFFMRMK CTVTNRGRTV
NLKSATWKVL HCTGQVKVYN NCPPHNSLCG YKEPLLSCLI IMCEPIQHPS HMDIPLDSKT
FLSRHSMDMK FTYCDDRITE LVGYHPEELL GRSAYEFYHA LDSENMTKSH QNLCTKGQVV
SGQYRMLAKH GGYVWLETQG TVIYNPRNLQ PQCIMCVNYV LSEIEKNDVV FSMDQTESLF
KPHLMAMNGI FDNSGEVAAS EKSNFLFTKL KEEPEELAQL APTAGDAIIS LDFGSQNFEE
SSAYGKAILP PSQPWAGELR SHGTQSEARS LPAFTVPQAA APGSTTPSAS SSSSCSTPSS
PGDYYTSLND DLKIEAIEKL FAMDTEAKDQ CSTHTDFNEL DLETLAPYIP MDGEDFQLSP
ICPEERLLPE NPQSIPQQCF STMTNIFQPL APVDPHRPFL LDKYQQQLES KKIEPEHRPM
SSIFFDGGTK ASLPLCCGQA STPLSSMGGR SNTQWPPDPP LHFGPAKWPV GNQHTESLGA
SPLGPPVTSP HLSMFKKRSA KGFGPRDPDT MSPAMIALSN KLKLKRQLEY EEQAFQDMSG
ADPPGSSASH LMWKRMKSLR GGGNCPLMPD KPLSANVPSD EFTQNPLRGL SQPLRHLPPP
PQPPSAVSPR ENAKSGFPPQ CYAPQYQDYG LPSAHKLSGM ASRLLGPSFE PYLLPELTRY
DCEVNVPVPG SSTLLQGGDL LRALDQAS
//
