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Database: UniProt
Entry: Q5R4G1_PONAB
LinkDB: Q5R4G1_PONAB
Original site: Q5R4G1_PONAB 
ID   Q5R4G1_PONAB            Unreviewed;       827 AA.
AC   Q5R4G1;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=Hypoxia-inducible factor 1-alpha {ECO:0000256|ARBA:ARBA00014446};
GN   Name=DKFZp459N173 {ECO:0000313|EMBL:CAH93355.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|EMBL:CAH93355.1};
RN   [1] {ECO:0000313|EMBL:CAH93355.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cortex {ECO:0000313|EMBL:CAH93355.1};
RG   The German cDNA Consortium;
RA   Wambutt R., Heubner D., Mewes H.W., Weil B., Amid C., Osanger A., Fobo G.,
RA   Han M., Wiemann S.;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
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DR   EMBL; CR861288; CAH93355.1; -; mRNA.
DR   RefSeq; NP_001126975.1; NM_001133503.1.
DR   AlphaFoldDB; Q5R4G1; -.
DR   GeneID; 100173994; -.
DR   KEGG; pon:100173994; -.
DR   CTD; 3091; -.
DR   OrthoDB; 5396877at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0001666; P:response to hypoxia; IEA:UniProt.
DR   CDD; cd19727; bHLH-PAS_HIF1a_PASD8; 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; IPR001321; HIF-1_alpha.
DR   InterPro; IPR014887; HIF-1_CTAD.
DR   InterPro; IPR021537; HIF_alpha-like.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR23043; HYPOXIA-INDUCIBLE FACTOR 1 ALPHA; 1.
DR   PANTHER; PTHR23043:SF7; 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; PF08447; PAS_3; 1.
DR   PRINTS; PR01080; HYPOXIAIF1A.
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   2: Evidence at transcript level;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          18..71
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   DOMAIN          94..149
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          248..299
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         403
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
FT   MOD_RES         565
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
FT   MOD_RES         804
FT                   /note="(3S)-3-hydroxyasparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
SQ   SEQUENCE   827 AA;  92821 MW;  B64FB01E8EFCE232 CRC64;
     MEGAGGANDK KNRISSERRK EKSRDAARSR RSKESEVFYE LAHQLPLPHN VSSHLDKASV
     MRLTISYLRV RKLLDAGDLD IEDEMKAQMN CFYLKALDGF VMVLTDDGDM IYISDNVNKY
     MGLTQFELTG HSVFDFTHPC DHEEMREMLT HRNGPVKKGK EQNTQRSFFL RMKCTLTSRG
     RTMNIKSATW KVLHCTGHIH VYDTNSNQPQ CGYKKPPMTC LVLICEPIPH PSNIEIPLDS
     KTFLSRHSLD MKFSYCDERI TELMGYEPEE LLGRSIYEYY HALDSDHLTK THHDMFTKGQ
     VTTGQYRMLA KRGGYVWVET QATVIYNTKN SQPQCIVCVN YVVSGIIQHD LIFSLQQTEC
     VLKPVESSDM KMTQLFTKVE SEDTSSLFDK LKKEPDALTL LAPAAGDTII SLDFGSNDTE
     TDDQQLEEVP LYNDVMLPSP NEKLQNINLA MSPLPTAETP KPLRSSADPA LNQEVALKLE
     PNPESLELSF TMPQIQDQPP SPSDGSTRQS SPEPNSPSEY CFYVDSDMVN EFKLELVEKL
     FAEDTEAKNP FSTQDTDLDL EMLAPYIPMD DDFQLRSFDQ LSPLESSSAS PESASPQSTV
     TVFQQTQIQE PTANATTTTA TTDELKTVTK DRMEDIKILI ASPSPTHIHK ETTSATSSPY
     RDTQSRTASP NRAGKGVIEQ TEKSHPRSPN VLSVALSQRT TVPEEELNPK ILALQNAQRK
     RKMEHDGSLF QAVGIGTLLQ QPEDHAATTS LSWKRVKGCK SSEQNGMEQK TIILIPSDLA
     CRLLGQSMDE SGLPQLTSYD CEVNAPIQGS RNLLQGEELL RALDQVN
//
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