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Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha)

 HIF1A_EOSFB             Reviewed;         819 AA.
Q309Z6;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
28-MAR-2018, entry version 88.
RecName: Full=Hypoxia-inducible factor 1-alpha;
Short=HIF-1-alpha;
Short=HIF1-alpha;
Name=HIF1A;
Eospalax fontanierii baileyi (Plateau zokor) (Eospalax baileyi).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Spalacidae; Myospalacinae; Eospalax.
NCBI_TaxID=146132;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Chen X.-Q., Xie Z.-Y., Du J.-Z.;
"Cloning of hypoxia-inducible factor 1 alpha from plateau zokor
(Myospalax baileyi).";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Functions as a master transcriptional regulator of the
adaptive response to hypoxia. Under hypoxic conditions, activates
the transcription of over 40 genes, including erythropoietin,
glucose transporters, glycolytic enzymes, vascular endothelial
growth factor, HILPDA, and other genes whose protein products
increase oxygen delivery or facilitate metabolic adaptation to
hypoxia. Plays an essential role in embryonic vascularization,
tumor angiogenesis and pathophysiology of ischemic disease. Binds
to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response
element (HRE) of target gene promoters. Activation requires
recruitment of transcriptional coactivators such as CREBBP and
EP300. Activity is enhanced by interaction with both, NCOA1 or
NCOA2. Interaction with redox regulatory protein APEX seems to
activate CTAD and potentiates activation by NCOA1 and CREBBP.
Involved in the axonal distribution and transport of mitochondria
in neurons during hypoxia (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with COPS5 subunit of COP9 signalosome complex,
leading to the regulation of its stability. Efficient DNA binding
requires heterodimerization of an alpha and a beta/ARNT subunit.
Interacts with NCOA1, NCOA2, APEX, HSP90 and TSGA10. Interacts
with VHL which docks HFA1 to the E3 ubiquitin ligase complex for
subsequent destruction. Interaction, via the ODD domain, with the
beta domain of VHLL, protects HIF1A from destruction by competing
against the destructive targeting initiated by VHL. Interacts with
RORA (via the DNA binding domain); the interaction enhances HIF1A
transcription under hypoxia through increasing protein stability.
Interacts with USP20. Interacts with RACK1; promotes HIF1A
ubiquitination and proteasome-mediated degradation. Interacts with
EP300 (via TAZ-type 1 domain); the interaction is stimulated in
response to hypoxia and inhibited by CITED2. Interacts with CREBBP
(via TAZ-type 1 domain). Interacts (via N-terminus) with USP19.
Interacts with SIRT2. Interacts (deacetylated form) with EGLN1.
Interacts with RWDD3; the interaction enhances HIF1A sumoylation.
Interacts with HIF3A. Interacts with CBFA2T3. Interacts with
HSP90AA1 and HSP90AB1. {ECO:0000250|UniProtKB:Q16665,
ECO:0000250|UniProtKB:Q61221}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250|UniProtKB:Q61221, ECO:0000255|PROSITE-
ProRule:PRU00981}. Nucleus speckle {ECO:0000250|UniProtKB:Q61221}.
Note=Colocalizes with HIF3A in the nucleus and speckles.
Cytoplasmic in normoxia, nuclear translocation in response to
hypoxia. {ECO:0000250|UniProtKB:Q61221}.
-!- DOMAIN: Contains two independent C-terminal transactivation
domains, NTAD and CTAD, which function synergistically. Their
transcriptional activity is repressed by an intervening inhibitory
domain (ID) (By similarity). {ECO:0000250}.
-!- PTM: S-nitrosylation of Cys-793 may be responsible for increased
recruitment of p300 coactivator necessary for transcriptional
activity of HIF-1 complex. {ECO:0000250}.
-!- PTM: Acetylation of Lys-533 by ARD1 increases interaction with VHL
and stimulates subsequent proteasomal degradation. Deacetylation
of Lys-702 by SIRT2 increases its interaction with and
hydroxylation by EGLN1 thereby inactivating HIF1A activity by
inducing its proteasomal degradation (By similarity).
{ECO:0000250}.
-!- PTM: Requires phosphorylation for DNA-binding. Phosphorylation at
Ser-248 by CSNK1D/CK1 represses kinase activity and impairs ARNT
binding. Phosphorylation by GSK3-beta and PLK3 promote degradation
by the proteasome (By similarity). {ECO:0000250}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
asparagine is (S) stereospecific within HIF CTAD domains.
{ECO:0000250}.
-!- PTM: Sumoylated; with SUMO1 under hypoxia. Sumoylation is enhanced
through interaction with RWDD3. Both sumoylation and desumoylation
seem to be involved in the regulation of its stability during
hypoxia. Sumoylation can promote either its stabilization or its
VHL-dependent degradation by promoting hydroxyproline-independent
HIF1A-VHL complex binding, thus leading to HIF1A ubiquitination
and proteasomal degradation. Desumoylation by SENP1 increases its
stability amd transcriptional activity. There is a disaccord
between various publications on the effect of sumoylation and
desumoylation on its stability and transcriptional activity (By
similarity). {ECO:0000250}.
-!- PTM: In normoxia, is hydroxylated on Pro-403 and Pro-565 in the
oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and
EGLN2/PHD1. EGLN3/PHD3 has also been shown to hydroxylate Pro-565.
The hydroxylated prolines promote interaction with VHL, initiating
rapid ubiquitination and subsequent proteasomal degradation.
Deubiquitinated by USP20. Under hypoxia, proline hydroxylation is
impaired and ubiquitination is attenuated, resulting in
stabilization (By similarity). In normoxia, is hydroxylated on
Asn-796 by HIF1AN, thus abrogating interaction with CREBBP and
EP300 and preventing transcriptional activation. Repressed by iron
ion, via Fe(2+) prolyl hydroxylase (PHD) enzymes-mediated
hydroxylation and subsequent proteasomal degradation.
{ECO:0000250|UniProtKB:Q16665}.
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EMBL; DQ229099; ABB17537.1; -; mRNA.
ProteinModelPortal; Q309Z6; -.
SMR; Q309Z6; -.
HOVERGEN; HBG060456; -.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 2.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR001321; HIF-1_alpha.
InterPro; IPR014887; HIF-1_TAD_C.
InterPro; IPR021537; HIF_alpha_subunit.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR013655; PAS_fold_3.
Pfam; PF11413; HIF-1; 1.
Pfam; PF08778; HIF-1a_CTAD; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF08447; PAS_3; 1.
PRINTS; PR01080; HYPOXIAIF1A.
SMART; SM00353; HLH; 1.
SMART; SM00086; PAC; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
TIGRFAMs; TIGR00229; sensory_box; 2.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 2.
2: Evidence at transcript level;
Acetylation; Activator; Cytoplasm; DNA-binding; Hydroxylation;
Isopeptide bond; Nucleus; Phosphoprotein; Repeat; S-nitrosylation;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 819 Hypoxia-inducible factor 1-alpha.
/FTId=PRO_0000254948.
DOMAIN 18 71 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 86 159 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 229 299 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 303 346 PAC.
REGION 1 402 Interaction with TSGA10. {ECO:0000250}.
REGION 402 599 ODD.
REGION 532 576 NTAD.
REGION 577 778 ID.
REGION 779 819 CTAD.
MOTIF 711 717 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 248 248 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 403 403 4-hydroxyproline. {ECO:0000250}.
MOD_RES 533 533 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 552 552 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 556 556 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 565 565 4-hydroxyproline.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 577 577 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 650 650 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 702 702 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 793 793 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 796 796 (3S)-3-hydroxyasparagine. {ECO:0000250}.
CROSSLNK 533 533 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q16665}.
CROSSLNK 539 539 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q16665}.
CROSSLNK 548 548 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q16665}.
SEQUENCE 819 AA; 91660 MW; 5BC90BD0FD279FE8 CRC64;
MEGAAGGEEK KNRMSSERRK EKSRDAARSR RSKESEVFYE LAHQLPLPHN VSSHLDKASV
MRLTISYLRV RKLLDAGDLD IEDDMKAQMN CFYLKALDGF VMVLTDDGDM IYISDNVNKY
MGLTQFELTG HSVFDFTHPC DHEEMREMLT HRNGPIKKGK EQNTQRSFFL RMKCTLTSRG
RTMNIKSATW KVLHCTGHIH VYDTNSNQPQ CGYKKPPMTC LVLICEPIPH PSNIEIPLDS
KTFLSRHSLD MKFSYCDERI TELMGYEPEE LLGRSIYEYY HALDSDHLTK THHDMFTKGQ
VTTGQYRMLA KRGGYVWVET QATVIYNTKN SQPQCIVCVN YVVSGIIQHD LIFSLQQTEC
VLKPVESSDM KMTQLFTKVE SEDTSCLFDK LKKEPDALTL LAPAAGDTII SLDFGSDDTE
TEDQQLEDVP LYNDVMFPSS DDKLTSINLA MSPLPASETP KPLRSNADPA LNQEVALKLE
PNAESLELSF TMPQIQDQPA SPSDGSTRQS SPEPNSPSEY CFDVDSDMVN VFKLELVEKL
FAEDTEAKNP FSTQDTDLDL EMLAPYIPMD DDFQLRSFDQ LSPLESSSPN PPSVSTAFQQ
TQLQEPTITT TTTEELKTVT KDSTEDIKIL ITSPSSTHTP KETTTATTSS PYSGTQSRTA
SPNRAGQGVI EQTEKSHPRS PNVLSVTLSQ RNTVPEEELN PKIIALQNAQ RKRKMEHDGS
LFQAAGIGTL LQQPDDRAPA TSLSWKRVKG CKSSGQNGME QKTIILIPSD LACRLLGQSM
DGSGLPQLTS YDCEVNAPIQ GSRNLLQGEE LLRALDQVN


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