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

 HIF1A_BOVIN             Reviewed;         823 AA.
Q9XTA5;
03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
18-JUL-2018, entry version 150.
RecName: Full=Hypoxia-inducible factor 1-alpha;
Short=HIF-1-alpha;
Short=HIF1-alpha;
Name=HIF1A;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Artery;
PubMed=10320777; DOI=10.1016/S0167-4781(99)00048-2;
Hara S., Kobayashi C., Imura N.;
"Molecular cloning of cDNAs encoding hypoxia-inducible factor (HIF)-
1alpha and -2alpha of bovine arterial endothelial cells.";
Biochim. Biophys. Acta 1445:237-243(1999).
-!- 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.
Heterodimerizes with ARNT; heterodimer binds to core DNA sequence
5'-TACGTG-3' within the hypoxia response element (HRE) of target
gene promoters (By similarity). 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,
ECO:0000250|UniProtKB:Q61221}.
-!- SUBUNIT: Interacts with COPS5 subunit of COP9 signalosome complex,
leading to the regulation of its stability. Interacts with the
ARNT; forms a heterodimer that binds core DNA sequence 5'-TACGTG-
3' within the hypoxia response element (HRE) of target gene
promoters (By similarity). 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. Interaction with
PSMA7 inhibits the transactivation activity of HIF1A under both
normoxic and hypoxia-mimicking conditions. 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|UniProtKB:Q16665}.
Nucleus {ECO:0000250|UniProtKB:Q61221}. Note=Colocalizes with
HIF3A in the nucleus and speckles (By similarity). Cytoplasmic in
normoxia, nuclear translocation in response to hypoxia (By
similarity). {ECO:0000250|UniProtKB:Q16665,
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-797 may be responsible for increased
recruitment of p300 coactivator necessary for transcriptional
activity of HIF-1 complex. {ECO:0000250}.
-!- PTM: Acetylation of Lys-532 by ARD1 increases interaction with VHL
and stimulates subsequent proteasomal degradation. Deacetylation
of Lys-706 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-247 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-402 and Pro-564 in the
oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and
EGLN2/PHD1. EGLN3/PHD3 has also been shown to hydroxylate Pro-564.
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-800 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; AB018398; BAA78675.1; -; mRNA.
UniGene; Bt.4184; -.
ProteinModelPortal; Q9XTA5; -.
SMR; Q9XTA5; -.
STRING; 9913.ENSBTAP00000027885; -.
PaxDb; Q9XTA5; -.
PRIDE; Q9XTA5; -.
eggNOG; KOG3558; Eukaryota.
eggNOG; ENOG410YK57; LUCA.
HOGENOM; HOG000234306; -.
HOVERGEN; HBG060456; -.
InParanoid; Q9XTA5; -.
Proteomes; UP000009136; Unplaced.
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; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; 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:0010575; P:positive regulation of vascular endothelial growth factor production; 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; Complete proteome; Cytoplasm; DNA-binding;
Hydroxylation; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; S-nitrosylation; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 823 Hypoxia-inducible factor 1-alpha.
/FTId=PRO_0000127219.
DOMAIN 17 70 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 85 158 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 228 298 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 302 345 PAC.
REGION 1 401 Interaction with TSGA10. {ECO:0000250}.
REGION 21 30 DNA-binding.
{ECO:0000250|UniProtKB:Q61221}.
REGION 170 191 Required for heterodimer formation with
ARNT. {ECO:0000250|UniProtKB:Q61221}.
REGION 401 600 ODD.
REGION 531 575 NTAD.
REGION 576 782 ID.
REGION 783 823 CTAD.
MOTIF 715 721 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 247 247 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 402 402 4-hydroxyproline. {ECO:0000250}.
MOD_RES 532 532 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 551 551 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 555 555 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 564 564 4-hydroxyproline.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 576 576 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 589 589 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 654 654 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 706 706 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 797 797 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 800 800 (3S)-3-hydroxyasparagine. {ECO:0000250}.
CROSSLNK 532 532 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q16665}.
CROSSLNK 538 538 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q16665}.
CROSSLNK 547 547 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q16665}.
SEQUENCE 823 AA; 92128 MW; 12674E467A61B1A1 CRC64;
MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM
RLTISYLRVR KLLDAGDLDI EDEMKAQMNC FYLKALDGFV MVLTDDGDMI YISDNVNKYM
GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGLVKKGKE QNTQRSFFLR MKCTLTSRGR
TMNIKSATWK VLHCTGHIHV YDTNSNQSQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK
TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
TTGQYRMLAK RGGYVWIETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL IFSLQQTECV
LKPVESSDMK MTQLFTKVES EDTSSLFDKL KKEPDALTLL APAAGDTIIS LDFGSNDTET
DDQQLEEVPL YNDVMLPSSN EKLQNINLAM SPLPASETPK PLRSSADPAL NQEVALKLEP
NPESLELSFT MPQIQDQPAS PSDGSTRQSS PEPNSPSEYC FDVDSDMVNE FKLELVEKLF
AEDTEAKNPF STQDTDLDLE MLAPYIPMDD DFQLRSFDQL SPLENSSTSP QSASTNTVFQ
PTQMQKPPIA TVTTTATSDE LKTVTKDGME DIKILIAFPS PPHVPKEPPC ATTSPYSDTG
SRTASPNRAG KGVIEQTEKS HPRSPNVLSV ALSQRTTAPE EELNPKILAL QNAQRKRKIE
HDGSLFQAVG IGTLLQQPDD RATTTSLSWK RVKGCKSSEQ NGMEQKTIIL IPSDLACRLL
GQSMDESGLP QLTSYDCEVN APIQGSRNLL QGEELLRALD QVN


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