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

 HIF1A_RAT               Reviewed;         825 AA.
O35800; Q9WTU9;
03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
12-SEP-2018, entry version 171.
RecName: Full=Hypoxia-inducible factor 1-alpha;
Short=HIF-1-alpha;
Short=HIF1-alpha;
Name=Hif1a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Hepatocyte;
PubMed=11237857; DOI=10.1042/0264-6021:3540531;
Kietzmann T., Cornesse Y., Brechtel K., Modaressi S., Jungermann K.;
"Perivenous expression of the mRNA of the three hypoxia-inducible
factor a-subunits HIF-1a, HIF2a and HIF3a in rat liver.";
Biochem. J. 354:531-537(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=11526200;
Zou A.-P., Yang Z.-Z., Li P.-L., Cowley A.W. Jr.;
"Oxygen-dependent expression of hypoxia-inducible factor-1alpha in
renal medullary cells of rats.";
Physiol. Genomics 6:159-168(2001).
-!- 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 bi nding
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. Nucleus speckle {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}.
-!- TISSUE SPECIFICITY: Expressed in the kidney, higher expression is
seen in the renal medulla than in the cortex. Expressed also in
the perivenous zone of the liver.
-!- 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-799 may be responsible for increased
recruitment of p300 coactivator necessary for transcriptional
activity of HIF-1 complex. {ECO:0000250}.
-!- PTM: Acetylation of Lys-531 by ARD1 increases interaction with VHL
and stimulates subsequent proteasomal degradation. Deacetylated 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-563 in the
oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and
EGLN2/PHD1. EGLN3/PHD3 has also been shown to hydroxylate Pro-563.
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-802 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; Y09507; CAA70701.1; -; mRNA.
EMBL; AF057308; AAD24413.1; -; mRNA.
PIR; JC5809; JC5809.
RefSeq; NP_077335.1; NM_024359.1.
UniGene; Rn.10852; -.
ProteinModelPortal; O35800; -.
SMR; O35800; -.
BioGrid; 248194; 6.
IntAct; O35800; 1.
MINT; O35800; -.
STRING; 10116.ENSRNOP00000042230; -.
PhosphoSitePlus; O35800; -.
PaxDb; O35800; -.
PRIDE; O35800; -.
GeneID; 29560; -.
KEGG; rno:29560; -.
UCSC; RGD:61928; rat.
CTD; 3091; -.
RGD; 61928; Hif1a.
eggNOG; KOG3558; Eukaryota.
eggNOG; ENOG410YK57; LUCA.
HOGENOM; HOG000234306; -.
HOVERGEN; HBG060456; -.
InParanoid; O35800; -.
KO; K08268; -.
PRO; PR:O35800; -.
Proteomes; UP000002494; Unplaced.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
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; IDA:RGD.
GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
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; IDA:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0006953; P:acute-phase response; IEP:RGD.
GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
GO; GO:0071245; P:cellular response to carbon monoxide; IEP:RGD.
GO; GO:0071279; P:cellular response to cobalt ion; IEP:RGD.
GO; GO:1903928; P:cellular response to cyanide; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071257; P:cellular response to electrical stimulus; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IMP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071482; P:cellular response to light stimulus; IEP:RGD.
GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071250; P:cellular response to nitrite; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0097237; P:cellular response to toxic substance; IEP:RGD.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0045793; P:positive regulation of cell size; IEP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
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:1900037; P:regulation of cellular response to hypoxia; IEP:RGD.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0043279; P:response to alkaloid; IEP:RGD.
GO; GO:0072347; P:response to anesthetic; IEP:RGD.
GO; GO:0010996; P:response to auditory stimulus; IEP:RGD.
GO; GO:0032025; P:response to cobalt ion; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0060992; P:response to fungicide; IMP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0014074; P:response to purine-containing compound; IEP:RGD.
GO; GO:0009651; P:response to salt stress; IEP:RGD.
GO; GO:0010165; P:response to X-ray; IEP:RGD.
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; IPR013655; PAS_fold_3.
Pfam; PF11413; HIF-1; 1.
Pfam; PF08778; HIF-1a_CTAD; 1.
Pfam; PF08447; PAS_3; 1.
Pfam; PF13426; PAS_9; 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 1 825 Hypoxia-inducible factor 1-alpha.
/FTId=PRO_0000127222.
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 401 602 ODD.
REGION 530 574 NTAD.
REGION 575 784 ID.
REGION 785 825 CTAD.
MOTIF 717 721 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 531 531 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 550 550 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 554 554 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 563 563 4-hydroxyproline.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 575 575 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 588 588 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 657 657 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 799 799 S-nitrosocysteine.
{ECO:0000250|UniProtKB:Q16665}.
MOD_RES 802 802 (3S)-3-hydroxyasparagine. {ECO:0000250}.
CROSSLNK 531 531 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q16665}.
CROSSLNK 537 537 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q16665}.
CROSSLNK 546 546 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q16665}.
CONFLICT 12 12 K -> NR (in Ref. 2; AAD24413).
{ECO:0000305}.
CONFLICT 74 74 D -> G (in Ref. 2; AAD24413).
{ECO:0000305}.
CONFLICT 96 96 P -> L (in Ref. 2; AAD24413).
{ECO:0000305}.
CONFLICT 329 329 D -> N (in Ref. 2; AAD24413).
{ECO:0000305}.
CONFLICT 613 619 ATATTAT -> TATA (in Ref. 2; AAD24413).
{ECO:0000305}.
CONFLICT 708 708 R -> K (in Ref. 2; AAD24413).
{ECO:0000305}.
SEQUENCE 825 AA; 92319 MW; C4109A57F38667E9 CRC64;
MEGAGGENEK KKMSSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM
RLTISYLRVR KLLDAGDLDI EDEMKAQMNC FYLKAPDGFV MVLTDDGDMI YISDNVNKYM
GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGPVRKGKE QNTQRSFFLR MKCTLTSRGR
TMNIKSATWK VLHCTGHIHV YDTSSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK
TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
TTGQYRMLAK RGGYVWVETQ ATVIYNTKDS QPQCIVCVNY VVSGIIQHDL IFSLQQTESV
LKPVESSDMK MTQLFTKVES EDTSCLFDKL KKEPDALTLL APAAGDTIIS LDFGSDDTET
EDQQLEDVPL YNDVMFPSSN EKLNINLAMS PLPASETPKP LRSSADPALN QEVALKLESS
PESLGLSFTM PQIQDQPASP SDGSTRQSSP EPNSPSEYCF DVDSDMVNVF KLELVEKLFA
EDTEAKNPFS AQDTDLDLEM LAPYIPMDDD FQLRSFDQLS PLESNSPSPP SVSTVTGFQQ
TQLQKPTITV TAATATTATT TDESKAVTKD NIEDIKILIA SPPSTQVPQE MTTAKASAYS
GTHSRTASPD RAGKRVIEKT DKAHPRSLNL SVTLNQRNTV PEEELNPRTI ALQNAQRKRK
MEHDGSLFQA AGIGTLLQQP GDRAPTMSLS WKRVKGYISS EQDGMEQKTI FLIPSDLACR
LLGQSMDESG LPQLTSYDCE VNAPIQGSRN LLQGEELLRA LDQVN


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