HIF1_CAEEL
ID HIF1_CAEEL Reviewed; 719 AA.
AC G5EGD2; G5ECE6; G5EDZ3; G5EE28; Q8I4D0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Hypoxia-inducible factor 1 {ECO:0000303|PubMed:11427734, ECO:0000303|PubMed:12006646};
DE AltName: Full=Hypoxia-induced factor 1 {ECO:0000303|PubMed:12006646, ECO:0000312|EMBL:AAK62778.1};
GN Name=hif-1 {ECO:0000312|EMBL:CCD31074.1, ECO:0000312|WormBase:F38A6.3a};
GN ORFNames=F38A6.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK62778.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH AHA-1,
RP TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11427734; DOI=10.1073/pnas.141234698;
RA Jiang H., Guo R., Powell-Coffman J.A.;
RT "The Caenorhabditis elegans hif-1 gene encodes a bHLH-PAS protein that is
RT required for adaptation to hypoxia.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7916-7921(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB07380.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH VHL-1, HYDROXYLATION AT PRO-621, AND MUTAGENESIS OF
RP PRO-621.
RX PubMed=11595184; DOI=10.1016/s0092-8674(01)00507-4;
RA Epstein A.C.R., Gleadle J.M., McNeill L.A., Hewitson K.S., O'Rourke J.,
RA Mole D.R., Mukherji M., Metzen E., Wilson M.I., Dhanda A., Tian Y.M.,
RA Masson N., Hamilton D.L., Jaakkola P., Barstead R., Hodgkin J.,
RA Maxwell P.H., Pugh C.W., Schofield C.J., Ratcliffe P.J.;
RT "C. elegans EGL-9 and mammalian homologs define a family of dioxygenases
RT that regulate HIF by prolyl hydroxylation.";
RL Cell 107:43-54(2001).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12006646; DOI=10.1091/mbc.01-12-0594;
RA Padilla P.A., Nystul T.G., Zager R.A., Johnson A.C., Roth M.B.;
RT "Dephosphorylation of cell cycle-regulated proteins correlates with anoxia-
RT induced suspended animation in Caenorhabditis elegans.";
RL Mol. Biol. Cell 13:1473-1483(2002).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12686697; DOI=10.1152/physiolgenomics.00179.2002;
RA Treinin M., Shliar J., Jiang H., Powell-Coffman J.A., Bromberg Z.,
RA Horowitz M.;
RT "HIF-1 is required for heat acclimation in the nematode Caenorhabditis
RT elegans.";
RL Physiol. Genomics 14:17-24(2003).
RN [6]
RP FUNCTION.
RX PubMed=15781453; DOI=10.1074/jbc.m501894200;
RA Shen C., Nettleton D., Jiang M., Kim S.K., Powell-Coffman J.A.;
RT "Roles of the HIF-1 hypoxia-inducible factor during hypoxia response in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 280:20580-20588(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16091039; DOI=10.1111/j.1365-2958.2005.04739.x;
RA Anyanful A., Dolan-Livengood J.M., Lewis T., Sheth S., Dezalia M.N.,
RA Sherman M.A., Kalman L.V., Benian G.M., Kalman D.;
RT "Paralysis and killing of Caenorhabditis elegans by enteropathogenic
RT Escherichia coli requires the bacterial tryptophanase gene.";
RL Mol. Microbiol. 57:988-1007(2005).
RN [8]
RP FUNCTION.
RX PubMed=18477695; DOI=10.1073/pnas.0802164105;
RA Chang A.J., Bargmann C.I.;
RT "Hypoxia and the HIF-1 transcriptional pathway reorganize a neuronal
RT circuit for oxygen-dependent behavior in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7321-7326(2008).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19461873; DOI=10.1371/journal.pgen.1000486;
RA Chen D., Thomas E.L., Kapahi P.;
RT "HIF-1 modulates dietary restriction-mediated lifespan extension via IRE-1
RT in Caenorhabditis elegans.";
RL PLoS Genet. 5:E1000486-E1000486(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21093262; DOI=10.1016/j.cub.2010.10.057;
RA Lee S.J., Hwang A.B., Kenyon C.;
RT "Inhibition of respiration extends C. elegans life span via reactive oxygen
RT species that increase HIF-1 activity.";
RL Curr. Biol. 20:2131-2136(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19889840; DOI=10.1091/mbc.e09-03-0199;
RA Budde M.W., Roth M.B.;
RT "Hydrogen sulfide increases hypoxia-inducible factor-1 activity
RT independently of von Hippel-Lindau tumor suppressor-1 in C. elegans.";
RL Mol. Biol. Cell 21:212-217(2010).
RN [12]
RP FUNCTION.
RX PubMed=20520707; DOI=10.1038/nature09141;
RA Sendoel A., Kohler I., Fellmann C., Lowe S.W., Hengartner M.O.;
RT "HIF-1 antagonizes p53-mediated apoptosis through a secreted neuronal
RT tyrosinase.";
RL Nature 465:577-583(2010).
RN [13]
RP FUNCTION.
RX PubMed=20400959; DOI=10.1038/nn.2537;
RA Pocock R., Hobert O.;
RT "Hypoxia activates a latent circuit for processing gustatory information in
RT C. elegans.";
RL Nat. Neurosci. 13:610-614(2010).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20865124; DOI=10.1371/journal.ppat.1001075;
RA Shao Z., Zhang Y., Ye Q., Saldanha J.N., Powell-Coffman J.A.;
RT "C. elegans SWAN-1 Binds to EGL-9 and regulates HIF-1-mediated resistance
RT to the bacterial pathogen Pseudomonas aeruginosa PAO1.";
RL PLoS Pathog. 6:E1001075-E1001075(2010).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21241450; DOI=10.1111/j.1474-9726.2011.00672.x;
RA Leiser S.F., Begun A., Kaeberlein M.;
RT "HIF-1 modulates longevity and healthspan in a temperature-dependent
RT manner.";
RL Aging Cell 10:318-326(2011).
RN [16]
RP FUNCTION, INDUCTION BY IRON, AND DISRUPTION PHENOTYPE.
RX PubMed=22194696; DOI=10.1371/journal.pgen.1002394;
RA Romney S.J., Newman B.S., Thacker C., Leibold E.A.;
RT "HIF-1 regulates iron homeostasis in Caenorhabditis elegans by activation
RT and inhibition of genes involved in iron uptake and storage.";
RL PLoS Genet. 7:E1002394-E1002394(2011).
RN [17]
RP FUNCTION.
RX PubMed=22396654; DOI=10.1371/journal.pgen.1002498;
RA Ackerman D., Gems D.;
RT "Insulin/IGF-1 and hypoxia signaling act in concert to regulate iron
RT homeostasis in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002498-E1002498(2012).
RN [18]
RP FUNCTION.
RX PubMed=22792069; DOI=10.1371/journal.ppat.1002798;
RA Luhachack L.G., Visvikis O., Wollenberg A.C., Lacy-Hulbert A., Stuart L.M.,
RA Irazoqui J.E.;
RT "EGL-9 controls C. elegans host defense specificity through prolyl
RT hydroxylation-dependent and -independent HIF-1 pathways.";
RL PLoS Pathog. 8:E1002798-E1002798(2012).
CC -!- FUNCTION: A transcription factor which is a key regulator in various
CC cellular processes; including environment stress resistance (oxygen
CC levels, hydrogen sulfide and cyanide levels and heat), negative
CC regulation of cell apoptosis in ASJ neurons by inhibition of cep-1 via
CC transcriptional activation of tyr-2, resistance/susceptibility to
CC pathogenic bacteria, lifespan and brood size (PubMed:11427734,
CC PubMed:12006646, PubMed:12686697, PubMed:15781453, PubMed:18477695,
CC PubMed:19461873, PubMed:21093262, PubMed:19889840, PubMed:20520707,
CC PubMed:20400959). Involved in mediating susceptibility to
CC enteropathogenic E.coli (PubMed:16091039). Increased levels of hif-1
CC activity confer resistance to P.aeruginosa-mediated death but also
CC confer susceptibility to S.aureus infection (PubMed:20865124,
CC PubMed:22792069). Required for aha-1 nuclear localization
CC (PubMed:11427734). Following hypoxic stress, up-regulates serotonin
CC levels through activation of tph-1 expression (PubMed:20400959). Role
CC in life span extension is dependent of temperature (PubMed:21241450).
CC Not required for survival in anoxic conditions (PubMed:11427734).
CC Involved in iron homeostasis by repressing transcription of ferritin
CC ftn-1 and ftn-2, and divalent metal transporter smf-3 (PubMed:22396654,
CC PubMed:22194696). May be involved in manganese homeostasis by
CC repressing divalent metal transporter smf-3 (PubMed:22194696).
CC {ECO:0000269|PubMed:11427734, ECO:0000269|PubMed:12006646,
CC ECO:0000269|PubMed:12686697, ECO:0000269|PubMed:15781453,
CC ECO:0000269|PubMed:16091039, ECO:0000269|PubMed:18477695,
CC ECO:0000269|PubMed:19461873, ECO:0000269|PubMed:19889840,
CC ECO:0000269|PubMed:20400959, ECO:0000269|PubMed:20520707,
CC ECO:0000269|PubMed:20865124, ECO:0000269|PubMed:21093262,
CC ECO:0000269|PubMed:21241450, ECO:0000269|PubMed:22194696,
CC ECO:0000269|PubMed:22396654, ECO:0000269|PubMed:22792069}.
CC -!- SUBUNIT: Binds to aha-1 (PubMed:11427734). Interacts (hydroxylated on
CC Pro-621) with vhl-1; the interaction induces hif-1 degradation
CC (PubMed:11595184). {ECO:0000269|PubMed:11427734,
CC ECO:0000269|PubMed:11595184}.
CC -!- INTERACTION:
CC G5EGD2; O02219: aha-1; NbExp=3; IntAct=EBI-319821, EBI-2408984;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:19889840}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=a {ECO:0000269|PubMed:11427734};
CC IsoId=G5EGD2-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=G5EGD2-2; Sequence=VSP_043009;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=G5EGD2-3; Sequence=VSP_043005, VSP_043007;
CC Name=d {ECO:0000269|PubMed:9851916};
CC IsoId=G5EGD2-4; Sequence=VSP_043008;
CC Name=e {ECO:0000269|PubMed:9851916};
CC IsoId=G5EGD2-5; Sequence=VSP_043006;
CC -!- TISSUE SPECIFICITY: Expressed in all somatic cells.
CC {ECO:0000269|PubMed:11427734, ECO:0000269|PubMed:19461873}.
CC -!- INDUCTION: By heat acclimation, hypoxia and addition of 50 ppm hydrogen
CC sulfide (PubMed:11427734, PubMed:12686697, PubMed:19889840). By low
CC iron levels (PubMed:22194696). {ECO:0000269|PubMed:11427734,
CC ECO:0000269|PubMed:12686697, ECO:0000269|PubMed:19889840,
CC ECO:0000269|PubMed:22194696}.
CC -!- PTM: Hydroxylation on Pro-621 by egl-9 during normoxia conditions is
CC required for vhl-1-mediated proteasomal degradation.
CC {ECO:0000269|PubMed:11595184}.
CC -!- DISRUPTION PHENOTYPE: 66% do not survive embryogenesis when cultured in
CC hypoxic conditions of 1% oxygen. Able to survive anoxic conditions
CC (PubMed:11427734, PubMed:12006646). Inefficient translocation of aha-1
CC to the nucleus (PubMed:11427734). Inability to acclimate to heat
CC (PubMed:12686697). Partial resistance to paralysis and killing by
CC enteropathogenic E.coli and P.aeruginosa (PubMed:16091039,
CC PubMed:20865124). Extends lifespan in a temperature dependent manner
CC but not when grown with a restricted diet (PubMed:19461873,
CC PubMed:21093262). At lower temperatures impairs lifespan because of a
CC vulval integrity defect (PubMed:21241450). Unable to survive in even
CC relatively low concentrations of hydrogen sulfide (PubMed:19889840).
CC Reduced body levels of Mn(2+) and iron (PubMed:22194696). In low iron
CC conditions, only 20% of animals reach the L4 larval stage
CC (PubMed:22194696). RNAi-mediated knockdown causes an increase in ftn-1
CC and ftn-2 mRNA levels in normal conditions and prevents the repression
CC of smf-3, ftn-1 and to a lesser extent ftn-2 mRNA transcription in
CC response to low iron levels (PubMed:22194696).
CC {ECO:0000269|PubMed:11427734, ECO:0000269|PubMed:12006646,
CC ECO:0000269|PubMed:12686697, ECO:0000269|PubMed:16091039,
CC ECO:0000269|PubMed:19461873, ECO:0000269|PubMed:19889840,
CC ECO:0000269|PubMed:20865124, ECO:0000269|PubMed:21093262,
CC ECO:0000269|PubMed:21241450, ECO:0000269|PubMed:22194696}.
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DR EMBL; AF364604; AAK62778.1; -; mRNA.
DR EMBL; Z92833; CAB07380.2; -; Genomic_DNA.
DR EMBL; AL023842; CAB07380.2; JOINED; Genomic_DNA.
DR EMBL; Z92833; CAB07381.2; -; Genomic_DNA.
DR EMBL; AL023842; CAB07381.2; JOINED; Genomic_DNA.
DR EMBL; AL023842; CAD54167.1; -; Genomic_DNA.
DR EMBL; Z92833; CAD54141.2; -; Genomic_DNA.
DR EMBL; AL023842; CAD54141.2; JOINED; Genomic_DNA.
DR EMBL; Z92833; CCD31074.1; -; Genomic_DNA.
DR EMBL; AL023842; CCD31074.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001023891.2; NM_001028720.3. [G5EGD2-2]
DR RefSeq; NP_001023892.1; NM_001028721.2. [G5EGD2-3]
DR RefSeq; NP_001023893.1; NM_001028722.3.
DR RefSeq; NP_001023894.2; NM_001028723.2. [G5EGD2-5]
DR RefSeq; NP_508008.4; NM_075607.5. [G5EGD2-1]
DR AlphaFoldDB; G5EGD2; -.
DR SMR; G5EGD2; -.
DR BioGRID; 45316; 57.
DR ELM; G5EGD2; -.
DR IntAct; G5EGD2; 51.
DR MINT; G5EGD2; -.
DR STRING; 6239.F38A6.3b; -.
DR EPD; G5EGD2; -.
DR PaxDb; G5EGD2; -.
DR EnsemblMetazoa; F38A6.3a.1; F38A6.3a.1; WBGene00001851. [G5EGD2-1]
DR EnsemblMetazoa; F38A6.3b.1; F38A6.3b.1; WBGene00001851. [G5EGD2-2]
DR EnsemblMetazoa; F38A6.3c.1; F38A6.3c.1; WBGene00001851. [G5EGD2-3]
DR EnsemblMetazoa; F38A6.3d.1; F38A6.3d.1; WBGene00001851. [G5EGD2-4]
DR EnsemblMetazoa; F38A6.3e.1; F38A6.3e.1; WBGene00001851. [G5EGD2-5]
DR GeneID; 180359; -.
DR KEGG; cel:CELE_F38A6.3; -.
DR UCSC; F38A6.3a; c. elegans.
DR CTD; 180359; -.
DR WormBase; F38A6.3a; CE38182; WBGene00001851; hif-1. [G5EGD2-1]
DR WormBase; F38A6.3b; CE42263; WBGene00001851; hif-1. [G5EGD2-2]
DR WormBase; F38A6.3c; CE32019; WBGene00001851; hif-1. [G5EGD2-3]
DR WormBase; F38A6.3d; CE38181; WBGene00001851; hif-1. [G5EGD2-4]
DR WormBase; F38A6.3e; CE46300; WBGene00001851; hif-1. [G5EGD2-5]
DR eggNOG; KOG3558; Eukaryota.
DR GeneTree; ENSGT00940000174266; -.
DR InParanoid; G5EGD2; -.
DR OMA; WLFRDQP; -.
DR OrthoDB; 469209at2759; -.
DR Reactome; R-CEL-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-8951664; Neddylation.
DR SignaLink; G5EGD2; -.
DR PRO; PR:G5EGD2; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001851; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; G5EGD2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0061433; P:cellular response to caloric restriction; IMP:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0048678; P:response to axon injury; IMP:WormBase.
DR GO; GO:0001666; P:response to hypoxia; IMP:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR Pfam; PF00989; PAS; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; DNA-binding; Hydroxylation; Nucleus;
KW Reference proteome; Repeat; Repressor; Stress response; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..719
FT /note="Hypoxia-inducible factor 1"
FT /id="PRO_0000416938"
FT DOMAIN 11..65
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 86..153
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 222..292
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 296..340
FT /note="PAC"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 621
FT /note="4-hydroxyproline; by egl-9"
FT /evidence="ECO:0000269|PubMed:11595184"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043005"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043006"
FT VAR_SEQ 217..226
FT /note="TTNANASAMT -> MSRDSEYLDR (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043007"
FT VAR_SEQ 415..719
FT /note="ARKNSYDDVLQWLFRDQPSSPPPARYRSADRFRTTEPSNFGSALASPDFMDS
FT SSRTSRPKTSYGRRAQSQGSRTTGSSSTSASATLPHSANYSPLAEGISQCGLNSPPSIK
FT SGQVVYGDARSMGRSCDPSDSSRRFSALSPSDTLNVSSTRGINPVIGSNDVFSTMPFAD
FT SIAIAERIDSSPTLTSGEPILCDDLQWEEPDLSCLAPFVDTYDMMQMDEGLPPELQALY
FT DLPDFTPAVPQAPAARPVHIDRSPPAKRMHQSGPSDLDFMYTQHYQPFQQDETYWQGQQ
FT QQNEQQPSSYSPFPMLS -> IYSVTDEYEQRVYGQISAGNDIEDCDMDSDTESIEDSG
FT LAPEFDVDLAPIYNEKMEVDGEDEDGGEEEHVRTATMTFCNGFFATSQALRRRHATGQR
FT TASGQPNRRISVPLWPRRTSWIRHLVPPDRRHHTDEEHKVREVEQLDRLPRQHRPHCHT
FT VPTTRHLQRASHNVDLTVPRVSNLDKSCTETLDLWDVAAIRPIRHDAFPPFHHQILSMC
FT RPLEASTQSSEAMMCSPLCLLPILSPLPKGSIRRQH (in isoform d)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043008"
FT VAR_SEQ 523
FT /note="S -> SCS (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043009"
FT MUTAGEN 621
FT /note="P->G: Loss of egl-9-mediated hydroxylation resulting
FT in the loss of interaction with vhl-1. Normal
FT susceptibility to P.aeruginosa killing."
FT /evidence="ECO:0000269|PubMed:11595184,
FT ECO:0000269|PubMed:20865124"
SQ SEQUENCE 719 AA; 79934 MW; E6F5762100E179FE CRC64;
MEDNRKRNME RRRETSRHAA RDRRSKESDI FDDLKMCVPI VEEGTVTHLD RIALLRVAAT
ICRLRKTAGN VLENNLDNEI TNEVWTEDTI AECLDGFVMI VDSDSSILYV TESVAMYLGL
TQTDLTGRAL RDFLHPSDYD EFDKQSKMLH KPRGEDTDTT GINMVLRMKT VISPRGRCLN
LKSALYKSVS FLVHSKVSTG GHVSFMQGIT IPAGQGTTNA NASAMTKYTE SPMGAFTTRH
TCDMRITFVS DKFNYILKSE LKTLMGTSFY ELVHPADMMI VSKSMKELFA KGHIRTPYYR
LIAANDTLAW IQTEATTITH TTKGQKGQYV ICVHYVLGIQ GAEESLVVCT DSMPAGMQVD
IKKEVDDTRD YIGRQPEIVE CVDFTPLIEP EDPFDTVIEP VVGGEEPVKQ ADMGARKNSY
DDVLQWLFRD QPSSPPPARY RSADRFRTTE PSNFGSALAS PDFMDSSSRT SRPKTSYGRR
AQSQGSRTTG SSSTSASATL PHSANYSPLA EGISQCGLNS PPSIKSGQVV YGDARSMGRS
CDPSDSSRRF SALSPSDTLN VSSTRGINPV IGSNDVFSTM PFADSIAIAE RIDSSPTLTS
GEPILCDDLQ WEEPDLSCLA PFVDTYDMMQ MDEGLPPELQ ALYDLPDFTP AVPQAPAARP
VHIDRSPPAK RMHQSGPSDL DFMYTQHYQP FQQDETYWQG QQQQNEQQPS SYSPFPMLS
