GenomeNet

Database: UniProt
Entry: G5EBV0
LinkDB: G5EBV0
Original site: G5EBV0 
ID   EGL9_CAEEL              Reviewed;         723 AA.
AC   G5EBV0; G5ECV8; G5EE79; G5EEP8; Q56W01;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   18-SEP-2019, entry version 63.
DE   RecName: Full=Hypoxia-inducible factor prolyl hydroxylase {ECO:0000250|UniProtKB:Q9GZT9};
DE            Short=HIF-PH {ECO:0000303|PubMed:11595184};
DE            EC=1.14.11.29 {ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:19737748};
DE   AltName: Full=Egg-laying defective protein 9 {ECO:0000312|WormBase:F22E12.4a};
DE   AltName: Full=Hypoxia-inducible factor-proline dioxygenase {ECO:0000305};
GN   Name=egl-9 {ECO:0000312|WormBase:F22E12.4a};
GN   ORFNames=F22E12.4 {ECO:0000312|WormBase:F22E12.4a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|EMBL:AAD56365.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Bristol N2 {ECO:0000303|PubMed:10611362};
RX   PubMed=10611362; DOI=10.1073/pnas.96.26.15202;
RA   Darby C., Cosma C.L., Thomas J.H., Manoil C.;
RT   "Lethal paralysis of Caenorhabditis elegans by Pseudomonas
RT   aeruginosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15202-15207(1999).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS OF HIS-487.
RX   PubMed=19737748; DOI=10.1534/genetics.109.107284;
RA   Shao Z., Zhang Y., Powell-Coffman J.A.;
RT   "Two distinct roles for EGL-9 in the regulation of HIF-1-mediated gene
RT   expression in Caenorhabditis elegans.";
RL   Genetics 183:821-829(2009).
RN   [3] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [4] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=11813735;
RA   Trent C., Tsuing N., Horvitz H.R.;
RT   "Egg-laying defective mutants of the nematode Caenorhabditis
RT   elegans.";
RL   Genetics 104:619-647(1983).
RN   [5] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
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.,
RA   O'Rourke J., Mole D.R., Mukherji M., Metzen E., Wilson M.I.,
RA   Dhanda A., Tian Y.M., Masson N., Hamilton D.L., Jaakkola P.,
RA   Barstead R., Hodgkin J., Maxwell P.H., Pugh C.W., Schofield C.J.,
RA   Ratcliffe P.J.;
RT   "C. elegans EGL-9 and mammalian homologs define a family of
RT   dioxygenases that regulate HIF by prolyl hydroxylation.";
RL   Cell 107:43-54(2001).
RN   [6] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=11591663; DOI=10.1128/jb.183.21.6207-6214.2001;
RA   Gallagher L.A., Manoil C.;
RT   "Pseudomonas aeruginosa PAO1 kills Caenorhabditis elegans by cyanide
RT   poisoning.";
RL   J. Bacteriol. 183:6207-6214(2001).
RN   [7] {ECO:0000305}
RP   FUNCTION.
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   [8] {ECO:0000305}
RP   INDUCTION BY HYPOXIA.
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
RT   in Caenorhabditis elegans.";
RL   J. Biol. Chem. 280:20580-20588(2005).
RN   [9] {ECO:0000305}
RP   FUNCTION.
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   [10] {ECO:0000305}
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   [11] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20011506; DOI=10.1371/journal.ppat.1000689;
RA   Bellier A., Chen C.S., Kao C.Y., Cinar H.N., Aroian R.V.;
RT   "Hypoxia and the hypoxic response pathway protect against pore-forming
RT   toxins in C. elegans.";
RL   PLoS Pathog. 5:E1000689-E1000689(2009).
RN   [12] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19372390; DOI=10.1126/science.1173507;
RA   Mehta R., Steinkraus K.A., Sutphin G.L., Ramos F.J., Shamieh L.S.,
RA   Huh A., Davis C., Chandler-Brown D., Kaeberlein M.;
RT   "Proteasomal regulation of the hypoxic response modulates aging in C.
RT   elegans.";
RL   Science 324:1196-1198(2009).
RN   [13] {ECO:0000305}
RP   FUNCTION, AND INTERACTION WITH SWAN-1.
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
RT   resistance to the bacterial pathogen Pseudomonas aeruginosa PAO1.";
RL   PLoS Pathog. 6:E1001075-E1001075(2010).
RN   [14] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH LIN-10, SUBCELLULAR LOCATION, MUTAGENESIS
RP   OF HIS-487, AND CHARACTERIZATION OF ISOFORMS A; C AND E.
RX   PubMed=22252129; DOI=10.1038/emboj.2011.499;
RA   Park E.C., Ghose P., Shao Z., Ye Q., Kang L., Xu X.Z.,
RA   Powell-Coffman J.A., Rongo C.;
RT   "Hypoxia regulates glutamate receptor trafficking through an HIF-
RT   independent mechanism.";
RL   EMBO J. 31:1379-1393(2012).
RN   [15] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH CYSL-1, AND MUTAGENESIS OF GLU-720.
RX   PubMed=22405203; DOI=10.1016/j.neuron.2011.12.037;
RA   Ma D.K., Vozdek R., Bhatla N., Horvitz H.R.;
RT   "CYSL-1 interacts with the O2-sensing hydroxylase EGL-9 to promote
RT   H2S-modulated hypoxia-induced behavioral plasticity in C. elegans.";
RL   Neuron 73:925-940(2012).
RN   [16] {ECO:0000305}
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   [17] {ECO:0000305}
RP   FUNCTION, AND DOMAIN.
RX   PubMed=22792069; DOI=10.1371/journal.ppat.1002798;
RA   Luhachack L.G., Visvikis O., Wollenberg A.C., Lacy-Hulbert A.,
RA   Stuart L.M., 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).
RN   [18] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=24385935; DOI=10.1371/journal.pgen.1004063;
RA   Ghose P., Park E.C., Tabakin A., Salazar-Vasquez N., Rongo C.;
RT   "Anoxia-reoxygenation regulates mitochondrial dynamics through the
RT   hypoxia response pathway, SKN-1/Nrf, and stomatin-like protein STL-
RT   1/SLP-2.";
RL   PLoS Genet. 9:E1004063-E1004063(2013).
CC   -!- FUNCTION: Cellular oxygen sensor which regulates the stability and
CC       the activity of hypoxia-inducible transcription factor, hif-1. In
CC       normoxic conditions, hydroxylates hif-1 targeting it for vhl-1-
CC       mediated proteasomal degradation (PubMed:11595184). In addition,
CC       regulates hif-1 transcriptional activity in a vhl-1-independent
CC       manner and independently of its hydroxylase activity
CC       (PubMed:19737748). By regulating hif-1 activity, controls several
CC       cellular responses. Mediates susceptibility to B.thuringiensis and
CC       V.cholerae pore-forming toxins and enteropathogenic E.coli
CC       (PubMed:20011506, PubMed:16091039). Mediates susceptibility to
CC       P.aeruginosa PAO1-mediated killing by regulating resistance to
CC       cyanide produced by P.aeruginosa (PubMed:10611362,
CC       PubMed:11591663, PubMed:20865124). Mediates resistance to
CC       S.aureus-mediated killing (PubMed:22792069). In addition, plays a
CC       role in heat acclimation, neuronal development, behavioral
CC       responses to reoxygenation and hydrogen sulfide, iron homeostasis
CC       and aging (PubMed:12686697, PubMed:18477695, PubMed:22405203,
CC       PubMed:19372390, PubMed:22396654). In neurons, involved in
CC       mitochondrion fusion during reoxygenation (PubMed:24385935).
CC       Involved in egg laying (PubMed:10611362, PubMed:11813735).
CC       {ECO:0000269|PubMed:10611362, ECO:0000269|PubMed:11591663,
CC       ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:11813735,
CC       ECO:0000269|PubMed:12686697, ECO:0000269|PubMed:16091039,
CC       ECO:0000269|PubMed:18477695, ECO:0000269|PubMed:19372390,
CC       ECO:0000269|PubMed:19737748, ECO:0000269|PubMed:20011506,
CC       ECO:0000269|PubMed:20865124, ECO:0000269|PubMed:22396654,
CC       ECO:0000269|PubMed:22405203, ECO:0000269|PubMed:22792069,
CC       ECO:0000269|PubMed:24385935}.
CC   -!- FUNCTION: Isoform e: Regulates the trafficking of the glutamate
CC       receptor glr-1, probably independently of hif-1, by regulating
CC       lin-10 subcellular localization in response to oxygen levels. May
CC       hydroxylate lin-10. {ECO:0000269|PubMed:22252129}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + [hypoxia-inducible factor alpha
CC         subunit]-L-proline + O2 = [hypoxia-inducible factor alpha
CC         subunit]-trans-4-hydroxy-L-proline + CO2 + succinate;
CC         Xref=Rhea:RHEA:48400, Rhea:RHEA-COMP:12093, Rhea:RHEA-
CC         COMP:12094, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:50342,
CC         ChEBI:CHEBI:61965; EC=1.14.11.29;
CC         Evidence={ECO:0000269|PubMed:11595184,
CC         ECO:0000269|PubMed:19737748};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:11595184,
CC         ECO:0000269|PubMed:19737748};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000269|PubMed:11595184};
CC   -!- ACTIVITY REGULATION: Inhibited by Co(2+) and dimethyloxalylglycine
CC       (PubMed:11595184). Inhibited by the iron chelator 2, 2'-dipyridyl
CC       (PubMed:19737748). {ECO:0000269|PubMed:11595184,
CC       ECO:0000269|PubMed:19737748}.
CC   -!- SUBUNIT: Interacts (via catalytic domain) with lin-10 (via N-
CC       terminus); the interaction regulates lin-10 subcellular
CC       localization; the interaction is direct (PubMed:22252129).
CC       Interacts (via catalytic domain) with swan-1 (via WD 1-3 repeats);
CC       the interaction may regulate vhl-1-independent hif-1
CC       transcriptional activity; the interaction is direct
CC       (PubMed:20865124). Interacts (via C-terminus) with cysl-1; the
CC       interaction is enhanced by hydrogen disulfide and activates hif-1-
CC       mediated transcription; the interaction is direct
CC       (PubMed:22405203). {ECO:0000269|PubMed:20865124,
CC       ECO:0000269|PubMed:22252129, ECO:0000269|PubMed:22405203}.
CC   -!- INTERACTION:
CC       Q93244:cysl-1; NbExp=3; IntAct=EBI-2004151, EBI-2413537;
CC       Q7K7J0:gei-18; NbExp=3; IntAct=EBI-2004151, EBI-2315822;
CC       Q93758:swan-1; NbExp=2; IntAct=EBI-2004151, EBI-331968;
CC   -!- SUBCELLULAR LOCATION: Isoform a: Cytoplasm
CC       {ECO:0000269|PubMed:22252129}. Nucleus
CC       {ECO:0000269|PubMed:22252129}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:22252129}. Note=In interneurons, localizes
CC       throughout the ventral cord dendrites.
CC       {ECO:0000269|PubMed:22252129}.
CC   -!- SUBCELLULAR LOCATION: Isoform c: Cytoplasm
CC       {ECO:0000269|PubMed:22252129}. Nucleus
CC       {ECO:0000269|PubMed:22252129}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:22252129}. Note=In interneurons, localizes
CC       throughout the ventral cord dendrites.
CC       {ECO:0000269|PubMed:22252129}.
CC   -!- SUBCELLULAR LOCATION: Isoform e: Cytoplasm
CC       {ECO:0000269|PubMed:22252129}. Nucleus
CC       {ECO:0000269|PubMed:22252129}. Cell projection, axon
CC       {ECO:0000269|PubMed:22252129}. Note=In interneurons, localizes in
CC       puncta (which probably correspond to endosomes) along the ventral
CC       cord. Localization to puncta is regulated by oxygen levels. Co-
CC       localizes with lin-10 in puncta. {ECO:0000269|PubMed:22252129}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=a {ECO:0000312|WormBase:F22E12.4a};
CC         IsoId=G5EBV0-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:F22E12.4b};
CC         IsoId=G5EBV0-2; Sequence=VSP_057747, VSP_057748;
CC         Note=No experimental confirmation available. {ECO:0000305};
CC       Name=c {ECO:0000312|WormBase:F22E12.4c};
CC         IsoId=G5EBV0-3; Sequence=VSP_057745;
CC         Note=No experimental confirmation available. {ECO:0000305};
CC       Name=d {ECO:0000312|WormBase:F22E12.4d};
CC         IsoId=G5EBV0-4; Sequence=VSP_057749;
CC         Note=No experimental confirmation available. {ECO:0000305};
CC       Name=e {ECO:0000312|WormBase:F22E12.4e};
CC         IsoId=G5EBV0-5; Sequence=VSP_057746;
CC         Note=No experimental confirmation available. {ECO:0000305};
CC   -!- TISSUE SPECIFICITY: In larvae and adults, expressed in pharyngeal
CC       and body wall muscles. {ECO:0000269|PubMed:10611362}.
CC   -!- INDUCTION: Induced by hypoxia. {ECO:0000269|PubMed:15781453}.
CC   -!- DOMAIN: The MYND-type domain is not required for oxygen-mediated
CC       hif-1 degradation or for inhibiting hif-1 transcriptional activity
CC       (PubMed:19737748). Susceptibility to S.aureus infection requires
CC       the Ser-rich region but not the MYND-type or Fe2OG dioxygenase
CC       domains (PubMed:22792069). {ECO:0000269|PubMed:19737748,
CC       ECO:0000269|PubMed:22792069}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes enhanced
CC       resistance to polyglutamine or amyloid-beta-mediated paralysis and
CC       an increase in adult life span (PubMed:19372390). In addition,
CC       causes resistance to B.thuringiensis pore-forming toxin CryA21-
CC       mediated toxicity (PubMed:20011506). {ECO:0000269|PubMed:19372390,
CC       ECO:0000269|PubMed:20011506}.
DR   EMBL; AF178536; AAD56365.1; -; mRNA.
DR   EMBL; BX284605; CAA94893.2; -; Genomic_DNA.
DR   EMBL; BX284605; CAD44114.1; -; Genomic_DNA.
DR   EMBL; BX284605; CAI79247.1; -; Genomic_DNA.
DR   EMBL; BX284605; CAI79160.1; -; Genomic_DNA.
DR   EMBL; BX284605; CAK55177.1; -; Genomic_DNA.
DR   PIR; T21276; T21276.
DR   RefSeq; NP_001023832.1; NM_001028661.3. [G5EBV0-2]
DR   RefSeq; NP_001023833.1; NM_001028662.1. [G5EBV0-3]
DR   RefSeq; NP_001023834.1; NM_001028663.3. [G5EBV0-4]
DR   RefSeq; NP_001041105.1; NM_001047640.2. [G5EBV0-5]
DR   RefSeq; NP_741621.1; NM_171533.4. [G5EBV0-1]
DR   SMR; G5EBV0; -.
DR   IntAct; G5EBV0; 4.
DR   STRING; 6239.F22E12.4a.2; -.
DR   EPD; G5EBV0; -.
DR   PaxDb; G5EBV0; -.
DR   PeptideAtlas; G5EBV0; -.
DR   EnsemblMetazoa; F22E12.4a.1; F22E12.4a.1; WBGene00001178. [G5EBV0-1]
DR   EnsemblMetazoa; F22E12.4a.2; F22E12.4a.2; WBGene00001178. [G5EBV0-1]
DR   EnsemblMetazoa; F22E12.4b.1; F22E12.4b.1; WBGene00001178. [G5EBV0-2]
DR   EnsemblMetazoa; F22E12.4b.2; F22E12.4b.2; WBGene00001178. [G5EBV0-2]
DR   EnsemblMetazoa; F22E12.4c.1; F22E12.4c.1; WBGene00001178. [G5EBV0-3]
DR   EnsemblMetazoa; F22E12.4d.1; F22E12.4d.1; WBGene00001178. [G5EBV0-4]
DR   EnsemblMetazoa; F22E12.4d.2; F22E12.4d.2; WBGene00001178. [G5EBV0-4]
DR   EnsemblMetazoa; F22E12.4e.1; F22E12.4e.1; WBGene00001178. [G5EBV0-5]
DR   GeneID; 179461; -.
DR   KEGG; cel:CELE_F22E12.4; -.
DR   CTD; 179461; -.
DR   WormBase; F22E12.4a; CE27755; WBGene00001178; egl-9. [G5EBV0-1]
DR   WormBase; F22E12.4b; CE31342; WBGene00001178; egl-9. [G5EBV0-2]
DR   WormBase; F22E12.4c; CE38327; WBGene00001178; egl-9. [G5EBV0-3]
DR   WormBase; F22E12.4d; CE38328; WBGene00001178; egl-9. [G5EBV0-4]
DR   WormBase; F22E12.4e; CE40254; WBGene00001178; egl-9. [G5EBV0-5]
DR   eggNOG; KOG3710; Eukaryota.
DR   eggNOG; ENOG410ZHZN; LUCA.
DR   GeneTree; ENSGT00940000155704; -.
DR   HOGENOM; HOG000018881; -.
DR   InParanoid; G5EBV0; -.
DR   KO; K09592; -.
DR   OMA; HRFAITI; -.
DR   OrthoDB; 694037at2759; -.
DR   Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   PRO; PR:G5EBV0; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00001178; Expressed in 4 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IDA:WormBase.
DR   GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:WormBase.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR   GO; GO:0001666; P:response to hypoxia; IMP:WormBase.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Complete proteome; Cytoplasm;
KW   Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW   Reference proteome; Vitamin C; Zinc; Zinc-finger.
FT   CHAIN         1    723       Hypoxia-inducible factor prolyl
FT                                hydroxylase. {ECO:0000305}.
FT                                /FTId=PRO_0000433363.
FT   DOMAIN      468    566       Fe2OG dioxygenase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   ZN_FING      39     79       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   COMPBIAS    161    273       Ser-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00016}.
FT   COMPBIAS    712    715       Poly-Pro. {ECO:0000255}.
FT   METAL       487    487       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   METAL       489    489       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   METAL       548    548       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   BINDING     557    557       2-oxoglutarate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   VAR_SEQ       1    292       MSSAPNDDCEIDKGTPSTASLFTTLMLSQPSSSTAVLQCTY
FT                                CGSSCTSSQLQTCLFCGTVAYCSKEHQQLDWLTHKMICKSL
FT                                QTSGMVPSNLMPQAAPAVMAPIPPTVSFDDPALTTSLLLSL
FT                                QNNPILNQTISNFPPTFSITSKTEPEPSIPIQIPQRISSTS
FT                                TVPFSSEGSAFKPYRNTHVFNSISSESMSSMCTSHEASLEH
FT                                MSSASLAMFPTSSTAQSDISRLAQVLSLAGDSPASLALVTT
FT                                SVPSTASTATIPPPATTTSSATSSGKSETITVGKEKIIQTD
FT                                DPDIQ -> MPLRTIVAPTSYGIPTPMPSQSRWKPYSKTMK
FT                                PS (in isoform c). {ECO:0000305}.
FT                                /FTId=VSP_057745.
FT   VAR_SEQ       1     76       Missing (in isoform e). {ECO:0000305}.
FT                                /FTId=VSP_057746.
FT   VAR_SEQ     362    363       YI -> RN (in isoform b). {ECO:0000305}.
FT                                /FTId=VSP_057747.
FT   VAR_SEQ     364    723       Missing (in isoform b). {ECO:0000305}.
FT                                /FTId=VSP_057748.
FT   VAR_SEQ     642    662       Missing (in isoform d). {ECO:0000305}.
FT                                /FTId=VSP_057749.
FT   MUTAGEN     487    487       H->A: Loss of hydroxylase activity
FT                                resulting in loss of oxygen-mediated hif-
FT                                1 degradation. Inhibition of hif-1
FT                                transcriptional activity, which is
FT                                independent of egl-9 hydroxylase
FT                                activity, is only slightly affected. Loss
FT                                of glr-1 recycling; in isoform e.
FT                                {ECO:0000269|PubMed:19737748,
FT                                ECO:0000269|PubMed:22252129}.
FT   MUTAGEN     720    720       E->K: Loss of interaction with cysl-1
FT                                associated with a loss of hypoxia-
FT                                mediated inhibition of behavior
FT                                adaptation.
FT                                {ECO:0000269|PubMed:22405203}.
SQ   SEQUENCE   723 AA;  79743 MW;  15F65F197F9D1D52 CRC64;
     MSSAPNDDCE IDKGTPSTAS LFTTLMLSQP SSSTAVLQCT YCGSSCTSSQ LQTCLFCGTV
     AYCSKEHQQL DWLTHKMICK SLQTSGMVPS NLMPQAAPAV MAPIPPTVSF DDPALTTSLL
     LSLQNNPILN QTISNFPPTF SITSKTEPEP SIPIQIPQRI SSTSTVPFSS EGSAFKPYRN
     THVFNSISSE SMSSMCTSHE ASLEHMSSAS LAMFPTSSTA QSDISRLAQV LSLAGDSPAS
     LALVTTSVPS TASTATIPPP ATTTSSATSS GKSETITVGK EKIIQTDDPD IQIIETEGGS
     KPTVSRTRKR PTPSNSADPK INYKDHNKNV VYSTTLQEHQ KHLQNRGLAL SIHQAMVLRL
     RYIAEHVIRS LNEFGWAVVD NFLGSDHYKF TAKEIERLYE RGLFSPGQLM EAKHKDEFHI
     KDIRSDHIYW YDGYDGRAKD AATVRLLISM IDSVIQHFKK RIDHDIGGRS RAMLAIYPGN
     GTRYVKHVDN PVKDGRCITT IYYCNENWDM ATDGGTLRLY PETSMTPMDI DPRADRLVFF
     WSDRRNPHEV MPVFRHRFAI TIWYMDKSER DKALAKGKES DAACASKKEN DPTSSSLNSL
     IGSLLRPRKN PSTHDLSKLD LRLFPSTSSD PALVSAADED RVDISADFQS TSSLAHPEST
     DSGVSLSTFN VAHNHMERTT SLQSISDHFR SERSHERRSS TSSDQDLDEG LPPPPSTNPE
     YYI
//
DBGET integrated database retrieval system