RHY1_CAEEL
ID RHY1_CAEEL Reviewed; 502 AA.
AC Q9XVW1;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Regulator of hypoxia-inducible factor 1 {ECO:0000303|PubMed:16980385};
GN Name=rhy-1 {ECO:0000312|WormBase:W07A12.7};
GN ORFNames=W07A12.7 {ECO:0000312|WormBase:W07A12.7};
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|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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {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 in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 280:20580-20588(2005).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF SER-157.
RX PubMed=16980385; DOI=10.1534/genetics.106.063594;
RA Shen C., Shao Z., Powell-Coffman J.A.;
RT "The Caenorhabditis elegans rhy-1 gene inhibits HIF-1 hypoxia-inducible
RT factor activity in a negative feedback loop that does not include vhl-1.";
RL Genetics 174:1205-1214(2006).
RN [4] {ECO:0000305}
RP FUNCTION.
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 [5] {ECO:0000305}
RP FUNCTION.
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 [6] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-149.
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 H2S-
RT modulated hypoxia-induced behavioral plasticity in C. elegans.";
RL Neuron 73:925-940(2012).
CC -!- FUNCTION: Involved in the response to variation in environmental oxygen
CC levels by inhibiting hif-1-mediated gene transcription in a vhl-1-
CC independent manner (PubMed:16980385). Plays a role in susceptibility to
CC killing mediated by P.aeruginosa and by pore-forming toxins produced by
CC B.thuringiensis (PubMed:20011506, PubMed:20865124). Probably by
CC preventing hif-1 transcriptional activity, regulates behavioral
CC responses, such as locomotion speed following acute reoxygenation
CC (PubMed:22405203). Plays a role in normal egg-laying probably by
CC regulating spermatogenesis and in body morphogenesis (PubMed:16980385).
CC {ECO:0000269|PubMed:16980385, ECO:0000269|PubMed:20011506,
CC ECO:0000269|PubMed:20865124, ECO:0000269|PubMed:22405203}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16980385}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, some sensory neurons in the
CC head, body wall muscles and socket cells.
CC {ECO:0000269|PubMed:16980385}.
CC -!- DEVELOPMENTAL STAGE: In L4 stage, expressed in vulva, ventral nerve
CC cord, tail and at higher levels in hypodermis.
CC {ECO:0000269|PubMed:16980385}.
CC -!- INDUCTION: Induced by hypoxia. {ECO:0000269|PubMed:15781453}.
CC -!- DISRUPTION PHENOTYPE: Impaired acute acceleration of locomotion speed
CC upon rapid increase in oxygen levels (from 0% to 5-20% oxygen). In
CC double mutants for both rhy-1 and hif-1, normal increase in locomotion
CC speed is restored. {ECO:0000269|PubMed:22405203}.
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DR EMBL; Z68320; CAA92706.1; -; Genomic_DNA.
DR PIR; T26256; T26256.
DR RefSeq; NP_495954.1; NM_063553.4.
DR AlphaFoldDB; Q9XVW1; -.
DR STRING; 6239.W07A12.7; -.
DR EPD; Q9XVW1; -.
DR PaxDb; Q9XVW1; -.
DR EnsemblMetazoa; W07A12.7.1; W07A12.7.1; WBGene00012324.
DR GeneID; 174455; -.
DR KEGG; cel:CELE_W07A12.7; -.
DR UCSC; W07A12.7; c. elegans.
DR CTD; 174455; -.
DR WormBase; W07A12.7; CE20163; WBGene00012324; rhy-1.
DR eggNOG; KOG3700; Eukaryota.
DR GeneTree; ENSGT00970000196616; -.
DR HOGENOM; CLU_032855_0_0_1; -.
DR InParanoid; Q9XVW1; -.
DR OMA; YNAYLLH; -.
DR OrthoDB; 1171418at2759; -.
DR PhylomeDB; Q9XVW1; -.
DR PRO; PR:Q9XVW1; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00012324; Expressed in embryo and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IMP:CACAO.
DR GO; GO:0001666; P:response to hypoxia; IMP:WormBase.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..502
FT /note="Regulator of hypoxia-inducible factor 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433364"
FT TRANSMEM 54..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT MUTAGEN 149
FT /note="G->E: In 5500; impaired hypoxia-induced behavioral
FT plasticity."
FT /evidence="ECO:0000269|PubMed:22405203"
FT MUTAGEN 157
FT /note="S->F: In ia38; loss of inhibition of hif-1
FT activity."
FT /evidence="ECO:0000269|PubMed:16980385"
SQ SEQUENCE 502 AA; 56103 MW; 35F88FE1E97E9432 CRC64;
MSSSPHTHTL IIMERLSEVR LYSSPMTSVL NSNLSSCLTN AFIPDTVRMA SSPLLAWMTL
VVIGTLAPVS VFSCLSLKRS VKELLTERSS KLDVLDIFRF VAILWVMLNH TGSEGRIDIL
DRLPSADAFK SAMHDHPIFG ALMGNSALGV EIFLVLSGLL AARSWLRKAD EPFFQHWKSF
IARRLLRLAP SMFIFVYIAA GPIMNALLPR YSSSMVSACG FWGILSHVTF TSNWQSTPTC
MGYLWYLGLD MQLYMVAPIF LNLLHKFPKR GMALTITTII ASMVIRAGYC TAYGTCNQSD
VDIPFISYPG QDAETLKSIY AGLWDMYSRP YTKCGPFLIG LLLGYITVSS KYIMVSTTSK
TLFRSSLIVA IATIYAILPE YWNPNAGNTL YNTVYTAVFR SVFAMAISGM IAALYFRQEY
RPTNPIFAML AKLTYNAYLL HMPVVYIFNW LPFLQAATSP IHLLLVLPFV AILSFIAALI
FYLFIEAPIG HLTSQYATRL GL
