IYD1H_CAEEL
ID IYD1H_CAEEL Reviewed; 325 AA.
AC P34273; L7TUZ3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Iodotyrosine dehalogenase 1 homolog {ECO:0000303|PubMed:24586202};
DE Short=IYD-1 {ECO:0000303|PubMed:24586202};
DE EC=1.21.1.- {ECO:0000305|PubMed:24586202};
GN Name=sup-18 {ECO:0000312|WormBase:C02C2.5};
GN ORFNames=C02C2.5 {ECO:0000312|WormBase:C02C2.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-137;
RP GLY-258; THR-271; GLY-280; ARG-288 AND THR-322.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AGC39147.1};
RX PubMed=24586202; DOI=10.1371/journal.pgen.1004175;
RA de la Cruz I.P., Ma L., Horvitz H.R.;
RT "The Caenorhabditis elegans iodotyrosine deiodinase ortholog SUP-18
RT functions through a conserved channel SC-box to regulate the muscle two-
RT pore domain potassium channel SUP-9.";
RL PLoS Genet. 10:E1004175-E1004175(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
CC -!- FUNCTION: May contribute to coordination of muscle contraction as
CC regulatory subunit of the nonessential sup-9 potassium channel complex.
CC May act downstream of sup-10. {ECO:0000305|PubMed:24586202}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9DCX8};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:24586202}; Single-
CC pass membrane protein {ECO:0000305|PubMed:24586202}. Note=In body-wall
CC muscle cells, localizes to dense body-like structures which connect the
CC myofibril lattice to the cell membrane. Colocalizes with sup-10.
CC Membrane localization is not essential for its activity.
CC {ECO:0000269|PubMed:24586202}.
CC -!- TISSUE SPECIFICITY: Expressed in body-wall, anal depressor and vulval
CC muscles. {ECO:0000269|PubMed:24586202}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Fully suppresses the rubber
CC band uncoordinated phenotype in gain of function (gf) mutants of sup-10
CC but only slightly in gf mutants of sup-9 and unc-93.
CC {ECO:0000269|PubMed:24586202}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; JX978835; AGC39147.1; -; mRNA.
DR EMBL; FO080276; CCD62530.2; -; Genomic_DNA.
DR PIR; S44738; S44738.
DR RefSeq; NP_498712.3; NM_066311.4.
DR AlphaFoldDB; P34273; -.
DR SMR; P34273; -.
DR STRING; 6239.C02C2.5; -.
DR EnsemblMetazoa; C02C2.5.1; C02C2.5.1; WBGene00015334.
DR GeneID; 182108; -.
DR KEGG; cel:CELE_C02C2.5; -.
DR UCSC; C02C2.5; c. elegans.
DR CTD; 182108; -.
DR WormBase; C02C2.5; CE49662; WBGene00015334; sup-18.
DR eggNOG; KOG3936; Eukaryota.
DR GeneTree; ENSGT00390000004348; -.
DR HOGENOM; CLU_070764_1_0_1; -.
DR InParanoid; P34273; -.
DR OMA; WVDQDLQ; -.
DR OrthoDB; 1524590at2759; -.
DR Reactome; R-CEL-209968; Thyroxine biosynthesis.
DR PRO; PR:P34273; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015334; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006570; P:tyrosine metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Ion transport; Membrane; Oxidoreductase; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..325
FT /note="Iodotyrosine dehalogenase 1 homolog"
FT /id="PRO_0000065104"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24586202"
FT BINDING 135..139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 163..164
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 273..275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 315
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT MUTAGEN 137
FT /note="S->N: In n1010; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 258
FT /note="G->D: In n1554; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 258
FT /note="G->S: In n1471; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 271
FT /note="T->I: In n1556; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 280
FT /note="G->R: In n1014; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 288
FT /note="R->K: In n1022; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 322
FT /note="T->P: In n528; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
SQ SEQUENCE 325 AA; 37261 MW; 973CECAAE4A3BA58 CRC64;
MKKHTHHKAY GDSTGKEPLI DLQSIKLWLN SFGNQGHSSE AVLNVLFTLG VILFVIYQVA
SLLHRMNKRV EKQLESRTKQ RKVEVADKHV GDEMVFTDLH ENVIRERMIP YRMPVINDDI
TLRNSQIFYE EMKMRRSCRQ FSSRDVPLKV IQNLLKTAGT SPSVGNLQPW TFCVVSSDSI
KTMIRKILEA DERDNYVSRK KGASWVVDVS QLQDTWRRPY ITDAPYLLIV CHEIFRDVHS
KTERVFHYNQ ISTSIAVGIL LAAIQNVGLS TVVTSPLNAG PDISRILRRP ENESILLLLP
LGYASEDVLV PDLKRKPVEH ITKLY
