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   27-MAR-2024, entry version 123.
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.C02C2.5.1; -.
DR   PaxDb; 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   AGR; WB:WBGene00015334; -.
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; FTDLHEN; -.
DR   OrthoDB; 5390904at2759; -.
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 cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140616; F:iodotyrosine deiodinase activity; IEA:UniProt.
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   CDD; cd02144; iodotyrosine_dehalogenase; 1.
DR   Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR   InterPro; IPR029479; Nitroreductase.
DR   InterPro; IPR000415; Nitroreductase-like.
DR   PANTHER; PTHR23026:SF90; IODOTYROSINE DEIODINASE 1; 1.
DR   PANTHER; PTHR23026; NADPH NITROREDUCTASE; 1.
DR   Pfam; PF00881; Nitroreductase; 1.
DR   SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 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
//