IOD2_PETMA
ID IOD2_PETMA Reviewed; 288 AA.
AC L7WGA7;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 02-JUN-2021, entry version 25.
DE RecName: Full=Type II iodothyronine deiodinase {ECO:0000250|UniProtKB:Q92813};
DE EC=1.21.99.4;
DE AltName: Full=5DII {ECO:0000250|UniProtKB:Q92813};
DE AltName: Full=DIOII {ECO:0000250|UniProtKB:Q92813};
DE AltName: Full=Type 2 DI {ECO:0000250|UniProtKB:Q92813};
DE AltName: Full=Type-II 5'-deiodinase {ECO:0000250|UniProtKB:Q92813};
GN Name=dio2 {ECO:0000250|UniProtKB:Q92813};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AGC79960.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC TISSUE=Intestine {ECO:0000312|EMBL:AGC79960.1};
RX PubMed=23295540; DOI=10.1016/j.ygcen.2012.12.007;
RA Stilborn S.S.M., Manzon L.A., Schauenberg J.D., Manzon R.G.;
RT "Thyroid hormone deiodinase type 2 mRNA levels in sea lamprey (Petromyzon
RT marinus) are regulated during metamorphosis and in response to a thyroid
RT challenge.";
RL Gen. Comp. Endocrinol. 183:63-68(2013).
CC -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-
CC tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for
CC providing the brain with appropriate levels of T3 during the critical
CC period of development. {ECO:0000250|UniProtKB:Q92813}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,3',5-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-
CC thyroxine; Xref=Rhea:RHEA:19745, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58448, ChEBI:CHEBI:533015; EC=1.21.99.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10107};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, liver, kidney and brain of
CC immediately premetamorphic larvae, of larvae in all stages of
CC metamorphosis and of parasitic feeding juveniles. In immediately
CC premetamorphic larvae, levels are significantly higher in intestine and
CC liver than in kidney and brain. {ECO:0000269|PubMed:23295540}.
CC -!- DEVELOPMENTAL STAGE: In the early developmental stages, elevated levels
CC in intestine, liver and kidney, followed by decline through to stages 4
CC and 5 of metamorphosis. Levels are relatively stable in the brain
CC during the same period. {ECO:0000269|PubMed:23295540}.
CC -!- INDUCTION: Treatment of larvae with thyroid hormone T3 causes a
CC significant decrease in intestinal levels. The thyroid hormone
CC synthesis inhibitor potassium perchlorate (KClO4) significantly
CC increases intestinal levels. Thyroid hormone T4 causes a decrease in
CC intestine at day 3 of treatment but levels return to normal by day 6.
CC Expression is significantly reduced in liver in response to all three
CC treatments. {ECO:0000269|PubMed:23295540}.
CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC {ECO:0000255}.
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DR EMBL; KC306946; AGC79960.1; -; mRNA.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR000643; Iodothyronine_deiodinase.
DR InterPro; IPR008261; Iodothyronine_deiodinase_AS.
DR PANTHER; PTHR11781; PTHR11781; 1.
DR Pfam; PF00837; T4_deiodinase; 1.
DR PIRSF; PIRSF001330; IOD; 1.
DR PROSITE; PS01205; T4_DEIODINASE; 1.
PE 2: Evidence at transcript level;
KW Membrane; Oxidoreductase; Reference proteome; Selenocysteine;
KW Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Type II iodothyronine deiodinase"
FT /id="PRO_0000424284"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 99..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /evidence="ECO:0000250|UniProtKB:P55073,
FT ECO:0000255|PROSITE-ProRule:PRU10107"
FT NON_STD 160
FT /note="Selenocysteine"
FT /evidence="ECO:0000312|EMBL:AGC79960.1"
SQ SEQUENCE 288 AA; 30946 MW; 67F0A5D0DAB81333 CRC64;
MPHVNLLVVL LILPGVFSNC LFLALYDAVS FLRRALQASL THSAKGDAQH PRMLTAQGML
SVWRSYVLDA HKKVRLGGKA PNSSVVALGG HSSSSPSFSC AASSSSSHET PTPRTTAEAA
ATVTTSTTTT STTSSTAACR LLDFARAHRP LVVNFGSASU PPFVEQLGEF CDLVRDFAGV
ADFLVVYIEE AHPSDAWPAP GGLEVPRHLA LGDRCVAASQ LRGLMPPLGR CPVVADAMDN
NANIDYGVSY ERLYVIQDGR IRYLGGKGPF FYRVREVKSF LESVKASR
