CRYM_RAT
ID CRYM_RAT Reviewed; 313 AA.
AC Q9QYU4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ketimine reductase mu-crystallin;
DE EC=1.5.1.25;
DE AltName: Full=CDK108;
DE AltName: Full=NADP-regulated thyroid-hormone-binding protein;
GN Name=Crym;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=GK;
RA Zaidi Q.J.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 57-75, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Specifically catalyzes the reduction of imine bonds in brain
CC substrates that may include cystathionine ketimine (CysK) and
CC lanthionine ketimine (LK). Binds thyroid hormone which is a strong
CC reversible inhibitor. Presumably involved in the regulation of the free
CC intracellular concentration of triiodothyronine and access to its
CC nuclear receptors (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NAD(+) = 3,4-
CC dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:12504, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873;
CC EC=1.5.1.25;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NADP(+) = 3,4-
CC dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:12500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873;
CC EC=1.5.1.25;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000305}.
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DR EMBL; Y17328; CAB56625.1; -; mRNA.
DR EMBL; BC088121; AAH88121.1; -; mRNA.
DR RefSeq; NP_446407.1; NM_053955.1.
DR AlphaFoldDB; Q9QYU4; -.
DR SMR; Q9QYU4; -.
DR BioGRID; 250625; 2.
DR IntAct; Q9QYU4; 1.
DR MINT; Q9QYU4; -.
DR STRING; 10116.ENSRNOP00000066476; -.
DR iPTMnet; Q9QYU4; -.
DR PhosphoSitePlus; Q9QYU4; -.
DR World-2DPAGE; 0004:Q9QYU4; -.
DR PaxDb; Q9QYU4; -.
DR PRIDE; Q9QYU4; -.
DR Ensembl; ENSRNOT00000088482; ENSRNOP00000073313; ENSRNOG00000061215.
DR GeneID; 117024; -.
DR KEGG; rno:117024; -.
DR CTD; 1428; -.
DR RGD; 620943; Crym.
DR eggNOG; KOG3007; Eukaryota.
DR GeneTree; ENSGT00390000000237; -.
DR InParanoid; Q9QYU4; -.
DR OrthoDB; 1345495at2759; -.
DR PhylomeDB; Q9QYU4; -.
DR BRENDA; 1.5.1.21; 5301.
DR Reactome; R-RNO-71064; Lysine catabolism.
DR PRO; PR:Q9QYU4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0042562; F:hormone binding; ISO:RGD.
DR GO; GO:0050661; F:NADP binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0047127; F:thiomorpholine-carboxylate dehydrogenase activity; ISO:RGD.
DR GO; GO:0070324; F:thyroid hormone binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0006839; P:mitochondrial transport; IDA:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:RGD.
DR GO; GO:0070327; P:thyroid hormone transport; ISO:RGD.
DR Gene3D; 3.30.1780.10; -; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; PTHR13812; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..313
FT /note="Ketimine reductase mu-crystallin"
FT /id="PRO_0000200680"
FT BINDING 142..147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 33554 MW; E2F1839D9E5EC5ED CRC64;
MRRAPAFLSA DEVQDHLRSS SLLIPPLEAA LANFSKGPDG GVMQPVRTVV PVAKHRGFLG
VMPAYSAAED ALTTKLVTFY EGHSNNAVPS HQASVLLFDP SNGSLLAVMD GNVITAKRTA
AVSAIATKFL KPPGSDVLCI LGAGVQAYSH YEIFTEQFSF KEVRMWNRTR ENAEKFASSV
QGDVRVCSSV QEAVTGADVI ITVTMATEPI LFGEWVKPGA HINAVGASRP DWRELDDELM
KQAVLYVDSR EAALKESGDV LLSGADIFAE LGEVVSGAKP AYCEKTTVFK SLGMAVEDLV
AAKLVYDSWS SGK
