ID CRYM_BOVIN Reviewed; 314 AA.
AC Q2KHX6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE RecName: Full=Ketimine reductase mu-crystallin;
DE EC=1.5.1.25;
DE AltName: Full=NADP-regulated thyroid-hormone-binding protein;
GN Name=CRYM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC112846; AAI12847.1; -; mRNA.
DR RefSeq; NP_001039379.1; NM_001045914.2.
DR AlphaFoldDB; Q2KHX6; -.
DR SMR; Q2KHX6; -.
DR STRING; 9913.ENSBTAP00000012972; -.
DR PaxDb; 9913-ENSBTAP00000012972; -.
DR Ensembl; ENSBTAT00000012972.3; ENSBTAP00000012972.2; ENSBTAG00000009842.3.
DR GeneID; 505167; -.
DR KEGG; bta:505167; -.
DR CTD; 1428; -.
DR VEuPathDB; HostDB:ENSBTAG00000009842; -.
DR VGNC; VGNC:27745; CRYM.
DR eggNOG; KOG3007; Eukaryota.
DR GeneTree; ENSGT00390000000237; -.
DR HOGENOM; CLU_042088_1_1_1; -.
DR InParanoid; Q2KHX6; -.
DR OMA; AVKAFTY; -.
DR OrthoDB; 2501268at2759; -.
DR TreeFam; TF105309; -.
DR Reactome; R-BTA-71064; Lysine catabolism.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000009842; Expressed in Ammon's horn and 91 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0050661; F:NADP binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0047127; F:thiomorpholine-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070324; F:thyroid hormone binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IBA:GO_Central.
DR GO; GO:0070327; P:thyroid hormone transport; IEA:Ensembl.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..313
FT /note="Ketimine reductase mu-crystallin"
FT /id="PRO_0000328261"
FT BINDING 143..148
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"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 33747 MW; D9EAE1F47B7CAE2B CRC64;
MSSRPVFLSA ADVQDHLRSS SLLIAPLETA LANFSSGPDG GVVQPVRTVV PVAKHRGFLG
VMPAYSAAED ALTTKLVTFY EDHSATSTVP SHQATVLLFQ PSNGSLLAVM DGNVITAKRT
AAVSAIATKF LKPPNSEVLC ILGAGVQAYS HYEVFTEQFF FKEVRIWNRT KENAEKFVNT
VPGEVRICSS VQEAVTGADV IITVTMATEP ILFGEWVKPG AHINAIGASR PDWRELDDEL
MKQAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVVKGVK PAHCEKTTVF KSLGMAVEDM
VAAKLVYDSW SSGK
//
