ID   CRYM_MOUSE              Reviewed;         313 AA.
AC   O54983;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 149.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain;
RA   Sperbeck S.J., Segovia L., Wistow G.J.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
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 4-18; 37-47; 119-128 AND 176-185, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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; AF039391; AAB94770.1; -; mRNA.
DR   EMBL; BC045159; AAH45159.1; -; mRNA.
DR   CCDS; CCDS21794.1; -.
DR   RefSeq; NP_057878.1; NM_016669.1.
DR   PDB; 4BV8; X-ray; 2.30 A; A/B=1-313.
DR   PDB; 4BV9; X-ray; 2.19 A; A/B=1-313.
DR   PDB; 4BVA; X-ray; 1.75 A; A/B=1-313.
DR   PDBsum; 4BV8; -.
DR   PDBsum; 4BV9; -.
DR   PDBsum; 4BVA; -.
DR   AlphaFoldDB; O54983; -.
DR   SMR; O54983; -.
DR   BioGRID; 198923; 5.
DR   IntAct; O54983; 3.
DR   MINT; O54983; -.
DR   STRING; 10090.ENSMUSP00000033198; -.
DR   GlyGen; O54983; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O54983; -.
DR   PhosphoSitePlus; O54983; -.
DR   SwissPalm; O54983; -.
DR   jPOST; O54983; -.
DR   PaxDb; 10090-ENSMUSP00000033198; -.
DR   PeptideAtlas; O54983; -.
DR   ProteomicsDB; 285339; -.
DR   Antibodypedia; 12355; 365 antibodies from 28 providers.
DR   DNASU; 12971; -.
DR   Ensembl; ENSMUST00000033198.6; ENSMUSP00000033198.6; ENSMUSG00000030905.6.
DR   GeneID; 12971; -.
DR   KEGG; mmu:12971; -.
DR   UCSC; uc009jmk.1; mouse.
DR   AGR; MGI:102675; -.
DR   CTD; 1428; -.
DR   MGI; MGI:102675; Crym.
DR   VEuPathDB; HostDB:ENSMUSG00000030905; -.
DR   eggNOG; KOG3007; Eukaryota.
DR   GeneTree; ENSGT00390000000237; -.
DR   HOGENOM; CLU_042088_1_1_1; -.
DR   InParanoid; O54983; -.
DR   OMA; AVKAFTY; -.
DR   OrthoDB; 2501268at2759; -.
DR   PhylomeDB; O54983; -.
DR   TreeFam; TF105309; -.
DR   BRENDA; 1.5.1.21; 3474.
DR   Reactome; R-MMU-71064; Lysine catabolism.
DR   BioGRID-ORCS; 12971; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Crym; mouse.
DR   PRO; PR:O54983; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O54983; Protein.
DR   Bgee; ENSMUSG00000030905; Expressed in dentate gyrus of hippocampal formation granule cell and 189 other cell types or tissues.
DR   ExpressionAtlas; O54983; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0042562; F:hormone binding; IMP:MGI.
DR   GO; GO:0050661; F:NADP binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0047127; F:thiomorpholine-carboxylate dehydrogenase activity; ISO:MGI.
DR   GO; GO:0070324; F:thyroid hormone binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0006839; P:mitochondrial transport; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; IMP:MGI.
DR   GO; GO:0070327; P:thyroid hormone transport; ISO:MGI.
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.
DR   Genevisible; O54983; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; NAD; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..313
FT                   /note="Ketimine reductase mu-crystallin"
FT                   /id="PRO_0000200679"
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"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           10..15
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           20..35
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          57..66
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   TURN            67..70
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          71..80
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          91..98
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           112..130
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           145..157
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           170..179
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           190..194
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          221..224
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           237..242
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          243..248
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           250..256
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           258..263
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           271..275
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   STRAND          287..290
FT                   /evidence="ECO:0007829|PDB:4BVA"
FT   HELIX           295..311
FT                   /evidence="ECO:0007829|PDB:4BVA"
SQ   SEQUENCE   313 AA;  33523 MW;  0898EDA9E2D34C83 CRC64;
     MKRAPAFLSA EEVQDHLRSS SLLIPPLEAA LANFSKGPDG GVMQPVRTVV PVAKHRGFLG
     VMPAYSAAED ALTTKLVTFY EGHSNTAVPS HQASVLLFDP SNGSLLAVMD GNVITAKRTA
     AVSAIATKLL KPPGSDVLCI LGAGVQAYSH YEIFTEQFSF KEVRMWNRTR ENAEKFASTV
     QGDVRVCSSV QEAVTGADVI ITVTMATEPI LFGEWVKPGA HINAVGASRP DWRELDDELM
     RQAVLYVDSR EAALKESGDV LLSGADIFAE LGEVISGAKP AHCEKTTVFK SLGMAVEDLV
     AAKLVYDSWS SGK
//