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 Genevisible; O54983; MM.
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.
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
//
