CRYM_MACFL
ID CRYM_MACFL Reviewed; 314 AA.
AC Q28488;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Macropus fuliginosus (Western gray kangaroo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Macropus.
OX NCBI_TaxID=9316;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1384048; DOI=10.1073/pnas.89.19.9292;
RA Kim R.Y., Gasser R., Wistow G.J.;
RT "Mu-crystallin is a mammalian homologue of Agrobacterium ornithine
RT cyclodeaminase and is expressed in human retina.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9292-9296(1992).
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). Major component of eye lens in
CC marsupials. {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.
CC -!- TISSUE SPECIFICITY: Expressed at high abundance in lens, but outside
CC the lens it is preferentially expressed in neural tissues, retina and
CC brain.
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000305}.
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DR EMBL; M90841; AAA31606.1; -; mRNA.
DR PIR; A46290; A46290.
DR AlphaFoldDB; Q28488; -.
DR SMR; Q28488; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0047127; F:thiomorpholine-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Cytoplasm; Eye lens protein; NAD; NADP; Oxidoreductase.
FT CHAIN 1..314
FT /note="Ketimine reductase mu-crystallin"
FT /id="PRO_0000200677"
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; 33931 MW; C4036168580ADC17 CRC64;
MSWSPAFLRS EDVERYLGSS SILLPALEKA LANFSSGSEG GVVQPVRTVI PVAKHQGFLG
IMPVYSASED ALTTKLVTFY EGMSPTSTAP SHQTTVLFFD PSNGSLLSIM DGNIITAKRT
AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFKEQFS FKEVRIWNRT KKNAEKFAQT
VKGDVRVCSS VQEAVTGADV IITVTMATKP ILFGEWVKPG AHINAVGASR PDWRELDDEI
MKNCVLYVDS REAALKESGD VILSGAEIFA ELGEVVKGVK PAHREKTTVF KSLGMAVEDA
VAAKLVYDSW SSGK
