Ketimine reductase mu-crystallin

Details

Name
Ketimine reductase mu-crystallin
Synonyms
  • 1.5.1.25
  • NADP-regulated thyroid-hormone-binding protein
  • THBP
Gene Name
CRYM
Organism
Humans
Amino acid sequence
>lcl|BSEQ0009936|Ketimine reductase mu-crystallin
MSRVPAFLSAAEVEEHLRSSSLLIPPLETALANFSSGPEGGVMQPVRTVVPVTKHRGYLG
VMPAYSAAEDALTTKLVTFYEDRGITSVVPSHQATVLLFEPSNGTLLAVMDGNVITAKRT
AAVSAIATKFLKPPSSEVLCILGAGVQAYSHYEIFTEQFSFKEVRIWNRTKENAEKFADT
VQGEVRVCSSVQEAVAGADVIITVTLATEPILFGEWVKPGAHINAVGASRPDWRELDDEL
MKEAVLYVDSQEAALKESGDVLLSGAEIFAELGEVIKGVKPAHCEKTTVFKSLGMAVEDT
VAAKLIYDSWSSGK
Number of residues
314
Molecular Weight
33775.285
Theoretical pI
4.8
GO Classification
Functions
NADP binding / protein homodimerization activity / thiomorpholine-carboxylate dehydrogenase activity / thyroid hormone binding / transcription corepressor activity
Processes
cellular nitrogen compound metabolic process / lysine catabolic process / negative regulation of transcription from RNA polymerase II promoter / sensory perception of sound / small molecule metabolic process / thyroid hormone metabolic process / thyroid hormone transport
Components
cytoplasm / extracellular exosome / mitochondrion / nucleus / peroxisomal matrix
General Function
Transcription corepressor activity
Specific Function
Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0009937|Ketimine reductase mu-crystallin (CRYM)
ATGAGCCGGGTACCAGCGTTCCTGAGCGCGGCCGAGGTGGAGGAACACCTCCGCAGCTCC
AGCCTCCTCATCCCGCCTCTAGAGACGGCCCTGGCCAACTTCTCCAGCGGTCCCGAAGGA
GGGGTCATGCAGCCCGTGCGCACCGTGGTGCCGGTGACCAAGCACAGGGGCTACCTGGGG
GTCATGCCCGCCTACAGTGCTGCAGAGGATGCACTGACCACCAAGTTGGTCACCTTCTAC
GAGGACCGCGGCATCACCTCGGTCGTCCCTTCCCACCAGGCTACTGTGCTACTCTTTGAG
CCCAGCAATGGCACCCTGCTGGCGGTCATGGATGGAAATGTCATAACTGCAAAGAGAACA
GCTGCAGTTTCTGCCATTGCCACCAAGTTTCTGAAACCTCCCAGCAGTGAAGTGCTGTGC
ATCCTTGGGGCTGGGGTCCAGGCCTACAGCCATTATGAGATCTTCACAGAGCAGTTCTCC
TTTAAGGAGGTGAGGATATGGAACCGCACCAAAGAAAATGCAGAGAAGTTTGCAGACACA
GTGCAAGGAGAGGTACGGGTCTGTTCTTCGGTCCAGGAGGCTGTGGCAGGTGCAGATGTG
ATCATCACAGTCACCCTGGCAACAGAGCCCATTTTGTTTGGTGAATGGGTGAAGCCAGGG
GCTCACATCAATGCTGTTGGAGCCAGCAGACCTGACTGGAGAGAACTGGATGATGAGCTC
ATGAAAGAAGCTGTGCTGTACGTGGATTCCCAGGAGGCTGCCCTGAAGGAGTCTGGAGAT
GTCCTGCTGTCAGGGGCCGAGATCTTTGCTGAGCTGGGAGAAGTGATTAAGGGAGTGAAA
CCAGCCCACTGTGAGAAGACCACCGTGTTCAAGTCTTTGGGAATGGCAGTGGAAGACACA
GTTGCAGCCAAACTCATCTATGATTCCTGGTCATCTGGTAAATAA
Chromosome Location
16
Locus
16p13.11-p12.3
External Identifiers
ResourceLink
UniProtKB IDQ14894
UniProtKB Entry NameCRYM_HUMAN
GenBank Protein ID1066343
GenBank Gene IDL02950
GenAtlas IDCRYM
HGNC IDHGNC:2418
General References
  1. Segovia L, Horwitz J, Gasser R, Wistow G: Two roles for mu-crystallin: a lens structural protein in diurnal marsupials and a possible enzyme in mammalian retinas. Mol Vis. 1997 Sep 9;3:9. [Article]
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  8. Kim RY, Gasser R, Wistow GJ: mu-crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9292-6. [Article]
  9. Abe S, Katagiri T, Saito-Hisaminato A, Usami S, Inoue Y, Tsunoda T, Nakamura Y: Identification of CRYM as a candidate responsible for nonsyndromic deafness, through cDNA microarray analysis of human cochlear and vestibular tissues. Am J Hum Genet. 2003 Jan;72(1):73-82. Epub 2002 Dec 6. [Article]
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  12. Cheng Z, Sun L, He J, Gong W: Crystal structure of human micro-crystallin complexed with NADPH. Protein Sci. 2007 Feb;16(2):329-35. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB05235NRP409investigationalunknownDetails