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Protein

Ketimine reductase mu-crystallin

Gene

CRYM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H.1 Publication

Cofactori

NAD(+)2 Publications, NADP(+)2 Publications

Kineticsi

  1. KM=47 µM for 3,4-dehydro-thiomorpholine-3-carboxylate (at pH 5.0 and 37 degrees Celsius)1 Publication
  2. KM=3.6 µM for NADH (at pH 5.0 and 37 degrees Celsius)1 Publication

Vmax=9.6 µmol/min/mg enzyme with 3,4-dehydro-thiomorpholine-3-carboxylate as substrate (at pH 5.0 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 4.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681NADP1 Publication
Binding sitei169 – 1691NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi143 – 1486NADP1 Publication

GO - Molecular functioni

  1. NADP binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
  3. thiomorpholine-carboxylate dehydrogenase activity Source: UniProtKB-EC
  4. thyroid hormone binding Source: UniProtKB
  5. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  2. sensory perception of sound Source: UniProtKB
  3. thyroid hormone metabolic process Source: Ensembl
  4. thyroid hormone transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Ketimine reductase mu-crystallin (EC:1.5.1.25)
Alternative name(s):
NADP-regulated thyroid-hormone-binding protein
Gene namesi
Name:CRYM
Synonyms:THBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2418. CRYM.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrion Source: Ensembl
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBiPA26924.

Polymorphism and mutation databases

BioMutaiCRYM.
DMDMi2498259.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Ketimine reductase mu-crystallinPRO_0000200678Add
BLAST

Proteomic databases

MaxQBiQ14894.
PaxDbiQ14894.
PRIDEiQ14894.

PTM databases

PhosphoSiteiQ14894.

Expressioni

Tissue specificityi

Expressed in neural tissue, muscle and kidney.

Gene expression databases

BgeeiQ14894.
CleanExiHS_CRYM.
ExpressionAtlasiQ14894. baseline and differential.
GenevestigatoriQ14894.

Organism-specific databases

HPAiHPA019086.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi107815. 6 interactions.
IntActiQ14894. 2 interactions.
MINTiMINT-4532969.
STRINGi9606.ENSP00000219599.

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi10 – 167Combined sources
Helixi20 – 234Combined sources
Helixi24 – 3512Combined sources
Helixi37 – 404Combined sources
Beta strandi48 – 525Combined sources
Helixi53 – 553Combined sources
Beta strandi57 – 6610Combined sources
Turni67 – 704Combined sources
Beta strandi71 – 8010Combined sources
Beta strandi84 – 874Combined sources
Beta strandi89 – 9911Combined sources
Turni101 – 1033Combined sources
Beta strandi106 – 1116Combined sources
Helixi113 – 13119Combined sources
Beta strandi138 – 1425Combined sources
Helixi146 – 15813Combined sources
Beta strandi162 – 1676Combined sources
Helixi171 – 18010Combined sources
Beta strandi181 – 1833Combined sources
Helixi191 – 1955Combined sources
Beta strandi199 – 2035Combined sources
Helixi214 – 2163Combined sources
Beta strandi222 – 2254Combined sources
Helixi238 – 2436Combined sources
Beta strandi244 – 2496Combined sources
Helixi251 – 2577Combined sources
Helixi259 – 2624Combined sources
Turni263 – 2653Combined sources
Helixi272 – 2776Combined sources
Beta strandi288 – 2914Combined sources
Helixi296 – 31015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I99X-ray2.60A/B2-313[»]
ProteinModelPortaliQ14894.
SMRiQ14894. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14894.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2423.
GeneTreeiENSGT00390000000237.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiQ14894.
KOiK18258.
OMAiKHRGYLG.
PhylomeDBiQ14894.
TreeFamiTF105309.

Family and domain databases

Gene3Di3.30.1780.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR003462. ODC_Mu_crystall.
IPR023401. ODC_N.
[Graphical view]
PfamiPF02423. OCD_Mu_crystall. 1 hit.
[Graphical view]
PIRSFiPIRSF001439. CryM. 1 hit.

Sequencei

Sequence statusi: Complete.

Q14894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV
60 70 80 90 100
PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE
110 120 130 140 150
PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS
160 170 180 190 200
HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV
210 220 230 240 250
IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS
260 270 280 290 300
QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT
310
VAAKLIYDSW SSGK
Length:314
Mass (Da):33,776
Last modified:November 1, 1997 - v1
Checksum:iA49D316B41CE6648
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02950 mRNA. Translation: AAC16914.1.
U85772 mRNA. Translation: AAB81564.1.
AF039397
, AF039392, AF039393, AF039394, AF039395, AF039396 Genomic DNA. Translation: AAB94938.1.
AK290852 mRNA. Translation: BAF83541.1.
BX648477 mRNA. Translation: CAI46030.1.
AF001550 Genomic DNA. Translation: AAB67600.1.
CH471228 Genomic DNA. Translation: EAW66863.1.
BC018061 mRNA. Translation: AAH18061.1.
CCDSiCCDS10597.1.
PIRiB46290.
RefSeqiNP_001879.1. NM_001888.4.
UniGeneiHs.924.

Genome annotation databases

EnsembliENST00000219599; ENSP00000219599; ENSG00000103316.
ENST00000543948; ENSP00000440227; ENSG00000103316.
GeneIDi1428.
KEGGihsa:1428.
UCSCiuc002dil.3. human.

Polymorphism and mutation databases

BioMutaiCRYM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02950 mRNA. Translation: AAC16914.1.
U85772 mRNA. Translation: AAB81564.1.
AF039397
, AF039392, AF039393, AF039394, AF039395, AF039396 Genomic DNA. Translation: AAB94938.1.
AK290852 mRNA. Translation: BAF83541.1.
BX648477 mRNA. Translation: CAI46030.1.
AF001550 Genomic DNA. Translation: AAB67600.1.
CH471228 Genomic DNA. Translation: EAW66863.1.
BC018061 mRNA. Translation: AAH18061.1.
CCDSiCCDS10597.1.
PIRiB46290.
RefSeqiNP_001879.1. NM_001888.4.
UniGeneiHs.924.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I99X-ray2.60A/B2-313[»]
ProteinModelPortaliQ14894.
SMRiQ14894. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107815. 6 interactions.
IntActiQ14894. 2 interactions.
MINTiMINT-4532969.
STRINGi9606.ENSP00000219599.

PTM databases

PhosphoSiteiQ14894.

Polymorphism and mutation databases

BioMutaiCRYM.
DMDMi2498259.

Proteomic databases

MaxQBiQ14894.
PaxDbiQ14894.
PRIDEiQ14894.

Protocols and materials databases

DNASUi1428.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219599; ENSP00000219599; ENSG00000103316.
ENST00000543948; ENSP00000440227; ENSG00000103316.
GeneIDi1428.
KEGGihsa:1428.
UCSCiuc002dil.3. human.

Organism-specific databases

CTDi1428.
GeneCardsiGC16M021269.
HGNCiHGNC:2418. CRYM.
HPAiHPA019086.
MIMi123740. gene.
neXtProtiNX_Q14894.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBiPA26924.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2423.
GeneTreeiENSGT00390000000237.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiQ14894.
KOiK18258.
OMAiKHRGYLG.
PhylomeDBiQ14894.
TreeFamiTF105309.

Miscellaneous databases

ChiTaRSiCRYM. human.
EvolutionaryTraceiQ14894.
GeneWikiiCRYM.
GenomeRNAii1428.
NextBioi5823.
PROiQ14894.
SOURCEiSearch...

Gene expression databases

BgeeiQ14894.
CleanExiHS_CRYM.
ExpressionAtlasiQ14894. baseline and differential.
GenevestigatoriQ14894.

Family and domain databases

Gene3Di3.30.1780.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR003462. ODC_Mu_crystall.
IPR023401. ODC_N.
[Graphical view]
PfamiPF02423. OCD_Mu_crystall. 1 hit.
[Graphical view]
PIRSFiPIRSF001439. CryM. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two roles for mu-crystallin: a lens structural protein in diurnal marsupials and a possible enzyme in mammalian retinas."
    Segovia L., Horwitz J., Gasser R., Wistow G.
    Mol. Vis. 3:9-9(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "Purification, molecular cloning, and functional expression of the human nicotinamide-adenine dinucleotide phosphate-regulated thyroid hormone-binding protein."
    Vie M.-P., Evrard C., Osty J., Breton-Gilet A., Blanchet P., Pomerance M., Rouget P., Francon J., Blondeau J.-P.
    Mol. Endocrinol. 11:1728-1736(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Human and mouse Mu-crystallin."
    Sperbeck S.J., Segovia L., Wistow G.J.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterine endothelium.
  7. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  10. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 4-18; 57-83; 177-186; 243-277 AND 292-314, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  11. "Mu-crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina."
    Kim R.Y., Gasser R., Wistow G.J.
    Proc. Natl. Acad. Sci. U.S.A. 89:9292-9296(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 37-314.
    Tissue: Retina.
  12. "Mammalian forebrain ketimine reductase identified as mu-crystallin; potential regulation by thyroid hormones."
    Hallen A., Cooper A.J., Jamie J.F., Haynes P.A., Willows R.D.
    J. Neurochem. 118:379-387(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KETIMINE REDUCTASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS, PH DEPENDENCE, COFACTOR.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Crystal structure of human micro-crystallin complexed with NADPH."
    Cheng Z., Sun L., He J., Gong W.
    Protein Sci. 16:329-335(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-313 IN COMPLEX WITH NADPH, SUBUNIT, NADP-BINDING SITES.

Entry informationi

Entry nameiCRYM_HUMAN
AccessioniPrimary (citable) accession number: Q14894
Secondary accession number(s): D5MNX0, Q5HYB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.