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Q14894 (CRYM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ketimine reductase mu-crystallin

EC=1.5.1.25
Alternative name(s):
NADP-regulated thyroid-hormone-binding protein
Gene names
Name:CRYM
Synonyms:THBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.12

Catalytic activity

Thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H. Ref.12

Cofactor

NAD or NADP. Ref.12

Subunit structure

Homodimer. Ref.13

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in neural tissue, muscle and kidney.

Sequence similarities

Belongs to the ornithine cyclodeaminase family.

Biophysicochemical properties

Kinetic parameters:

KM=47 µM for 3,4-dehydro-thiomorpholine-3-carboxylate (at pH 5.0 and 37 degrees Celsius) Ref.12

KM=3.6 µM for NADH (at pH 5.0 and 37 degrees Celsius)

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

pH dependence:

Optimum pH is 4.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Ketimine reductase mu-crystallin
PRO_0000200678

Regions

Nucleotide binding143 – 1486NADP

Sites

Binding site1681NADP
Binding site1691NADP

Secondary structure

.......................................................... 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14894 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A49D316B41CE6648

FASTA31433,776
        10         20         30         40         50         60 
MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG 

        70         80         90        100        110        120 
VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT 

       130        140        150        160        170        180 
AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT 

       190        200        210        220        230        240 
VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL 

       250        260        270        280        290        300 
MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT 

       310 
VAAKLIYDSW SSGK 

« Hide

References

« Hide 'large scale' references
[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]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02950 mRNA. Translation: AAC16914.1.
U85772 mRNA. Translation: AAB81564.1.
AF039397 expand/collapse EMBL AC list , 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.
CCDSCCDS10597.1.
PIRB46290.
RefSeqNP_001014444.1. NM_001014444.2.
NP_001879.1. NM_001888.3.
UniGeneHs.924.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I99X-ray2.60A/B2-313[»]
ProteinModelPortalQ14894.
SMRQ14894. Positions 2-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107815. 3 interactions.
IntActQ14894. 2 interactions.
MINTMINT-4532969.
STRING9606.ENSP00000219599.

Chemistry

DrugBankDB00451. Levothyroxine.

PTM databases

PhosphoSiteQ14894.

Polymorphism databases

DMDM2498259.

Proteomic databases

MaxQBQ14894.
PaxDbQ14894.
PRIDEQ14894.

Protocols and materials databases

DNASU1428.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219599; ENSP00000219599; ENSG00000103316.
ENST00000396023; ENSP00000379341; ENSG00000103316.
ENST00000543948; ENSP00000440227; ENSG00000103316.
GeneID1428.
KEGGhsa:1428.
UCSCuc002dil.3. human.

Organism-specific databases

CTD1428.
GeneCardsGC16M021269.
HGNCHGNC:2418. CRYM.
HPAHPA019086.
MIM123740. gene.
neXtProtNX_Q14894.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKBPA26924.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2423.
HOGENOMHOG000137263.
HOVERGENHBG005408.
InParanoidQ14894.
KOK18258.
OMAFANEFED.
PhylomeDBQ14894.
TreeFamTF105309.

Gene expression databases

ArrayExpressQ14894.
BgeeQ14894.
CleanExHS_CRYM.
GenevestigatorQ14894.

Family and domain databases

Gene3D3.30.1780.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR016040. NAD(P)-bd_dom.
IPR003462. ODC_Mu_crystall.
IPR023401. ODC_N.
[Graphical view]
PfamPF02423. OCD_Mu_crystall. 1 hit.
[Graphical view]
PIRSFPIRSF001439. CryM. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ14894.
GeneWikiCRYM.
GenomeRNAi1428.
NextBio5823.
PROQ14894.
SOURCESearch...

Entry information

Entry nameCRYM_HUMAN
AccessionPrimary (citable) accession number: Q14894
Secondary accession number(s): D5MNX0, Q5HYB7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM