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Q14894

- CRYM_HUMAN

UniProt

Q14894 - CRYM_HUMAN

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Protein
Ketimine reductase mu-crystallin
Gene
CRYM, THBP
Organism
Homo sapiens (Human)
Status
Reviewed - 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 or NADP.1 Publication

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)

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 dependencei

Optimum pH is 4.5.

Sites

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

Regions

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

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: Chromosome 16

Organism-specific databases

HGNCiHGNC:2418. CRYM.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

Orphaneti90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKBiPA26924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Ketimine reductase mu-crystallin
PRO_0000200678Add
BLAST

Proteomic databases

MaxQBiQ14894.
PaxDbiQ14894.
PRIDEiQ14894.

PTM databases

PhosphoSiteiQ14894.

Expressioni

Tissue specificityi

Expressed in neural tissue, muscle and kidney.

Gene expression databases

ArrayExpressiQ14894.
BgeeiQ14894.
CleanExiHS_CRYM.
GenevestigatoriQ14894.

Organism-specific databases

HPAiHPA019086.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi107815. 3 interactions.
IntActiQ14894. 2 interactions.
MINTiMINT-4532969.
STRINGi9606.ENSP00000219599.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I99X-ray2.60A/B2-313[»]
ProteinModelPortaliQ14894.
SMRiQ14894. Positions 2-313.

Miscellaneous databases

EvolutionaryTraceiQ14894.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2423.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiQ14894.
KOiK18258.
OMAiFANEFED.
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

MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV    50
PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE 100
PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS 150
HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV 200
IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS 250
QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT 300
VAAKLIYDSW SSGK 314
Length:314
Mass (Da):33,776
Last modified:November 1, 1997 - v1
Checksum:iA49D316B41CE6648
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001014444.1. NM_001014444.2.
NP_001879.1. NM_001888.3.
UniGeneiHs.924.

Genome annotation databases

EnsembliENST00000219599; ENSP00000219599; ENSG00000103316.
ENST00000396023; ENSP00000379341; ENSG00000103316.
ENST00000543948; ENSP00000440227; ENSG00000103316.
GeneIDi1428.
KEGGihsa:1428.
UCSCiuc002dil.3. human.

Polymorphism databases

DMDMi2498259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10597.1.
PIRi B46290.
RefSeqi NP_001014444.1. NM_001014444.2.
NP_001879.1. NM_001888.3.
UniGenei Hs.924.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I99 X-ray 2.60 A/B 2-313 [» ]
ProteinModelPortali Q14894.
SMRi Q14894. Positions 2-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107815. 3 interactions.
IntActi Q14894. 2 interactions.
MINTi MINT-4532969.
STRINGi 9606.ENSP00000219599.

Chemistry

DrugBanki DB00451. Levothyroxine.

PTM databases

PhosphoSitei Q14894.

Polymorphism databases

DMDMi 2498259.

Proteomic databases

MaxQBi Q14894.
PaxDbi Q14894.
PRIDEi Q14894.

Protocols and materials databases

DNASUi 1428.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219599 ; ENSP00000219599 ; ENSG00000103316 .
ENST00000396023 ; ENSP00000379341 ; ENSG00000103316 .
ENST00000543948 ; ENSP00000440227 ; ENSG00000103316 .
GeneIDi 1428.
KEGGi hsa:1428.
UCSCi uc002dil.3. human.

Organism-specific databases

CTDi 1428.
GeneCardsi GC16M021269.
HGNCi HGNC:2418. CRYM.
HPAi HPA019086.
MIMi 123740. gene.
neXtProti NX_Q14894.
Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKBi PA26924.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2423.
HOGENOMi HOG000137263.
HOVERGENi HBG005408.
InParanoidi Q14894.
KOi K18258.
OMAi FANEFED.
PhylomeDBi Q14894.
TreeFami TF105309.

Miscellaneous databases

EvolutionaryTracei Q14894.
GeneWikii CRYM.
GenomeRNAii 1428.
NextBioi 5823.
PROi Q14894.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14894.
Bgeei Q14894.
CleanExi HS_CRYM.
Genevestigatori Q14894.

Family and domain databases

Gene3Di 3.30.1780.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR016040. NAD(P)-bd_dom.
IPR003462. ODC_Mu_crystall.
IPR023401. ODC_N.
[Graphical view ]
Pfami PF02423. OCD_Mu_crystall. 1 hit.
[Graphical view ]
PIRSFi PIRSF001439. CryM. 1 hit.
ProtoNeti Search...

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. "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: July 9, 2014
This is version 134 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

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