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Q14894

- CRYM_HUMAN

UniProt

Q14894 - CRYM_HUMAN

Protein

Ketimine reductase mu-crystallin

Gene

CRYM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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.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

    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

    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-crystallinPRO_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

    1
    314
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14894.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ornithine cyclodeaminase family.Curated

    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.
    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 .
    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

    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: October 1, 2014
    This is version 135 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