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Protein

Ketimine reductase mu-crystallin

Gene

Crym

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

NAD(+)By similarity, NADP(+)By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671NADPBy similarity
Binding sitei168 – 1681NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1476NADPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  2. sensory perception of sound Source: MGI
  3. thyroid hormone metabolic process Source: MGI
  4. thyroid hormone transport Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:102675. Crym.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Ketimine reductase mu-crystallinPRO_0000200679Add
BLAST

Proteomic databases

MaxQBiO54983.
PaxDbiO54983.
PRIDEiO54983.

PTM databases

PhosphoSiteiO54983.

Expressioni

Gene expression databases

BgeeiO54983.
CleanExiMM_CRYM.
ExpressionAtlasiO54983. baseline and differential.
GenevestigatoriO54983.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiO54983. 3 interactions.
MINTiMINT-4092055.
STRINGi10090.ENSMUSP00000033198.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi10 – 156Combined sources
Helixi20 – 3516Combined sources
Helixi37 – 404Combined sources
Beta strandi48 – 525Combined sources
Helixi53 – 553Combined sources
Beta strandi57 – 6610Combined sources
Turni67 – 704Combined sources
Beta strandi71 – 8010Combined sources
Beta strandi91 – 988Combined sources
Turni100 – 1023Combined sources
Beta strandi105 – 1117Combined sources
Helixi112 – 13019Combined sources
Beta strandi137 – 1415Combined sources
Helixi145 – 15713Combined sources
Beta strandi161 – 1666Combined sources
Helixi170 – 17910Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1863Combined sources
Helixi190 – 1945Combined sources
Beta strandi198 – 2025Combined sources
Helixi213 – 2153Combined sources
Beta strandi221 – 2244Combined sources
Helixi237 – 2426Combined sources
Beta strandi243 – 2486Combined sources
Helixi250 – 2567Combined sources
Helixi258 – 2636Combined sources
Helixi271 – 2755Combined sources
Beta strandi287 – 2904Combined sources
Helixi295 – 31117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BV8X-ray2.30A/B1-313[»]
4BV9X-ray2.19A/B1-313[»]
4BVAX-ray1.75A/B1-313[»]
ProteinModelPortaliO54983.
SMRiO54983. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2423.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiO54983.
KOiK18258.
OMAiKHRGYLG.
OrthoDBiEOG7S7SFB.
PhylomeDBiO54983.
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.

O54983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRAPAFLSA EEVQDHLRSS SLLIPPLEAA LANFSKGPDG GVMQPVRTVV
60 70 80 90 100
PVAKHRGFLG VMPAYSAAED ALTTKLVTFY EGHSNTAVPS HQASVLLFDP
110 120 130 140 150
SNGSLLAVMD GNVITAKRTA AVSAIATKLL KPPGSDVLCI LGAGVQAYSH
160 170 180 190 200
YEIFTEQFSF KEVRMWNRTR ENAEKFASTV QGDVRVCSSV QEAVTGADVI
210 220 230 240 250
ITVTMATEPI LFGEWVKPGA HINAVGASRP DWRELDDELM RQAVLYVDSR
260 270 280 290 300
EAALKESGDV LLSGADIFAE LGEVISGAKP AHCEKTTVFK SLGMAVEDLV
310
AAKLVYDSWS SGK
Length:313
Mass (Da):33,523
Last modified:June 1, 1998 - v1
Checksum:i0898EDA9E2D34C83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039391 mRNA. Translation: AAB94770.1.
BC045159 mRNA. Translation: AAH45159.1.
CCDSiCCDS21794.1.
RefSeqiNP_057878.1. NM_016669.1.
UniGeneiMm.9114.

Genome annotation databases

EnsembliENSMUST00000033198; ENSMUSP00000033198; ENSMUSG00000030905.
GeneIDi12971.
KEGGimmu:12971.
UCSCiuc009jmk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039391 mRNA. Translation: AAB94770.1.
BC045159 mRNA. Translation: AAH45159.1.
CCDSiCCDS21794.1.
RefSeqiNP_057878.1. NM_016669.1.
UniGeneiMm.9114.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BV8X-ray2.30A/B1-313[»]
4BV9X-ray2.19A/B1-313[»]
4BVAX-ray1.75A/B1-313[»]
ProteinModelPortaliO54983.
SMRiO54983. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54983. 3 interactions.
MINTiMINT-4092055.
STRINGi10090.ENSMUSP00000033198.

PTM databases

PhosphoSiteiO54983.

Proteomic databases

MaxQBiO54983.
PaxDbiO54983.
PRIDEiO54983.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033198; ENSMUSP00000033198; ENSMUSG00000030905.
GeneIDi12971.
KEGGimmu:12971.
UCSCiuc009jmk.1. mouse.

Organism-specific databases

CTDi1428.
MGIiMGI:102675. Crym.

Phylogenomic databases

eggNOGiCOG2423.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiO54983.
KOiK18258.
OMAiKHRGYLG.
OrthoDBiEOG7S7SFB.
PhylomeDBiO54983.
TreeFamiTF105309.

Miscellaneous databases

ChiTaRSiCrym. mouse.
NextBioi282732.
PROiO54983.
SOURCEiSearch...

Gene expression databases

BgeeiO54983.
CleanExiMM_CRYM.
ExpressionAtlasiO54983. baseline and differential.
GenevestigatoriO54983.

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. Sperbeck S.J., Segovia L., Wistow G.J.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/N.
    Tissue: Brain.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Retina.
  3. Lubec G., Kang S.U.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 4-18; 37-47; 119-128 AND 176-185, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiCRYM_MOUSE
AccessioniPrimary (citable) accession number: O54983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: March 4, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.