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Protein

Ketimine reductase mu-crystallin

Gene

Crym

Organism
Mus musculus (Mouse)
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 (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)DescriptionActionsGraphical viewLength
Binding sitei167NADPBy similarity1
Binding sitei168NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 147NADPBy similarity6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

ReactomeiR-MMU-71064. Lysine catabolism.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:102675. Crym.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002006791 – 313Ketimine reductase mu-crystallinAdd BLAST313

Proteomic databases

PaxDbiO54983.
PeptideAtlasiO54983.
PRIDEiO54983.

PTM databases

iPTMnetiO54983.
PhosphoSitePlusiO54983.

Expressioni

Gene expression databases

BgeeiENSMUSG00000030905.
CleanExiMM_CRYM.
ExpressionAtlasiO54983. baseline and differential.
GenevisibleiO54983. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiO54983. 4 interactors.
MINTiMINT-4092055.
STRINGi10090.ENSMUSP00000033198.

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi10 – 15Combined sources6
Helixi20 – 35Combined sources16
Helixi37 – 40Combined sources4
Beta strandi48 – 52Combined sources5
Helixi53 – 55Combined sources3
Beta strandi57 – 66Combined sources10
Turni67 – 70Combined sources4
Beta strandi71 – 80Combined sources10
Beta strandi91 – 98Combined sources8
Turni100 – 102Combined sources3
Beta strandi105 – 111Combined sources7
Helixi112 – 130Combined sources19
Beta strandi137 – 141Combined sources5
Helixi145 – 157Combined sources13
Beta strandi161 – 166Combined sources6
Helixi170 – 179Combined sources10
Beta strandi180 – 182Combined sources3
Beta strandi184 – 186Combined sources3
Helixi190 – 194Combined sources5
Beta strandi198 – 202Combined sources5
Helixi213 – 215Combined sources3
Beta strandi221 – 224Combined sources4
Helixi237 – 242Combined sources6
Beta strandi243 – 248Combined sources6
Helixi250 – 256Combined sources7
Helixi258 – 263Combined sources6
Helixi271 – 275Combined sources5
Beta strandi287 – 290Combined sources4
Helixi295 – 311Combined sources17

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3007. Eukaryota.
COG2423. LUCA.
GeneTreeiENSGT00390000000237.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiO54983.
KOiK18258.
OMAiQRNLVNM.
OrthoDBiEOG091G0NR8.
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.
SUPFAMiSSF51735. SSF51735. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BV8X-ray2.30A/B1-313[»]
4BV9X-ray2.19A/B1-313[»]
4BVAX-ray1.75A/B1-313[»]
ProteinModelPortaliO54983.
SMRiO54983.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54983. 4 interactors.
MINTiMINT-4092055.
STRINGi10090.ENSMUSP00000033198.

PTM databases

iPTMnetiO54983.
PhosphoSitePlusiO54983.

Proteomic databases

PaxDbiO54983.
PeptideAtlasiO54983.
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

eggNOGiKOG3007. Eukaryota.
COG2423. LUCA.
GeneTreeiENSGT00390000000237.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiO54983.
KOiK18258.
OMAiQRNLVNM.
OrthoDBiEOG091G0NR8.
PhylomeDBiO54983.
TreeFamiTF105309.

Enzyme and pathway databases

ReactomeiR-MMU-71064. Lysine catabolism.

Miscellaneous databases

ChiTaRSiCrym. mouse.
PROiO54983.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030905.
CleanExiMM_CRYM.
ExpressionAtlasiO54983. baseline and differential.
GenevisibleiO54983. MM.

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.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 112 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

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 one 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.