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Protein

Ketimine reductase mu-crystallin

Gene

Crym

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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

  • mitochondrial transport Source: RGD
  • response to hormone Source: RGD
  • response to vitamin D Source: RGD
  • thyroid hormone metabolic process Source: GO_Central

Keywordsi

Molecular functionOxidoreductase
LigandNAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Ketimine reductase mu-crystallin (EC:1.5.1.25)
Alternative name(s):
CDK108
NADP-regulated thyroid-hormone-binding protein
Gene namesi
Name:Crym
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi

Organism-specific databases

RGDi620943 Crym

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002006801 – 313Ketimine reductase mu-crystallinAdd BLAST313

Proteomic databases

PaxDbiQ9QYU4
PRIDEiQ9QYU4

2D gel databases

World-2DPAGEi0004:Q9QYU4

PTM databases

iPTMnetiQ9QYU4
PhosphoSitePlusiQ9QYU4

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi250625, 1 interactor
STRINGi10116.ENSRNOP00000066476

Structurei

3D structure databases

ProteinModelPortaliQ9QYU4
SMRiQ9QYU4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3007 Eukaryota
COG2423 LUCA
HOVERGENiHBG005408
InParanoidiQ9QYU4
KOiK18258
PhylomeDBiQ9QYU4

Family and domain databases

Gene3Di3.30.1780.10, 2 hits
InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR003462 ODC_Mu_crystall
IPR023401 ODC_N
PANTHERiPTHR13812 PTHR13812, 1 hit
PfamiView protein in Pfam
PF02423 OCD_Mu_crystall, 1 hit
PIRSFiPIRSF001439 CryM, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

Sequencei

Sequence statusi: Complete.

Q9QYU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRAPAFLSA DEVQDHLRSS SLLIPPLEAA LANFSKGPDG GVMQPVRTVV
60 70 80 90 100
PVAKHRGFLG VMPAYSAAED ALTTKLVTFY EGHSNNAVPS HQASVLLFDP
110 120 130 140 150
SNGSLLAVMD GNVITAKRTA AVSAIATKFL KPPGSDVLCI LGAGVQAYSH
160 170 180 190 200
YEIFTEQFSF KEVRMWNRTR ENAEKFASSV QGDVRVCSSV QEAVTGADVI
210 220 230 240 250
ITVTMATEPI LFGEWVKPGA HINAVGASRP DWRELDDELM KQAVLYVDSR
260 270 280 290 300
EAALKESGDV LLSGADIFAE LGEVVSGAKP AYCEKTTVFK SLGMAVEDLV
310
AAKLVYDSWS SGK
Length:313
Mass (Da):33,554
Last modified:May 1, 2000 - v1
Checksum:iE2F1839D9E5EC5ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17328 mRNA Translation: CAB56625.1
BC088121 mRNA Translation: AAH88121.1
RefSeqiNP_446407.1, NM_053955.1
UniGeneiRn.24561

Genome annotation databases

GeneIDi117024
KEGGirno:117024

Entry informationi

Entry nameiCRYM_RAT
AccessioniPrimary (citable) accession number: Q9QYU4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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