Scly selenocysteine lyase [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Sclyprovided by RGD
Official Full Name: selenocysteine lyaseprovided by RGD
Primary source: RGD:1359514
See related: EnsemblRapid:ENSRNOG00000020083 AllianceGenome:RGD:1359514
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables several functions, including protein homodimerization activity; selenocysteine lyase activity; and vitamin B6 binding activity. Involved in selenocysteine catabolic process. Part of catalytic complex. Orthologous to human SCLY (selenocysteine lyase). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in Kidney (RPKM 329.3), Liver (RPKM 195.9) and 8 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 9q36

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	9	NC_086027.1 (99337796..99358487)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	9	NC_051344.1 (91890269..91910947)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	9	NC_005108.4 (98438408..98459075)

Chromosome 9 - NC_086027.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

ESI-MS analysis of wild-type and C375A mutant SCL revealed that the catalytic reaction proceeds via the formation of an enzyme-bound selenopersulfide intermediate on the catalytically essential Cys-375 residue.
Title: Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.
An enhancer element between bp -152 and -298 of the SCL 5'-regulatory region was identified, with protein binding to an AP-1 binding site that may be involved in the regulation of SCL-RNA in vivo in an endogenous feedback mechanism.
Title: Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1.

Submit: New GeneRIF Correction

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables amino acid binding	IDA Inferred from Direct Assay more info	PubMed
enables lyase activity	IEA Inferred from Electronic Annotation more info
enables protein homodimerization activity	IDA Inferred from Direct Assay more info	PubMed
enables selenocysteine lyase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info
enables vitamin B6 binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within lipid metabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within negative regulation of cellular response to oxidative stress	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within response to insulin	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within selenium compound metabolic process	ISO Inferred from Sequence Orthology more info
involved_in selenocysteine catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
located_in Golgi apparatus	ISO Inferred from Sequence Orthology more info
part_of catalytic complex	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: selenocysteine lyase

NP_001007756.1

EC 4.4.1.16

XP_008765499.1

EC 4.4.1.16

XP_038939851.1

EC 4.4.1.16

XP_063123527.1

EC 4.4.1.16

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001007755.2 → NP_001007756.1 selenocysteine lyase

See identical proteins and their annotated locations for NP_001007756.1

Status: VALIDATED

Source sequence(s)

JAXUCZ010000009

UniProtKB/Swiss-Prot

Q68FT9

UniProtKB/TrEMBL

A0A8I6AR35

Related

ENSRNOP00000027220.5, ENSRNOT00000027220.7

Conserved Domains (1) summary

COG1104
Location:18 → 428

NifS; Cysteine sulfinate desulfinase/cysteine desulfurase or related enzyme [Amino acid transport and metabolism]

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

NC_086027.1 Reference GRCr8

Range

99337796..99358487

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_063267457.1 → XP_063123527.1 selenocysteine lyase isoform X3
XM_008767277.4 → XP_008765499.1 selenocysteine lyase isoform X1

UniProtKB/TrEMBL

A0A8I6AR35

Conserved Domains (1) summary

COG1104
Location:83 → 454

NifS; Cysteine sulfinate desulfinase/cysteine desulfurase or related enzyme [Amino acid transport and metabolism]
XM_039083923.2 → XP_038939851.1 selenocysteine lyase isoform X2

Conserved Domains (1) summary

cl18945
Location:83 → 273

AAT_I; Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the ...