serpinc1 serpin peptidase inhibitor, clade C (antithrombin), member 1 [Danio rerio (zebrafish)] - Gene

Summary

Official Symbol: serpinc1provided by ZNC
Official Full Name: serpin peptidase inhibitor, clade C (antithrombin), member 1provided by ZNC
Primary source: ZFIN:ZDB-GENE-030131-264
See related: Ensembl:ENSDARG00000042684 AllianceGenome:ZFIN:ZDB-GENE-030131-264
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Danio rerio
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio
Also known as: zgc:92299; wu:fb18f10
Summary: Predicted to enable serine-type endopeptidase inhibitor activity. Acts upstream of or within cellular response to estrogen stimulus and regulation of blood coagulation. Predicted to be located in extracellular region. Predicted to be active in extracellular space. Is expressed in liver; yolk; and yolk syncytial layer. Used to study disseminated intravascular coagulation. Human ortholog(s) of this gene implicated in antithrombin III deficiency; disseminated intravascular coagulation; intermediate coronary syndrome; thrombosis; and toxic shock syndrome. Orthologous to human SERPINC1 (serpin family C member 1). [provided by Alliance of Genome Resources, Dec 2024]
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 22

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCz11 (GCF_000002035.6)	22	NC_007133.7 (16022211..16028191)
105	previous assembly	GRCz10 (GCF_000002035.5)	22	NC_007133.6 (15995941..16001921)

Chromosome 22 - NC_007133.7 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: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
Description: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
BioProject: PRJEB1986
Analysis date: Fri Dec 8 19:48:10 2017

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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General gene information

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Gene Ontology Provided by ZFIN

Function	Evidence Code	Pubs
enables serine-type endopeptidase inhibitor activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within cellular response to estrogen stimulus	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within regulation of blood coagulation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in extracellular region	IEA Inferred from Electronic Annotation more info
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: antithrombin-III

Names: ATIII; antithrombin III; at3; serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1

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_182863.1 → NP_878283.1 antithrombin-III precursor

See identical proteins and their annotated locations for NP_878283.1

Status: PROVISIONAL

Source sequence(s)

AF515272

UniProtKB/TrEMBL

Q66HW6, Q8AYE3

Related

ENSDARP00000062617.4, ENSDART00000062618.5

Conserved Domains (1) summary

cd02045
Location:62 → 443

antithrombin-III_like; Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of coagulation. It is the most important anticoagulant molecule in mammalian circulation systems, controlled by its interaction with the co-factor, heparin, which ...