cfd complement factor D (adipsin) [Danio rerio (zebrafish)] - Gene

Summary

Official Symbol: cfdprovided by ZNC
Official Full Name: complement factor D (adipsin)provided by ZNC
Primary source: ZFIN:ZDB-GENE-050522-411
See related: Ensembl:ENSDARG00000039579 AllianceGenome:ZFIN:ZDB-GENE-050522-411
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: cfdl; fb61f12; zgc:92376; wu:fb61f12; zgc:109940
Summary: Predicted to enable serine-type endopeptidase activity. Predicted to be involved in protein maturation. Predicted to act upstream of or within proteolysis. Predicted to be active in extracellular space. Is expressed in adipose tissue; epidermis; periderm; pharyngeal arch; and pleuroperitoneal region. Orthologous to human CFD (complement factor D). [provided by Alliance of Genome Resources, Dec 2024]
Orthologs: all
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Genomic context

Location:: chromosome: 13

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCz11 (GCF_000002035.6)	13	NC_007124.7 (13681679..13684334)
105	previous assembly	GRCz10 (GCF_000002035.5)	13	NC_007124.6 (13550687..13553342)

Chromosome 13 - NC_007124.7 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?

Submit: New GeneRIF Correction

General gene information

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Markers

fc26a08.x1 (e-PCR)
- UniSTS:193293

fb61f12 (e-PCR)
- UniSTS:187305

Gene Ontology Provided by ZFIN

Function	Evidence Code	Pubs
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables peptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type peptidase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in protein maturation	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: complement factor D

Names: complement factor D (adipsin) like

NP_001018368.1

EC 3.4.21.46

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_001020532.1 → NP_001018368.1 complement factor D precursor

See identical proteins and their annotated locations for NP_001018368.1

Status: PROVISIONAL

Source sequence(s)

BC095067

UniProtKB/TrEMBL

B2GSA9, Q504D6, Q6DBS8

Related

ENSDARP00000057824.4, ENSDART00000057825.5

Conserved Domains (2) summary

smart00020
Location:21 → 243

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:21 → 246

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...