PPIAL4C peptidylprolyl isomerase A like 4C [Homo sapiens (human)] - Gene

Summary

Official Symbol: PPIAL4Cprovided by HGNC
Official Full Name: peptidylprolyl isomerase A like 4Cprovided by HGNC
Primary source: HGNC:HGNC:33995
See related: Ensembl:ENSG00000288867 AllianceGenome:HGNC:33995
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: COAS-2
Summary: Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Located in extracellular exosome. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

Location:: 1q21.2

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (149583848..149584607)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (148707993..148708752)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (149553028..149553787)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

PMC262691P6 (e-PCR)
- UniSTS:272328

NoName (e-PCR)
- UniSTS:483537

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity	IEA Inferred from Electronic Annotation more info
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of transcription by RNA polymerase II	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular exosome	HDA more info	PubMed

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase A-like 4A/B/C

Names: PPIase A-like 4A; PPIase A-like 4C; chromosome 1-amplified sequence 2; chromosome one-amplified sequence 2; cyclophilin homolog overexpressed in liver cancer; peptidylprolyl isomerase A (cyclophilin A)-like 4C

NP_001129261.2

EC 5.2.1.8

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_001135789.5 → NP_001129261.2 peptidyl-prolyl cis-trans isomerase A-like 4A/B/C

See identical proteins and their annotated locations for NP_001129261.2

Status: VALIDATED

Source sequence(s)

AC242842

Consensus CDS

CCDS72898.1

UniProtKB/Swiss-Prot

A0A0B4J2A2

UniProtKB/TrEMBL

A0A0H2UH34

Related

ENSP00000463057.2, ENST00000585245.3

Conserved Domains (1) summary

cl00197
Location:4 → 162

cyclophilin; cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the ...