Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000052

Gene Ontology annotation based on curation of immunofluorescence data

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:15063763

LEPREL1, a novel ER and Golgi resident member of the Leprecan family.

LEPREL1/P3H2 is an 80 kDa, 708-residue ER/Golgi-resident protein of the leprecan family with a signal sequence, four TPRs, a P4Halpha domain, and a C-terminal KDEL ER-retention motif; over-expression perturbs ER PDI staining.

PMID:18487197

Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV.

Recombinant human P3H2 has prolyl 3-hydroxylase activity on (Gly-Pro-4Hyp)5 and preferentially hydroxylates collagen IV-derived peptides over a collagen I site, identifying P3H2 as the collagen IV-modifying isoenzyme; it is enriched in basement-membrane-rich tissues such as kidney and does not require CRTAP.

PMID:19436308

The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer.

P3H2 (and P3H3) are silenced by promoter CpG hypermethylation in breast cancer; ectopic re-expression of P3H2 in silenced breast cancer cell lines suppresses colony growth, implying tumor-suppressor-like anti-proliferative activity.

PMID:29491144

Post-translational modification of type IV collagen with 3-hydroxyproline affects its interactions with glycoprotein VI and nidogens 1 and 2.

Using P3H2-knockout PFHR-9 cells and tandem MS, P3H2 is shown to be the major (but not the only) 3-hydroxyproline-modifying enzyme of type IV collagen; 3-Hyp on collagen IV modulates its interactions with glycoprotein VI (reduced 3-Hyp increases GP6 binding) and is required for nidogen 1/2 binding.

PMID:33918807

Prolyl 3-Hydroxylase 2 Is a Molecular Player of Angiogenesis.

P3H2 is induced by VEGF-A in human endothelial cells via VEGFR-2/p38 MAPK signaling; through its activity on type IV collagen it is required for angiogenic properties in vitro, and P3H2 knockdown prevents pathological angiogenesis in a laser-induced choroidal neovascularization model.

PMID:35499085

Loss of the collagen IV modifier prolyl 3-hydroxylase 2 causes thin basement membrane nephropathy.

P3H2 was identified as a glomerular basement membrane (GBM) modifier in a cohort of patients with albuminuria; it 3-hydroxylates prolines in collagen IV subchains in the ER, and podocyte-specific loss in mice produces a thin basement membrane nephropathy (TBMN) phenotype with progressive microhematuria and microalbuminuria. Loss/mutation of P3H2 causes TBMN and focal segmental glomerulosclerosis (FSGS) in mice and humans.

Reactome:R-HSA-1980233

Collagen prolyl 3-hydroxylase converts 4-Hyp collagen to 3,4-Hyp collagen

Reactome:R-HSA-8948226

Prolyl 3-hydroxylases:Fe2+:3,4-Hyp collagen propeptides dissociates

Reactome:R-HSA-8948230

P3HB binds 4-Hyp-collagen propeptides

file:human/P3H2/P3H2-uniprot.txt

UniProt entry Q8IVL5 (P3H2_HUMAN), prolyl 3-hydroxylase 2

ER-lumenal 2-oxoglutarate/Fe(II)-dependent dioxygenase (EC 1.14.11.7) that 3-hydroxylates procollagen prolyl residues (high activity on collagen IV/COL4A1, lower on COL1A1); uses Fe cation and L-ascorbate cofactors; contains an Fe2OG dioxygenase domain and a C-terminal KDEL-type ER-retention motif; ER/sarcoplasmic reticulum/Golgi localization; loss-of-function variant causes MCVD high myopia.