P3H2_RAT
ID P3H2_RAT Reviewed; 703 AA.
AC Q4KLM6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Prolyl 3-hydroxylase 2 {ECO:0000312|RGD:1304568};
DE EC=1.14.11.7 {ECO:0000305|PubMed:21757687};
DE AltName: Full=Leprecan-like protein 1 {ECO:0000250|UniProtKB:Q8IVL5};
DE Flags: Precursor;
GN Name=P3h2 {ECO:0000312|RGD:1304568};
GN Synonyms=Leprel1 {ECO:0000250|UniProtKB:Q8IVL5};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION AS PROLYL-3-HYDROXYLASE, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=21757687; DOI=10.1074/jbc.m111.267906;
RA Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.;
RT "A role for prolyl 3-hydroxylase 2 in post-translational modification of
RT fibril-forming collagens.";
RL J. Biol. Chem. 286:30662-30669(2011).
CC -!- FUNCTION: Prolyl 3-hydroxylase that catalyzes the post-translational
CC formation of 3-hydroxyproline on collagens (PubMed:21757687).
CC Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in
CC tendons, the eye sclera and in the eye lens capsule (By similarity).
CC Has high activity with the type IV collagen COL4A1, and lower activity
CC with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp
CC sequences where Hyp is 4-hydroxyproline. Has no activity on substrates
CC that lack 4-hydroxyproline in the third position (By similarity).
CC {ECO:0000250|UniProtKB:Q8CG71, ECO:0000250|UniProtKB:Q8IVL5,
CC ECO:0000305|PubMed:21757687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-3-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:22872, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11678, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; EC=1.14.11.7;
CC Evidence={ECO:0000305|PubMed:21757687};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q8IVL5};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q8IVL5};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8IVL5, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q8IVL5}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8IVL5}.
CC -!- TISSUE SPECIFICITY: Detected at low levels in cartilage.
CC {ECO:0000269|PubMed:21757687}.
CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
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DR EMBL; BC099107; AAH99107.1; -; mRNA.
DR RefSeq; NP_001020798.1; NM_001025627.1.
DR AlphaFoldDB; Q4KLM6; -.
DR STRING; 10116.ENSRNOP00000002639; -.
DR GlyGen; Q4KLM6; 3 sites.
DR iPTMnet; Q4KLM6; -.
DR PhosphoSitePlus; Q4KLM6; -.
DR PaxDb; Q4KLM6; -.
DR PRIDE; Q4KLM6; -.
DR Ensembl; ENSRNOT00000089540; ENSRNOP00000074673; ENSRNOG00000055751.
DR GeneID; 288016; -.
DR KEGG; rno:288016; -.
DR UCSC; RGD:1304568; rat.
DR CTD; 55214; -.
DR RGD; 1304568; P3h2.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000159593; -.
DR InParanoid; Q4KLM6; -.
DR OrthoDB; 660619at2759; -.
DR PhylomeDB; Q4KLM6; -.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:Q4KLM6; -.
DR Proteomes; UP000002494; Chromosome 11.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0032963; P:collagen metabolic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR039838; P3H2.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14049; PTHR14049; 1.
DR PANTHER; PTHR14049:SF1; PTHR14049:SF1; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..703
FT /note="Prolyl 3-hydroxylase 2"
FT /id="PRO_0000240358"
FT REPEAT 42..75
FT /note="TPR 1"
FT REPEAT 144..177
FT /note="TPR 2"
FT REPEAT 205..238
FT /note="TPR 3"
FT REPEAT 301..334
FT /note="TPR 4"
FT DOMAIN 552..666
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 18..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 700..703
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 657
FT /evidence="ECO:0000250"
FT BINDING 575
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 577
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 647
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 703 AA; 79833 MW; EFE57CEF5F209B63 CRC64;
MRESTWVSLL LLLLLPAPQR GGPQDGRGSP EPEPERGPLQ PFDLLYASGV AAYYSGDYEG
AVRDLEAALR SHRRLRDIRT RCARHCAARR PLAPPGAGPG AELPFFRAVL ERARCSRSCQ
SQRLGGPASR HRVSEDVRSD FQRRVPYNYL QRAYIKLNQL DKAMEAAHTF FMANPEHMEM
QQNIEDYKAT ARVEAPLVDR EAKPHLESYN AGVKHYEADD FEAAIKYFEQ ALREYFNEDM
VCRALCEGPQ RFEEYEYLGS KGSLYEAIAD HYMQVLVCQH ECVRELATRP GRLSPIENFL
PLHYDYLQFA YYRVGEYVKA LECAKAYLMF HPDDQDVLDN VDFYESLLDD STDPASIEAR
EDLTAFVKRH KLEAELIKSA AEGLGFSYSE PNYWISYGGR QDENRVPSGV NMDGAEVHGL
SMGKKSPPKI GRDLREGGPL LYENITFVYN SEQLNGTQRV LLDNVLSEEQ CRELHSVASG
IMLVGDGYRG KTSPHTPNEK FEGATVLKAL KFGYEGRVPL KSARLFYDIS EKARKIVESY
FMLNSTLYFS YTHMVCRTAL SGQQDRRNDL SHPIHADNCL LDPEANECWK EPPAYTFRDY
SALLYMNDDF EGGEFIFTEM DAKTVTASIK PKCGRMISFS SGGENPHGVK AVTRGQRCAV
ALWFTLDPLY RELERIQADE VIAILDQEQH GKHGLNINPK DEL
