P3H1_RAT
ID P3H1_RAT Reviewed; 728 AA.
AC Q9R1J8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Prolyl 3-hydroxylase 1 {ECO:0000312|RGD:628823};
DE EC=1.14.11.7;
DE AltName: Full=Leucine- and proline-enriched proteoglycan 1 {ECO:0000303|PubMed:10455179};
DE Short=Leprecan-1 {ECO:0000303|PubMed:10455179};
DE Flags: Precursor;
GN Name=P3h1 {ECO:0000312|RGD:628823};
GN Synonyms=Lepre1 {ECO:0000303|PubMed:10455179};
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 [MRNA], GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=10455179; DOI=10.1074/jbc.274.35.25004;
RA Wassenhove-McCarthy D.J., McCarthy K.J.;
RT "Molecular characterization of a novel basement membrane-associated
RT proteoglycan, leprecan.";
RL J. Biol. Chem. 274:25004-25017(1999).
CC -!- FUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan
CC (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-
CC translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences
CC in collagens, especially types IV and V. May be involved in the
CC secretory pathway of cells. Has growth suppressive activity in
CC fibroblasts (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:10455179}. Secreted, extracellular
CC space, extracellular matrix {ECO:0000269|PubMed:10455179}.
CC Note=Secreted into the extracellular matrix as a chondroitin sulfate
CC proteoglycan (CSPG).
CC -!- TISSUE SPECIFICITY: Expressed in basement membranes of cardiac muscle,
CC skeletal muscle, central nervous system, intestinal tract, trachea,
CC ear, skin, liver and kidney. In kidney, localizes to the glomerular
CC basement membrane, mesangial matrix and Bowman's capsule of the
CC nephron. In the renal parenchyma, expressed in the basement membranes
CC of tubules and blood vessels. In the ear and trachea, localizes to the
CC perimeter of resident chondrocytes in lacunae.
CC {ECO:0000269|PubMed:10455179}.
CC -!- PTM: O-glycosylated; chondroitin sulfate.
CC {ECO:0000269|PubMed:10455179}.
CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
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DR EMBL; AF087433; AAD51875.1; -; mRNA.
DR RefSeq; NP_446119.1; NM_053667.1.
DR AlphaFoldDB; Q9R1J8; -.
DR IntAct; Q9R1J8; 1.
DR STRING; 10116.ENSRNOP00000010395; -.
DR GlyGen; Q9R1J8; 4 sites.
DR jPOST; Q9R1J8; -.
DR PaxDb; Q9R1J8; -.
DR GeneID; 114200; -.
DR KEGG; rno:114200; -.
DR UCSC; RGD:628823; rat.
DR CTD; 64175; -.
DR RGD; 628823; P3h1.
DR eggNOG; KOG4459; Eukaryota.
DR InParanoid; Q9R1J8; -.
DR OrthoDB; 660619at2759; -.
DR PhylomeDB; Q9R1J8; -.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:Q9R1J8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0032963; P:collagen metabolic process; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:1901874; P:negative regulation of post-translational protein modification; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0018126; P:protein hydroxylation; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0030278; P:regulation of ossification; ISO:RGD.
DR GO; GO:0050708; P:regulation of protein secretion; ISO:RGD.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR039837; P3H1.
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:SF5; PTHR14049:SF5; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Dioxygenase; Endoplasmic reticulum; Extracellular matrix;
KW Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Secreted; Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..728
FT /note="Prolyl 3-hydroxylase 1"
FT /id="PRO_0000240354"
FT REPEAT 25..58
FT /note="TPR 1"
FT REPEAT 135..168
FT /note="TPR 2"
FT REPEAT 197..230
FT /note="TPR 3"
FT REPEAT 293..326
FT /note="TPR 4"
FT DOMAIN 556..670
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 691..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..431
FT /evidence="ECO:0000255"
FT MOTIF 725..728
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 714..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 661
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 581
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 651
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 728 AA; 82390 MW; 06AFE6972BF3EE1F CRC64;
MVAVAAAAAS RATAESEPEW NVAAPDLLYA EGTAAYARGD WPGVVLNMER ALRSRAALRA
LRLRCRTRCA TELPWAPDLD LGPASSLNHD PGAAALHDLR FFGALLRRAA CLRRCLGPPS
AHLLSEELDL EFNKRSPYNY LQVAYFKINK LEKAVAAAHT FFVGNPEHME MRQNLDYYQT
MSGVKEEDFK DLEAKPHMHE FRLGVRLYSE EKPLEAVPHL EAALQEYFVA DEECRALCEG
PYDYDGYNYL DYSADLFQAI TDHYVQVLSC KQNCVTELAS HPSREKPFED FLPSHYNYLQ
FAYYNIGNYT QAIECAKTYL LFFPNDEVMS QNLAYYTAVL GEEEASSISP RENAQEYRHR
SLLEKELLFF AYDIFGIPFV DPDSWTPEEV IPKRLQEKQK SERETAVRIS QEIGNLMKEI
ETLVEEKTKE SLDVSRLTRE GGPLLYEGIN LTMNSKVLNG SQRVVMDGVI SDDECQELQR
LTNAAATSGD GYRGQTSPHT PNEKFYGVTV LKALKLGQEG KVPLQSAHMY YNVTEKVRRV
MESYFRLDTP LYFSYSHLVC RTAIEESQAE RKDSSHPVHV DNCILNAESL VCIKEPPAYT
FRDYSAILYL NGDFDGGNFY FTELDAKTVT AEVQPQCGRA VGFSSGTENP HGVKAVTRGQ
RCAIALWFTL DPRHSERDRV QADDLVKMLF SPEEVDLPQE QPLPDQQGSP KPGEESLSDR
ESQPKDEL
