ID   P3H1_CHICK              Reviewed;         725 AA.
AC   Q6JHU8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Prolyl 3-hydroxylase 1 {ECO:0000250|UniProtKB:Q32P28};
DE            EC=1.14.11.7 {ECO:0000269|PubMed:15044469};
DE   AltName: Full=Leucine- and proline-enriched proteoglycan 1 homolog {ECO:0000250|UniProtKB:Q9R1J8};
DE            Short=Leprecan-1 homolog {ECO:0000250|UniProtKB:Q9R1J8};
DE   Flags: Precursor;
GN   Name=P3H1 {ECO:0000250|UniProtKB:Q32P28};
GN   Synonyms=LEPRE1 {ECO:0000250|UniProtKB:Q9R1J8};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, COMPONENT OF A
RP   UNFOLDED COLLAGEN-BINDING COMPLEX INCLUDING P3H1; CYPB AND CRTAP,
RP   CHARACTERIZATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND FUNCTION.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=15044469; DOI=10.1074/jbc.m312807200;
RA   Vranka J.A., Sakai L.Y., Bachinger H.P.;
RT   "Prolyl 3-hydroxylase 1, enzyme characterization and identification of a
RT   novel family of enzymes.";
RL   J. Biol. Chem. 279:23615-23621(2004).
CC   -!- FUNCTION: 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       secretoty pathway of cells. Has growth suppressive activity in
CC       fibroblasts. {ECO:0000269|PubMed:15044469}.
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:0000269|PubMed:15044469};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22873;
CC         Evidence={ECO:0000305|PubMed:15044469};
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   -!- SUBUNIT: Binds unfolded collagen in a complex with CYPB and CRTAP.
CC       {ECO:0000269|PubMed:15044469}.
CC   -!- INTERACTION:
CC       Q6JHU8; Q90830: CRTAP; NbExp=3; IntAct=EBI-1169258, EBI-1169253;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic dermis, tendon, cartilage,
CC       liver and kidney. Expression in the kidney is restricted to the calyx.
CC       In the liver, expression is restricted to the interlobular septum.
CC       {ECO:0000269|PubMed:15044469}.
CC   -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
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DR   EMBL; AY463528; AAS45237.1; -; mRNA.
DR   RefSeq; NP_001001529.1; NM_001001529.1.
DR   AlphaFoldDB; Q6JHU8; -.
DR   IntAct; Q6JHU8; 1.
DR   STRING; 9031.ENSGALP00000007707; -.
DR   GlyCosmos; Q6JHU8; 3 sites, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000007707; -.
DR   Ensembl; ENSGALT00010053151.1; ENSGALP00010032021.1; ENSGALG00010021847.1.
DR   Ensembl; ENSGALT00015060856; ENSGALP00015036977; ENSGALG00015024968.
DR   GeneID; 414142; -.
DR   KEGG; gga:414142; -.
DR   CTD; 64175; -.
DR   VEuPathDB; HostDB:geneid_414142; -.
DR   eggNOG; KOG4459; Eukaryota.
DR   GeneTree; ENSGT00940000158725; -.
DR   HOGENOM; CLU_017820_0_0_1; -.
DR   InParanoid; Q6JHU8; -.
DR   OMA; HTPSEMF; -.
DR   OrthoDB; 5398065at2759; -.
DR   PhylomeDB; Q6JHU8; -.
DR   BRENDA; 1.14.11.7; 1306.
DR   Reactome; R-GGA-1650814; Collagen biosynthesis and modifying enzymes.
DR   PRO; PR:Q6JHU8; -.
DR   Proteomes; UP000000539; Chromosome 21.
DR   Bgee; ENSGALG00000004833; Expressed in liver and 12 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
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:MGI.
DR   GO; GO:0060348; P:bone development; IEA:Ensembl.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR   GO; GO:0032963; P:collagen metabolic process; IDA:MGI.
DR   GO; GO:1904027; P:negative regulation of collagen fibril organization; IDA:UniProtKB.
DR   GO; GO:1901874; P:negative regulation of post-translational protein modification; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0050708; P:regulation of protein secretion; IEA:Ensembl.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR039575; P3H.
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; LEPRECAN 1; 1.
DR   PANTHER; PTHR14049:SF5; PROLYL 3-HYDROXYLASE 1; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Dioxygenase; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Repeat; Signal; TPR repeat; Vitamin C.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..725
FT                   /note="Prolyl 3-hydroxylase 1"
FT                   /id="PRO_0000240355"
FT   REPEAT          36..69
FT                   /note="TPR 1"
FT   REPEAT          136..169
FT                   /note="TPR 2"
FT   REPEAT          198..231
FT                   /note="TPR 3"
FT   REPEAT          294..327
FT                   /note="TPR 4"
FT   DOMAIN          557..671
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          701..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          394..441
FT                   /evidence="ECO:0000255"
FT   MOTIF           722..725
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        662
FT                   /evidence="ECO:0000250"
FT   BINDING         580
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         582
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         652
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   725 AA;  81676 MW;  2D227635DA36B605 CRC64;
     MALLLPLLPL LVWAAGPPGP LGPPEHSEPP LPAEPPDALF AAGAEAYARG DWPAVVLQME
     RALRARAAIR ARSVRCRLRC ANATAVVPTD GLEPTLHDLL FFRGLLRRAA CLRGCGPTQP
     SRYRLGEELE REFRKRSPYN YLQVAYFKIN KVAKAVAAAH TFFVANPEHV EMKQNLEYYQ
     MMAGVRESDF ADLEARPHMT EFRLGVRFYS EEQPAAAVLH LEKALQEYFV ADTECRALCE
     GPYDYEGYNY LEYNADLFQA MTDHYMQVLS CKQGCVTELA SQPGREKPLE DFLPSHFNYL
     QFAYYNNGNY EKAIECAKTY LLFFPNDEVM NQNLAYYTAV LGEDLARPIE PRKEIQAYRQ
     RSLMEKELLF FSYDVFGIPF VDPDTWTPEE VIPKRLREKQ KVERETAARI SEEIGNLMKE
     IETLVEEKAK ESAEMSKFIR EGGPLVYEGA SVTMNSKSLN GSQRVVVDGV LSAEECRELQ
     RLTNAAASAG DGYRGKTSPH TPSETFYGVT VLKALKLGQE GKVPLQSAHL YYNVTEKVRH
     MMESYFRLEV PLHFSYSHLV CRTAIDEKQE GRSDNSHEVH VDNCILNAEA LVCVKEPPAY
     TFRDYSAILY LNGDFEGGAF YFTELDAKTQ TAEVQPQCGR AVGFSSGSEN PHGVKAVTKG
     QRCAIALWFT LDPRHSERER VQADDLVKML FRTEEVDLLQ ETSAEQEPTA ATSTAGLHAA
     GKDEL
//