P3H1_CHICK
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 03-AUG-2022, entry version 122.
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 Ensembl; ENSGALT00000007719; ENSGALP00000007707; ENSGALG00000004833.
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; 660619at2759; -.
DR PhylomeDB; Q6JHU8; -.
DR BRENDA; 1.14.11.7; 1306.
DR PRO; PR:Q6JHU8; -.
DR Proteomes; UP000000539; Chromosome 21.
DR Bgee; ENSGALG00000004833; Expressed in liver and 12 other 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; 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 SUPFAM; SSF48452; SSF48452; 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
