P3H2_CHICK
ID P3H2_CHICK Reviewed; 694 AA.
AC Q6JHU7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Prolyl 3-hydroxylase 2 {ECO:0000250|UniProtKB:Q8IVL5};
DE EC=1.14.11.7 {ECO:0000250|UniProtKB:Q8IVL5};
DE AltName: Full=Leprecan-like protein 1 {ECO:0000250|UniProtKB:Q8IVL5};
DE Flags: Precursor;
GN Name=P3H2 {ECO:0000250|UniProtKB:Q8IVL5};
GN Synonyms=LEPREL1 {ECO:0000250|UniProtKB:Q8IVL5};
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].
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: Prolyl 3-hydroxylase that catalyzes the post-translational
CC formation of 3-hydroxyproline on collagens (By similarity). Contributes
CC to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons,
CC the eye sclera and in the eye lens capsule (By similarity). Has high
CC activity with the type IV collagen COL4A1, and lower activity with
CC 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 -!- 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:0000250|UniProtKB:Q8IVL5};
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 -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
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DR EMBL; AY463529; AAS45238.1; -; mRNA.
DR RefSeq; NP_001001530.1; NM_001001530.1.
DR AlphaFoldDB; Q6JHU7; -.
DR STRING; 9031.ENSGALP00000011808; -.
DR PaxDb; Q6JHU7; -.
DR Ensembl; ENSGALT00000046911; ENSGALP00000046986; ENSGALG00000040866.
DR GeneID; 414143; -.
DR KEGG; gga:414143; -.
DR CTD; 55214; -.
DR VEuPathDB; HostDB:geneid_414143; -.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000159593; -.
DR InParanoid; Q6JHU7; -.
DR OMA; AKPHMED; -.
DR OrthoDB; 660619at2759; -.
DR PhylomeDB; Q6JHU7; -.
DR PRO; PR:Q6JHU7; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000040866; Expressed in spleen and 7 other tissues.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0032963; P:collagen metabolic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; ISS: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 2: Evidence at transcript level;
KW Coiled coil; Dioxygenase; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Sarcoplasmic reticulum; Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..694
FT /note="Prolyl 3-hydroxylase 2"
FT /id="PRO_0000240359"
FT REPEAT 35..68
FT /note="TPR 1"
FT REPEAT 136..169
FT /note="TPR 2"
FT REPEAT 196..229
FT /note="TPR 3"
FT REPEAT 292..325
FT /note="TPR 4"
FT DOMAIN 543..657
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 395..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 386..418
FT /evidence="ECO:0000255"
FT MOTIF 691..694
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 409..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 648
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 568
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 638
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 694 AA; 78430 MW; 6263153C4577AFBD CRC64;
MAPGSRSWGA VLLLAAMLPA ACGSCGADGG PLEPFDALYA SGVEAYYGGD FAGAARCLEQ
ALRSRRELRA ERLRCRRRCR GQVRLAALGA GPAGELPFFG ALLRRAGCLR SCEEPRLGAA
SRHRAAEEVR SDFQRRVPYS YLQRAYIQLN KLEEAANAAH TFFMANPEHM EIQQDIENYK
TTAGKVSLID LEAKPHMEDY SAGVRHYDKE EYGLAITFLE RALEGYYAED EDCQIMCEGP
QRFEEHEYLE YKAGLYEAIA DHYMQVLACK HDCIRELATR SGRISPIENF LPLHYDYLQF
AYYRVGDYVK ALECARSYLL FHPDDEDVLE NAAYYEGLLE GTVDPATIKP RKEAKALLRR
HKLESHLLRV AAVGLGFTYT EPNYWKRYGA RQDEHSVPSS ISSEPEDGPR LSLTKKPTPK
PDRELKEGGP LLYSDVKFVY NSQQLNGTQR VLLDNVISEE QCRELHRVAS GIMLAGDGYR
GKTSPHTPNE RFEGATVLKA LKYGYEGRVP LKSARLFYDI SEKARRIVES YFMLNSTLYF
SYTHLVCRTA LSGQQERRND LSHPIHADNC LLDPEANECW KEPPAYTFRD YSALLYMNAD
FEGGEFIFTE MDAKTVTASI KPKCGRMVSF SSGGENPHGV KAVTKGQRCA VALWFTLDPL
YRELERIQAD EVIAMLDQEH VGRSEMNINP KDEL
