ID   Q66J10_XENLA            Unreviewed;       533 AA.
AC   Q66J10;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN   Name=p4ha2.L {ECO:0000313|RefSeq:NP_001087703.1,
GN   ECO:0000313|Xenbase:XB-GENE-957623};
GN   Synonyms=MGC83530 {ECO:0000313|EMBL:AAH81114.1}, p4ha2
GN   {ECO:0000313|RefSeq:NP_001087703.1,
GN   ECO:0000313|Xenbase:XB-GENE-957623};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH81114.1};
RN   [1] {ECO:0000313|RefSeq:NP_001087703.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH81114.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocytes {ECO:0000313|EMBL:AAH81114.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001087703.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC       hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC       proteins. {ECO:0000256|ARBA:ARBA00002035}.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the P4HA family.
CC       {ECO:0000256|ARBA:ARBA00006511}.
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DR   EMBL; BC081114; AAH81114.1; -; mRNA.
DR   RefSeq; NP_001087703.1; NM_001094234.1.
DR   DNASU; 447527; -.
DR   GeneID; 447527; -.
DR   KEGG; xla:447527; -.
DR   AGR; Xenbase:XB-GENE-957623; -.
DR   CTD; 447527; -.
DR   Xenbase; XB-GENE-957623; p4ha2.L.
DR   OrthoDB; 2899308at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 447527; Expressed in zone of skin and 19 other cell types or tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 6.10.140.1460; -; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   InterPro; IPR013547; Pro_4_hyd_alph_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10869:SF240; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF08336; P4Ha_N; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001087703.1}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..533
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001087703.1"
FT                   /id="PRO_5033206947"
FT   DOMAIN          412..518
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   533 AA;  61337 MW;  1CE86219156D64D9 CRC64;
     MEPNAISIIL VSLCCIWQVQ AEVFTSTGQM TDLIYRERDL VQSLKEYIQK EEERLSKIKR
     WVSQVDELTS RSTADPEGYL GHPVNAYKLV KRFNTDWTSL ENLVLQDSTK GFIANLTFQR
     EYFPTEEDEK GAAKALMRLQ DTYRLDPDII AKGKLPGTNY ISSLSAVDTF GMGKIAYHDG
     DYYHTVLWMQ QALKQLDEGE EAKISKVDVL DYLSYTVFQL GDVPRAVELT KRLLVLDANH
     ERAGSNLKYF EKMQERQKGE LKQNETIETE TRQPGVYNRP LDYLPERDVY EALCRGEGVK
     MNPRRQKRLF CRYHDGNRNP RLILGPIKME DEWDSPRIVR YLDVLSDEEI EKIKELAKPR
     LARATVRDPK TGVLTVANYR VSKSAWLEEY DDPVIGRVNS RMQAITGLTK DTAELLQVAN
     YGMGGQYEPH FDFSRRPFDS NLKTEGNRLA TYLNYMSDVE AGGATVFPDF GAAIWPRKGT
     AVFWYNLFRS GEGDYRTRHA ACPVLVGSKW VSNKWFHERG QEFLRPCGLT EVD
//