ID   P3H2_RAT                Reviewed;         703 AA.
AC   Q4KLM6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=Prolyl 3-hydroxylase 2;
DE            EC=1.14.11.7;
DE   AltName: Full=Leprecan-like protein 1;
DE   Flags: Precursor;
GN   Name=Leprel1; Synonyms=P3h2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Has prolyl 3-hydroxylase activity catalyzing the post-
CC       translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-
CC       sequences in collagens, especially types IV and V (By similarity).
CC   -!- CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O(2)
CC       = procollagen trans-3-hydroxy-L-proline + succinate + CO(2).
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- COFACTOR: Ascorbate (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the leprecan family.
CC   -!- SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
CC   -!- SIMILARITY: Contains 4 TPR repeats.
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DR   EMBL; BC099107; AAH99107.1; -; mRNA.
DR   IPI; IPI00561579; -.
DR   RefSeq; NP_001020798.1; -.
DR   UniGene; Rn.213595; -.
DR   Ensembl; ENSRNOG00000001925; Rattus norvegicus.
DR   GeneID; 288016; -.
DR   KEGG; rno:288016; -.
DR   RGD; 1304568; Leprel1.
DR   HOVERGEN; Q4KLM6; -.
DR   BRENDA; 1.14.11.7; 248.
DR   NextBio; 627416; -.
DR   ArrayExpress; Q4KLM6; -.
DR   GermOnline; ENSRNOG00000001925; Rattus norvegicus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000886; ER_targeting_sequence.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Iron; Metal-binding; Oxidoreductase; Repeat; Signal; TPR repeat;
KW   Vitamin C.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    703       Prolyl 3-hydroxylase 2.
FT                                /FTId=PRO_0000240358.
FT   REPEAT       42     75       TPR 1.
FT   REPEAT      144    177       TPR 2.
FT   REPEAT      205    238       TPR 3.
FT   REPEAT      301    334       TPR 4.
FT   DOMAIN      457    665       PKHD.
FT   MOTIF       700    703       Prevents secretion from ER (Potential).
FT   ACT_SITE    657    657       By similarity.
FT   METAL       575    575       Iron.
FT   METAL       577    577       Iron.
FT   METAL       647    647       Iron.
FT   CARBOHYD    444    444       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    455    455       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    544    544       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   703 AA;  79833 MW;  EFE57CEF5F209B63 CRC64;
     MRESTWVSLL LLLLLPAPQR GGPQDGRGSP EPEPERGPLQ PFDLLYASGV AAYYSGDYEG
     AVRDLEAALR SHRRLRDIRT RCARHCAARR PLAPPGAGPG AELPFFRAVL ERARCSRSCQ
     SQRLGGPASR HRVSEDVRSD FQRRVPYNYL QRAYIKLNQL DKAMEAAHTF FMANPEHMEM
     QQNIEDYKAT ARVEAPLVDR EAKPHLESYN AGVKHYEADD FEAAIKYFEQ ALREYFNEDM
     VCRALCEGPQ RFEEYEYLGS KGSLYEAIAD HYMQVLVCQH ECVRELATRP GRLSPIENFL
     PLHYDYLQFA YYRVGEYVKA LECAKAYLMF HPDDQDVLDN VDFYESLLDD STDPASIEAR
     EDLTAFVKRH KLEAELIKSA AEGLGFSYSE PNYWISYGGR QDENRVPSGV NMDGAEVHGL
     SMGKKSPPKI GRDLREGGPL LYENITFVYN SEQLNGTQRV LLDNVLSEEQ CRELHSVASG
     IMLVGDGYRG KTSPHTPNEK FEGATVLKAL KFGYEGRVPL KSARLFYDIS EKARKIVESY
     FMLNSTLYFS YTHMVCRTAL SGQQDRRNDL SHPIHADNCL LDPEANECWK EPPAYTFRDY
     SALLYMNDDF EGGEFIFTEM DAKTVTASIK PKCGRMISFS SGGENPHGVK AVTRGQRCAV
     ALWFTLDPLY RELERIQADE VIAILDQEQH GKHGLNINPK DEL
//