ID   P3H3_MOUSE              Reviewed;         732 AA.
AC   Q8CG70; O88836;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Prolyl 3-hydroxylase 3;
DE            EC=1.14.11.7;
DE   AltName: Full=Leprecan-like protein 2;
DE   AltName: Full=Protein B;
DE   Flags: Precursor;
GN   Name=Leprel2; Synonyms=P3h3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=15063763; DOI=10.1016/j.bbrc.2004.03.060;
RA   Jaernum S., Kjellman C., Darabi A., Nilsson I., Edvardsen K.,
RA   Aaman P.;
RT   "LEPREL1, a novel ER and Golgi resident member of the Leprecan
RT   family.";
RL   Biochem. Biophys. Res. Commun. 317:342-351(2004).
RN   [2]
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
RT   a novel family of enzymes.";
RL   J. Biol. Chem. 279:23615-23621(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 139-732.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 165-732.
RX   MEDLINE=98112780; PubMed=9445485;
RA   Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
RA   Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
RA   Gibbs R.A.;
RT   "Comparative sequence analysis of a gene-rich cluster at human
RT   chromosome 12p13 and its syntenic region in mouse chromosome 6.";
RL   Genome Res. 8:29-40(1998).
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 (By 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; AJ441086; CAD29580.1; -; mRNA.
DR   EMBL; AY463530; AAS45239.1; -; mRNA.
DR   EMBL; BC003726; AAH03726.1; -; mRNA.
DR   EMBL; BC016431; AAH16431.1; -; mRNA.
DR   EMBL; AC002397; AAC36012.1; -; Genomic_DNA.
DR   IPI; IPI00407527; -.
DR   RefSeq; NP_038562.2; -.
DR   UniGene; Mm.35708; -.
DR   Ensembl; ENSMUSG00000023191; Mus musculus.
DR   GeneID; 14789; -.
DR   KEGG; mmu:14789; -.
DR   MGI; MGI:1315208; Leprel2.
DR   HOVERGEN; Q8CG70; -.
DR   OMA; Q8CG70; KPLTYWK.
DR   BRENDA; 1.14.11.7; 244.
DR   NextBio; 286923; -.
DR   ArrayExpress; Q8CG70; -.
DR   Bgee; Q8CG70; -.
DR   CleanEx; MM_LEPREL2; -.
DR   GermOnline; ENSMUSG00000023191; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; 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; IPR006620; Pro_4_hyd_alph.
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   Coiled coil; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron;
KW   Metal-binding; Oxidoreductase; Repeat; Signal; TPR repeat; Vitamin C.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    732       Prolyl 3-hydroxylase 3.
FT                                /FTId=PRO_0000240361.
FT   REPEAT       39     72       TPR 1.
FT   REPEAT      152    185       TPR 2.
FT   REPEAT      214    247       TPR 3.
FT   REPEAT      312    345       TPR 4.
FT   DOMAIN      460    670       PKHD.
FT   COILED      674    703       Potential.
FT   MOTIF       729    732       Prevents secretion from ER (Potential).
FT   COMPBIAS     14     39       Pro-rich.
FT   COMPBIAS    689    697       Poly-Glu.
FT   ACT_SITE    662    662       By similarity.
FT   METAL       580    580       Iron.
FT   METAL       582    582       Iron.
FT   METAL       652    652       Iron.
FT   CARBOHYD    327    327       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    458    458       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   732 AA;  81701 MW;  BD54733B60F1687A CRC64;
     MLRLLRLLLL LLLPPPGSPE PPEPPGLAQL SPGSPPQAPD LLYADGLRAY SAGAWAPAVA
     LLREALRSRA ALGRARQECG ASCAAEPGAA LPSQLLGAPH PVSGPGVWEP LLLRATLRRA
     ECLTQCAVRR LGPGGAARLR VGSALRDAFR RREPYNYLQR AYYQLKKLDL AASAAHTFFV
     ANPTHLQMRE DMAKYRRMSA IRPQSFRDLV TPLYWAAYDT GLELLEQREA ALALPQLEEA
     LQGSLAHMES CRAACEGPEE HQGAEEEGEG SQGGLYEAIA GHWIRVLQCR QHCVADTATR
     PGRSFPVQDF LLSQLRRLHE AYAQVGNMSQ AMENVLSVLL FYPEDEAAKK ALNQYQTQLG
     EPRPDLGPRE DIQRFILRSL GEKRQLYYAM EHLGTSFKDP DSWTPEALIP KALRERLRED
     QEKKPWDHQP PQQKPLAHWK DALLMEGVTL TQDAQQLNGS ERAVLDGLLT SAECGVLLQL
     AKDAAQAGAR SGYRGRRSPH SPHERFEGLT VLKAAQLARA GTVGRPGAKL LLEVSERVRT
     LTQAYFSPER PLHLSFTHLV CRSAIEGEQE QRMDLSHPVH ADNCVLDPDT GECWREPPAY
     TYRDYSGLLY LNDDFKGGDL FFTQPNALTV TAQVRPRCGR LVAFSSGGEN PHGVWAVTRG
     RRCALALWHT WAPEHSEQEW TEAKELLQEE EEEEEEEDIL SRDPSPEPPS HKLQRVQEKA
     GKPRRVRVRE EL
//