ID   P3H2_MOUSE              Reviewed;         703 AA.
AC   Q8CG71; Q8C673;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 47.
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   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/6;
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 [LARGE SCALE MRNA] OF 295-703.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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; AJ430350; CAD23038.1; -; mRNA.
DR   EMBL; AK076434; BAC36342.1; -; mRNA.
DR   IPI; IPI00229428; -.
DR   RefSeq; NP_775555.1; -.
DR   UniGene; Mm.326869; -.
DR   Ensembl; ENSMUSG00000038168; Mus musculus.
DR   GeneID; 210530; -.
DR   KEGG; mmu:210530; -.
DR   MGI; MGI:2146663; Leprel1.
DR   HOVERGEN; Q8CG71; -.
DR   OMA; Q8CG71; LECAKAY.
DR   BRENDA; 1.14.11.7; 244.
DR   NextBio; 372972; -.
DR   ArrayExpress; Q8CG71; -.
DR   Bgee; Q8CG71; -.
DR   CleanEx; MM_LEPREL1; -.
DR   GermOnline; ENSMUSG00000038168; Mus musculus.
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_0000240357.
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    544    544       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    497    497       P -> A (in Ref. 2; BAC36342).
SQ   SEQUENCE   703 AA;  80154 MW;  1F42F9B9938573E4 CRC64;
     MRESTWVSLL LLLLLPTPQR GGPQDGRRSP EPEPERGPLQ PFDLLYASGV AAYYSGDYER
     AVRDLEAALS SHRRLRDIRT RCARHCAARR PLAPPGAGPG AELPFFRAVL ERARCSRSCQ
     SQRLGGPASR HRVSEDVRSD FQRRVPYNYL QRAYIKLNQL EKAMEAAHTF FMANPEHMEM
     QQDLEDYKAT ARVEAPLLDR EAKPHLESYN AGVKHYEADD FESAIKYFEQ ALREYFNEDM
     ECRALCEGPQ RFEEYEYLGY KGGLYEAIAD HYMQVLVCQH ECVRELATRP GRLSPIENFL
     PLHYDYLQFA YYRVGEYVKA LECAKAYLMF HPDNEDVLDN VDFYESLLDD STDPASIEAR
     EDLTAFVKRH KLEAELIKLA AEGLGFSYAE PNYWISYGGR QDENRVPSGV NMDGAEVHGL
     SMGKKSPPKI GRDLREGGPL LYENITFVYN SEQLNGTQRV LLDNVLSQEQ CRELHSVANG
     IMLVGDGYRG KTSPHTPNEK FEGATVLKAL KFGYEGRVPL KSARLFYDIS EKARKIVESY
     FMLNSTLYFS YTHMVCRTAL SGQQDRRNDL SHPIHADNCL LDPEANECWK EPPAYTFRDY
     SALLYMNDDF DGGEFIFTEM DAKTVTASIK PKCGRMISFS SGGENPHGVK AVTRGQRCAV
     ALWFTLDPLY RELERIQADE VIAILDQEQR GKHGLNINPK DEL
//