ID   P4HA3_BOVIN             Reviewed;         544 AA.
AC   Q75UG4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 39.
DE   RecName: Full=Prolyl 4-hydroxylase subunit alpha-3;
DE            EC=1.14.11.2;
DE   AltName: Full=4-PH alpha-3;
DE   AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3;
DE   Flags: Precursor;
GN   Name=P4HA3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adipose tissue;
RA   Tahara K., Aso H., Yamasaki T., Takano S.;
RT   "Cloning and expression of collagen prolyl 4-hydroxylase during bovine
RT   adipogenesis.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC       hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC       proteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: Procollagen L-proline + 2-oxoglutarate + O(2)
CC       = procollagen trans-4-hydroxy-L-proline + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- COFACTOR: Ascorbate (By similarity).
CC   -!- SUBUNIT: Heterotetramer of two alpha-3 chains and two beta chains
CC       (the beta chain is the multi-functional PDI) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC   -!- PTM: N-glycosylation plays no role in the catalytic activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the P4HA family.
CC   -!- SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
CC   -!- SIMILARITY: Contains 1 TPR repeat.
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DR   EMBL; AB126035; BAD18888.1; -; mRNA.
DR   RefSeq; NP_001001598.1; -.
DR   UniGene; Bt.88095; -.
DR   Ensembl; ENSBTAG00000006579; Bos taurus.
DR   GeneID; 414348; -.
DR   KEGG; bta:414348; -.
DR   HOVERGEN; Q75UG4; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
DR   InterPro; IPR005123; 2OG-FeII_Oase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR013547; Pro_4_hyd_alph_N.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF08336; P4Ha_N; 1.
DR   SMART; SM00702; P4Hc; 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; Signal; TPR repeat; Vitamin C.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    544       Prolyl 4-hydroxylase subunit alpha-3.
FT                                /FTId=PRO_0000317765.
FT   REPEAT      227    260       TPR.
FT   DOMAIN      422    529       PKHD.
FT   COILED      107    131       Potential.
FT   METAL       440    440       Iron (By similarity).
FT   METAL       442    442       Iron (By similarity).
FT   METAL       510    510       Iron (By similarity).
FT   BINDING     520    520       2-oxoglutarate (Potential).
FT   CARBOHYD    248    248       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    482    482       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   544 AA;  61023 MW;  D996D34D44A6F230 CRC64;
     MGPAARLAAL LAVLAFRAGD PAEVAARGDT FSALTSVARA LAPERRLLGL LRRYLRGEEA
     RLRDLTRFYH KVLSLHEDSA TPVSNPLLAF TLIKRLQSDW KNVVHSLEAS ENIRALKDGY
     ERVEQDLPAF EDLEGAARAL MRLQDVYMLN VKGLARGVFQ RVTGSAVTDL YSPRRLFSLT
     GDDCFQVGKV AYDMGDYYHA IPWLEEAVSL FRGSYGEWKT EDEASLEDAL DHLAFAYFQA
     GNVLCALNLS REFLLYSPDN KRVARNVLKY EKLLAESPNQ AVAETVMQRP NVPHLQTRDT
     YEGLCQTLGS QPTHYRIPSL YCSYETSSSP YLLLQPVRKE VIHLEPYVVL YHDFVSDAEA
     QTIRGLAEPW LQRSVVASGE KQLPVEYRIS KSAWLKDTVD PVLVTLDHRI AALTGLDVQP
     PYAEYLQVVN YGIGGHYEPH FDHATSPSSP LYRMNSGNRV ATFMIYLSSV EAGGATAFIY
     GNFSVPVVKN AALFWWNLHR SGEGDGDTLH AACPVLVGDK WVANKWIHEY GQEFRRPCSS
     RPED
//