ID   P4HA1_BOVIN             Reviewed;         534 AA.
AC   Q1RMU3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Prolyl 4-hydroxylase subunit alpha-1;
DE            EC=1.14.11.2;
DE   AltName: Full=4-PH alpha-1;
DE   AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1;
DE   Flags: Precursor;
GN   Name=P4HA1;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) 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-1 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   -!- 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; BC114708; AAI14709.1; -; mRNA.
DR   IPI; IPI00700678; -.
DR   RefSeq; NP_001069238.1; -.
DR   UniGene; Bt.41027; -.
DR   SMR; Q1RMU3; 161-254.
DR   GeneID; 518288; -.
DR   KEGG; bta:518288; -.
DR   HOVERGEN; Q1RMU3; -.
DR   BRENDA; 1.14.11.2; 251.
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: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:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR013547; Pro_4_hyd_alph_N.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR013026; TPR_region.
DR   InterPro; IPR019734; TPR_repeat.
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; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding;
KW   Oxidoreductase; Signal; TPR repeat; Vitamin C.
FT   SIGNAL        1     17       By similarity.
FT   CHAIN        18    534       Prolyl 4-hydroxylase subunit alpha-1.
FT                                /FTId=PRO_0000288111.
FT   REPEAT      205    238       TPR.
FT   DOMAIN      335    518       PKHD.
FT   METAL       429    429       Iron (By similarity).
FT   METAL       431    431       Iron (By similarity).
FT   METAL       500    500       Iron (By similarity).
FT   BINDING     510    510       2-oxoglutarate (Potential).
FT   CARBOHYD    113    113       N-linked (GlcNAc...).
FT   CARBOHYD    259    259       N-linked (GlcNAc...).
SQ   SEQUENCE   534 AA;  61010 MW;  D6AF8ECEA1447C62 CRC64;
     MIWYILVVGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE DKLEQIKKWA
     EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LVLKDMSDGF ISNLTIQRQY
     FPNDEDQVGA AKALLRLQDT YNLDTDTISK GDLPGVKHKS FLTVEDCFEL GKVAYTEADY
     YHTELWMEQA LRQLDEGEVS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR
     ANGNLKYFEY IMAKEKDANK SSSDDQSDQK TTLKKKGAAV DYLPERQKYE MLCRGEGIKM
     TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE VVKDLAKPRL
     RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR IQDLTGLDVS TAEELQVANY
     GVGGQYEPHF DFARKDEPDA FKELGTGNRI ATWLFYMSDV LAGGATVFPE VGASVWPKKG
     TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE
//