ID A6QLY3_BOVIN Unreviewed; 706 AA.
AC A6QLY3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=procollagen-proline 3-dioxygenase {ECO:0000256|ARBA:ARBA00012262};
DE EC=1.14.11.7 {ECO:0000256|ARBA:ARBA00012262};
GN Name=P3H2 {ECO:0000313|Ensembl:ENSBTAP00000027999.4,
GN ECO:0000313|VGNC:VGNC:32533};
GN Synonyms=LEPREL1 {ECO:0000313|EMBL:AAI48130.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI48130.1};
RN [1] {ECO:0000313|EMBL:AAI48130.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hereford {ECO:0000313|EMBL:AAI48130.1};
RC TISSUE=Fetal lung {ECO:0000313|EMBL:AAI48130.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000027999.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027999.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000027999.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027999.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-3-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:22872, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11678, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; EC=1.14.11.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024148};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the leprecan family.
CC {ECO:0000256|ARBA:ARBA00006487}.
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DR EMBL; BC148129; AAI48130.1; -; mRNA.
DR RefSeq; NP_001093815.1; NM_001100345.2.
DR STRING; 9913.ENSBTAP00000027999; -.
DR PaxDb; 9913-ENSBTAP00000027999; -.
DR Ensembl; ENSBTAT00000027999.5; ENSBTAP00000027999.4; ENSBTAG00000021025.5.
DR GeneID; 511799; -.
DR KEGG; bta:511799; -.
DR CTD; 55214; -.
DR VEuPathDB; HostDB:ENSBTAG00000021025; -.
DR VGNC; VGNC:32533; P3H2.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000159593; -.
DR HOGENOM; CLU_017820_0_0_1; -.
DR OMA; NEDTECR; -.
DR OrthoDB; 5398065at2759; -.
DR TreeFam; TF320837; -.
DR Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000021025; Expressed in spermatocyte and 99 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0032963; P:collagen metabolic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; ISS:UniProtKB.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14049; LEPRECAN 1; 1.
DR PANTHER; PTHR14049:SF1; PROLYL 3-HYDROXYLASE 2; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..706
FT /note="procollagen-proline 3-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014083943"
FT DOMAIN 555..669
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 706 AA; 80834 MW; 0D98C76E2068ACF9 CRC64;
MRERIWAPLP LLLPWLLLPP PLWCGPPDSR HPEREPEPGP LQPFDLLYAS GVAAYYSGDY
ELAVRDLEAA LRSHRRLREI RARCARHCAA RRPLAPPGAG PGAELPFFRA LLERARCYRS
CQSQRLGGPA SRHRASEDVR SDFQRRVPYN YLQRAYIKLN QMEKAVAAAH TFFMANPEHM
EMQQNIENYR TMAGVEDLQL VDREAKPHLE SYSAGVKHYE ADDFELAIKY FEQALREYFN
EDMECRALCE GPQRFEEYEY LGYKAGLYEA IADHYMQVLV CQHECVRELA TRPGRLSPIE
NFLPLHYDYL QFAYYRVGEY IKALECAKAY LLLHPDDEDV LDNVDYYESL LGDSADPASI
EAREDLAMFV KRHKLESELI KSAAEGLGFS YTEPNYWIRY GGRQDENRVP SGVNVEVAEV
HGLSMGKKSL PKIDRDLREG GPLLYENITF VYNSEQLNGT QRVLLDNVLS EEQCRELHSV
ASGIMLVGDG YRGKTSPHTP NEKFEGATVL KALKFGYEGR VPLKSARLFY DISEKARKIV
ESYFMLNSTL YFSYTHMVCR TALSGQQDRR NDLSHPIHAD NCLLDPEANE CWKEPPAYTF
RDYSALLYMN DDFEGGEFIF TEMDAKTVTA SIKPKCGRMI SFSSGGENPH GVKAVTKGQR
CAVALWFTLD PLYRELERIQ ADEVIAILDQ EQQGKHELNI NPKDEL
//
