P4HA3_BOVIN
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 03-AUG-2022, entry version 113.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-3;
DE Short=4-PH alpha-3;
DE EC=1.14.11.2 {ECO:0000250|UniProtKB:Q7Z4N8};
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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. {ECO:0000250|UniProtKB:Q7Z4N8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18946;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q7Z4N8};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4N8};
CC -!- SUBUNIT: Heterotetramer of two alpha-3 chains and two beta chains (the
CC beta chain is the multi-functional PDI).
CC {ECO:0000250|UniProtKB:Q7Z4N8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- PTM: N-glycosylation plays no role in the catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; AB126035; BAD18888.1; -; mRNA.
DR RefSeq; NP_001001598.1; NM_001001598.2.
DR AlphaFoldDB; Q75UG4; -.
DR SMR; Q75UG4; -.
DR STRING; 9913.ENSBTAP00000008644; -.
DR PaxDb; Q75UG4; -.
DR PRIDE; Q75UG4; -.
DR Ensembl; ENSBTAT00000008644; ENSBTAP00000008644; ENSBTAG00000006579.
DR GeneID; 414348; -.
DR KEGG; bta:414348; -.
DR CTD; 283208; -.
DR VEuPathDB; HostDB:ENSBTAG00000006579; -.
DR VGNC; VGNC:32537; P4HA3.
DR eggNOG; KOG1591; Eukaryota.
DR GeneTree; ENSGT00940000158967; -.
DR HOGENOM; CLU_024155_1_0_1; -.
DR InParanoid; Q75UG4; -.
DR OMA; EFAEPWL; -.
DR OrthoDB; 1438683at2759; -.
DR TreeFam; TF313393; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000006579; Expressed in pigment epithelium of eye and 98 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0004656; F:procollagen-proline 4-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR013547; Pro_4_hyd_alph_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10869; PTHR10869; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08336; P4Ha_N; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal; TPR repeat;
KW Vitamin C.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..544
FT /note="Prolyl 4-hydroxylase subunit alpha-3"
FT /id="PRO_0000317765"
FT REPEAT 227..260
FT /note="TPR"
FT DOMAIN 422..529
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT COILED 107..131
FT /evidence="ECO:0000255"
FT BINDING 440
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 442
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 510
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 520
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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
