P4HA3_RAT
ID P4HA3_RAT Reviewed; 544 AA.
AC Q6W3E9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=14500733; DOI=10.1074/jbc.m306806200;
RA Kukkola L., Hieta R., Kivirikko K.I., Myllyharju J.;
RT "Identification and characterization of a third human, rat, and mouse
RT collagen prolyl 4-hydroxylase isoenzyme.";
RL J. Biol. Chem. 278:47685-47693(2003).
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; AY313450; AAQ87605.1; -; mRNA.
DR RefSeq; NP_942070.1; NM_198775.1.
DR AlphaFoldDB; Q6W3E9; -.
DR SMR; Q6W3E9; -.
DR IntAct; Q6W3E9; 1.
DR STRING; 10116.ENSRNOP00000049901; -.
DR GlyGen; Q6W3E9; 2 sites.
DR PaxDb; Q6W3E9; -.
DR GeneID; 361612; -.
DR KEGG; rno:361612; -.
DR UCSC; RGD:735150; rat.
DR CTD; 283208; -.
DR RGD; 735150; P4ha3.
DR eggNOG; KOG1591; Eukaryota.
DR InParanoid; Q6W3E9; -.
DR OrthoDB; 1438683at2759; -.
DR PhylomeDB; Q6W3E9; -.
DR BRENDA; 1.14.11.2; 5301.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:Q6W3E9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; TAS:RGD.
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; IMP:RGD.
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 Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..544
FT /note="Prolyl 4-hydroxylase subunit alpha-3"
FT /id="PRO_0000317768"
FT REPEAT 227..260
FT /note="TPR"
FT DOMAIN 422..529
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
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 242
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; 61165 MW; 9D972AD28EC35C05 CRC64;
MGPGARLAAL LVLLKLGVGD PAAAAGREDT FSALTSVARA LAPERRLLGT LRRYLRGEEA
RLRDLTRFYD KVLSLHEDLK IPVVNPLLVF TLIKRLPSDW RNVVHSLEAT ENIRAPKDGY
EKVEQDLPAF EDLEGAARAL MRLQDAYMLN VKGLAQGVFQ RVTGSSITDL YSPRQLFSLT
ADDCFQVGKV AYDTGDYYHA IPWLEEAVSL FRRSYGEWKT EDEASLEDAL DYLAFACYQV
GNVSCALSLS REFLVYSPDN KRMARNVLKY ERLLAENGHL MAAETAIQRP NVPHLQTRDT
YEGLCQTLGS QPTHYQIPSL YCSYETNSSP YLLLQPARKE VIHLRPLVAL YHDFVSDEEA
QKIRELAEPW LQRSVVASGE KQLQVEYRIS KSAWLKDTVD PVLVTLDRRI AALTGLDIQP
PYAEYLQVVN YGIGGHYEPH FDHATSPSSP LYKMKSGNRA ATLMIYLSSV EAGGATAFIY
GNFSVPVVKN AALFWWNLHR SGEGDDDTLH AGCPVLVGDK WVANKWIHEY GQEFRRPCDT
NPED
