P4HA2_CHICK
ID P4HA2_CHICK Reviewed; 534 AA.
AC Q5ZLK5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-2;
DE Short=4-PH alpha-2;
DE EC=1.14.11.2 {ECO:0000269|PubMed:9211872};
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2;
DE Flags: Precursor;
GN Name=P4HA2; ORFNames=RCJMB04_5l17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9211872; DOI=10.1074/jbc.272.28.17342;
RA Annunen P., Helaakoski T., Myllyharju J., Veijola J., Pihlajaniemi T.,
RA Kivirikko K.I.;
RT "Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II)
RT and characterization of the type II enzyme tetramer. The alpha(I) and
RT alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer.";
RL J. Biol. Chem. 272:17342-17348(1997).
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC proteins. {ECO:0000269|PubMed:9211872}.
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:0000269|PubMed:9211872};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:O15460};
CC -!- SUBUNIT: Heterotetramer of two alpha-2 chains and two beta chains (the
CC beta chain is the multi-functional PDI).
CC {ECO:0000250|UniProtKB:O15460}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; AJ719729; CAG31388.1; -; mRNA.
DR RefSeq; NP_001006155.1; NM_001006155.1.
DR AlphaFoldDB; Q5ZLK5; -.
DR SMR; Q5ZLK5; -.
DR STRING; 9031.ENSGALP00000010783; -.
DR PaxDb; Q5ZLK5; -.
DR GeneID; 416326; -.
DR KEGG; gga:416326; -.
DR CTD; 8974; -.
DR VEuPathDB; HostDB:geneid_416326; -.
DR eggNOG; KOG1591; Eukaryota.
DR InParanoid; Q5ZLK5; -.
DR OrthoDB; 391515at2759; -.
DR SABIO-RK; Q5ZLK5; -.
DR PRO; PR:Q5ZLK5; -.
DR Proteomes; UP000000539; 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: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 1: Evidence at protein level;
KW Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal; TPR repeat; Vitamin C.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..534
FT /note="Prolyl 4-hydroxylase subunit alpha-2"
FT /id="PRO_0000041836"
FT REPEAT 207..240
FT /note="TPR"
FT DOMAIN 413..519
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 431
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 433
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 500
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 510
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 534 AA; 61435 MW; F3176919EBDEEBB1 CRC64;
MKPWLCLVFF TSAFLIWHAE AEFFTSIGQM TDLIYAEKDL VQSLKEYIRA EETKLSQIKS
WAEKMDVLTS KSTSDPEGYL AHPVNAYKLV KRLNTDWLEL ENLVLQDTTN GFITNLTIQR
QFFPTEEDET GAAKALMRLQ DTYKLDPETL SRGNLPGTKY RSSLTVSDCF GMGKTAYNDG
DYYHTVLWME QALKQHDEGE DTTVSKVEIL DYLSYAVFQF GDLHRAMELT RRLISLDSTH
ERAGSNLRYF EKLLEKEREK PSNKTVATTE PVVQSGAYER PLDYLPERDI YEALCRGEGV
KMTPRRQKRL FCRYHDGNRN PHLLIAPFKE EDEWDSPHIV RYYDVMSDEE IEKIKQLAKP
KLARATVRDP KTGVLTVASY RVSKSSWLEE DDDPVVAKVN QRMQQITGLT VKTAELLQVA
NYGMGGQYEP HFDFSRRPFD STLKSEGNRL ATFLNYMSDV EAGGATVFPD FGAAIWPKKG
TAVFWYNLFR SGEGDYRTRH AACPVLVGCK WVSNKWFHER GNEFLRPCGR TEVD
