P4HA1_CHICK
ID P4HA1_CHICK Reviewed; 516 AA.
AC P16924;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1;
DE Short=4-PH alpha-1;
DE EC=1.14.11.2 {ECO:0000250|UniProtKB:P13674};
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1;
GN Name=P4HA1; Synonyms=P4HA;
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 [MRNA] OF 28-516, AND PROTEIN SEQUENCE OF 1-42.
RX PubMed=2552442; DOI=10.1073/pnas.86.19.7382;
RA Bassuk J.A., Kao W.W.-Y., Herzer P., Kedersha N., Seyer J., Demartino J.A.,
RA Daugherty B.L., Mark G.E. III, Berg R.A.;
RT "Prolyl 4-hydroxylase: molecular cloning and the primary structure of the
RT alpha subunit from chicken embryo.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7382-7386(1989).
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:P13674}.
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:P13674};
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:P13674};
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains (the
CC beta chain is the multi-functional PDI).
CC {ECO:0000250|UniProtKB:P13674}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; M26217; AAA49002.1; -; mRNA.
DR PIR; A33832; DACHA.
DR AlphaFoldDB; P16924; -.
DR SMR; P16924; -.
DR STRING; 9031.ENSGALP00000006885; -.
DR BindingDB; P16924; -.
DR PaxDb; P16924; -.
DR VEuPathDB; HostDB:geneid_423704; -.
DR eggNOG; KOG1591; Eukaryota.
DR InParanoid; P16924; -.
DR PhylomeDB; P16924; -.
DR SABIO-RK; P16924; -.
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; ISS:UniProtKB.
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 InterPro; IPR019734; TPR_repeat.
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.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW TPR repeat; Vitamin C.
FT CHAIN 1..516
FT /note="Prolyl 4-hydroxylase subunit alpha-1"
FT /id="PRO_0000206659"
FT REPEAT 189..222
FT /note="TPR"
FT DOMAIN 393..501
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 411
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 413
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 482
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 492
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 59440 MW; 49EB14163CDE347B CRC64;
HTDFFTSIGH MTDLINTEKD LVISKLKDYI KAEESKLEQI KKWAEKLDKL TDTATKDPEG
FLGHPANAFK LMKRLNTEWG ELESLVLKDM SDGFISNMTI QRQFFPNDED QTGARKALLR
LQDTYNLDTD TLSRGNLPGV KHKSFLTAED CFELGKIRYT EADYYHTELW MEQALKQLDE
GEVSSADKVY ILDYLSYAVY QQGDLSKAMM LTKRLLELDP EHQRANGNMK YFEYIMAKEK
EANKSSTDAE DQTDKETEVK KKDYLPERRK YEMLCRGEGL KMTPRRQKRL FCRYYDGNRN
PRYILGPVKQ EDEWDKPRIV RFLDIISDEE IETVKELAKP RLSRATVHDP ETGKLTTAHY
RVSKSAWLSG YESPVVSRIN TRIQDLTGLD VSTAEELQVA NYGVGGQYEP HFDFGRKDEP
DAFKELGTGN RIATWLFYMS DVSAGGATVF PEVGASVWPK KGTAVFWYNL FPSGEGDYST
RHAACPVLVG NKWVSNKWLH ERGQEFRRPC TLSELE
