P4HA1_RAT
ID P4HA1_RAT Reviewed; 534 AA.
AC P54001; Q6AZ74;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
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;
DE Flags: Precursor;
GN Name=P4ha1; Synonyms=P4ha;
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].
RX PubMed=7959029; DOI=10.1016/0378-1119(94)90188-0;
RA Hopkinson I., Smith S.A., Donne A., Gregory H., Franklin T.J., Grant M.E.,
RA Rosamond J.;
RT "The complete cDNA derived sequence of the rat prolyl 4-hydroxylase alpha
RT subunit.";
RL Gene 149:391-392(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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-1 chains and two beta chains
CC (P4HB)(the beta chain is the multi-functional PDI), where P4HB plays
CC the role of a structural subunit; this tetramer catalyzes the formation
CC of 4-hydroxyproline in collagen. {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; X78949; CAA55546.1; -; mRNA.
DR EMBL; BC078703; AAH78703.1; -; mRNA.
DR PIR; S44204; S44204.
DR RefSeq; NP_742059.2; NM_172062.2.
DR RefSeq; XP_006256486.1; XM_006256424.3.
DR AlphaFoldDB; P54001; -.
DR SMR; P54001; -.
DR BioGRID; 249090; 1.
DR IntAct; P54001; 7.
DR STRING; 10116.ENSRNOP00000064405; -.
DR BindingDB; P54001; -.
DR ChEMBL; CHEMBL3301; -.
DR GlyGen; P54001; 2 sites.
DR jPOST; P54001; -.
DR PaxDb; P54001; -.
DR PRIDE; P54001; -.
DR Ensembl; ENSRNOT00000106077; ENSRNOP00000084000; ENSRNOG00000050655.
DR GeneID; 64475; -.
DR KEGG; rno:64475; -.
DR CTD; 5033; -.
DR RGD; 621000; P4ha1.
DR eggNOG; KOG1591; Eukaryota.
DR GeneTree; ENSGT00940000156635; -.
DR HOGENOM; CLU_024155_1_1_1; -.
DR InParanoid; P54001; -.
DR OMA; NLTQYRN; -.
DR OrthoDB; 391515at2759; -.
DR PhylomeDB; P54001; -.
DR BRENDA; 1.14.11.2; 5301.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:P54001; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000050655; Expressed in skeletal muscle tissue and 19 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:0016222; C:procollagen-proline 4-dioxygenase complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO: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; ISS:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; ISO:RGD.
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 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..17
FT /evidence="ECO:0000250"
FT CHAIN 18..534
FT /note="Prolyl 4-hydroxylase subunit alpha-1"
FT /id="PRO_0000022725"
FT REPEAT 205..238
FT /note="TPR"
FT DOMAIN 411..519
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 429
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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 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 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 265..267
FT /note="DQS -> ERA (in Ref. 1; CAA55546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 60898 MW; C44659978281FF30 CRC64;
MIWGVLMMGI LLPQCSAHPG FFTSIGQMTD LIHNEKDLVT SLKDYIKAEE DKLEQIKKWA
EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LILKDMSDGF ISNLTIQRQY
FPNDEDQVGA AKALFRLQDT YNLDTNTISK GNLPGVKHKS FLTAEDCFEL GKVAYTEADY
YHTELWMEQA LMQLEEGEMS TVDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR
ANGNLVYFEY IMSKEKDANK SASGDQSDQK TTPKKKGIAV DYLPERQKYE MLCRGEGIKM
TPRRQKRLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL
SRATVHDPET GKLTTAQYRV SKSAWLSGYE DPVVSRINMR IQDLTGLDVS TAEELQVANY
GVGGQYEPHF DFARKDEPDA FRELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG
TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE
