P4H1_ARATH
ID P4H1_ARATH Reviewed; 283 AA.
AC Q9ZW86;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Prolyl 4-hydroxylase 1 {ECO:0000305};
DE Short=AtP4H-1 {ECO:0000303|PubMed:11976332};
DE Short=AtP4H1 {ECO:0000303|Ref.6};
DE EC=1.14.11.2 {ECO:0000269|PubMed:11976332};
GN Name=P4H1 {ECO:0000303|Ref.6}; OrderedLocusNames=At2g43080; ORFNames=MFL8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-180; ASP-182; HIS-260; LYS-270; SER-272 AND ARG-278.
RX PubMed=11976332; DOI=10.1074/jbc.m201865200;
RA Hieta R., Myllyharju J.;
RT "Cloning and characterization of a low molecular weight prolyl 4-
RT hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-
RT rich, collagen-like, and hypoxia-inducible transcription factor alpha-like
RT peptides.";
RL J. Biol. Chem. 277:23965-23971(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX DOI=10.1111/j.1399-3054.2007.00915.x;
RA Vlad F., Spano T., Vlad D., Bou Daher F., Ouelhadj A., Kalaitzis P.;
RT "Arabidopsis prolyl 4-hydroxylases are differentially expressed in response
RT to hypoxia, anoxia and mechanical wounding.";
RL Physiol. Plantarum 130:471-483(2007).
RN [7]
RP FUNCTION, AND INDUCTION BY HYPOXIA.
RX PubMed=19277739; DOI=10.1007/s10142-009-0118-y;
RA Asif M.H., Trivedi P.K., Misra P., Nath P.;
RT "Prolyl-4-hydroxylase (AtP4H1) mediates and mimics low oxygen response in
RT Arabidopsis thaliana.";
RL Funct. Integr. Genomics 9:525-535(2009).
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide
CC sequences of plant glycoproteins and other proteins. Hydroxylates
CC preferentially prolines in second positions in the -Pro-Pro-Gly-
CC triplets. Hydroxyprolines are important constituent of many plant cell
CC wall glycoproteins such as extensins, hydroxyproline-rich
CC glycoproteins, lectins and arabinogalactan proteins. Can hydroxylate
CC collagen-like peptides and hypoxia-inducible transcription factor
CC peptides. {ECO:0000269|PubMed:11976332, ECO:0000269|PubMed:19277739}.
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:11976332};
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:Q86KR9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for 2-oxoglutarate {ECO:0000269|PubMed:11976332};
CC KM=2 uM for poly(L-proline) polypeptides of 5-10 kDa
CC {ECO:0000269|PubMed:11976332};
CC KM=0.2 uM for poly(L-proline) polypeptides of 10-20 kDa
CC {ECO:0000269|PubMed:11976332};
CC KM=60 uM for (Ala-Thr-Pro-Pro-Pro-Val)3 peptide present in
CC arabinogalactan protein {ECO:0000269|PubMed:11976332};
CC KM=10 uM for Ser-Pro-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Val-Ser-Pro-Pro-
CC Pro-Pro-Val peptide present in extensin protein
CC {ECO:0000269|PubMed:11976332};
CC KM=40 uM for Ser-Pro-Pro-Pro-Val-Tyr-Lys-Ser-Pro-Pro-Pro-Pro-Val-Lys-
CC His-Tyr-Ser-Pro-Pro-Pro-Val peptide present in extensin protein
CC {ECO:0000269|PubMed:11976332};
CC KM=60 uM for (Pro-Pro-Gly)10 {ECO:0000269|PubMed:11976332};
CC KM=120 uM for (Pro-Pro-Gly)5 {ECO:0000269|PubMed:11976332};
CC KM=100 uM for (Ala-Pro-Gly)5 {ECO:0000269|PubMed:11976332};
CC KM=280 uM for (Pro-Ala-Gly)5 {ECO:0000269|PubMed:11976332};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q24JN5}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q24JN5}.
CC -!- INDUCTION: By hypoxia. {ECO:0000269|PubMed:19277739}.
CC -!- MISCELLANEOUS: Plants over-expressing P4H1 show absence of trichome on
CC leaf and petal surfaces, increased root hair and reduction in seed
CC size. {ECO:0000305|PubMed:19277739}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; AC004450; AAC64297.1; -; Genomic_DNA.
DR EMBL; AC006224; AAM15158.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10206.1; -; Genomic_DNA.
DR EMBL; AK117688; BAC42340.1; -; mRNA.
DR EMBL; BT006098; AAP04083.1; -; mRNA.
DR PIR; G84861; G84861.
DR RefSeq; NP_181836.1; NM_129869.5.
DR AlphaFoldDB; Q9ZW86; -.
DR SMR; Q9ZW86; -.
DR STRING; 3702.AT2G43080.1; -.
DR PaxDb; Q9ZW86; -.
DR PRIDE; Q9ZW86; -.
DR ProteomicsDB; 248812; -.
DR EnsemblPlants; AT2G43080.1; AT2G43080.1; AT2G43080.
DR GeneID; 818910; -.
DR Gramene; AT2G43080.1; AT2G43080.1; AT2G43080.
DR KEGG; ath:AT2G43080; -.
DR Araport; AT2G43080; -.
DR TAIR; locus:2041001; AT2G43080.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_2_0_1; -.
DR InParanoid; Q9ZW86; -.
DR OMA; QVLHYRP; -.
DR OrthoDB; 1438683at2759; -.
DR PhylomeDB; Q9ZW86; -.
DR BioCyc; ARA:AT2G43080-MON; -.
DR BRENDA; 1.14.11.2; 399.
DR SABIO-RK; Q9ZW86; -.
DR PRO; PR:Q9ZW86; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW86; baseline and differential.
DR Genevisible; Q9ZW86; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IDA:TAIR.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:TAIR.
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 PANTHER; PTHR10869; PTHR10869; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Endoplasmic reticulum; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..283
FT /note="Prolyl 4-hydroxylase 1"
FT /id="PRO_0000429335"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..283
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 162..279
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 270
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MUTAGEN 180
FT /note="H->A: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 180
FT /note="H->E: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 182
FT /note="D->A: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 182
FT /note="D->E: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 260
FT /note="H->A: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 260
FT /note="H->E: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 270
FT /note="K->A: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 270
FT /note="K->R: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 272
FT /note="S->A: Reduces activity 6-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 278
FT /note="R->A: Reduces activity more than 500-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
FT MUTAGEN 278
FT /note="R->H: Reduces activity 4-fold."
FT /evidence="ECO:0000269|PubMed:11976332"
SQ SEQUENCE 283 AA; 31530 MW; C4C02FBDB29D3F24 CRC64;
MAPAMKIVFG LLTFVTVGMV IGSLLQLAFI NRLEDSYGTG FPSLRGLRGQ NTRYLRDVSR
WANDKDAELL RIGNVKPEVV SWSPRIIVLH DFLSPEECEY LKAIARPRLQ VSTVVDVKTG
KGVKSDVRTS SGMFLTHVER SYPIIQAIEK RIAVFSQVPA ENGELIQVLR YEPQQFYKPH
HDYFADTFNL KRGGQRVATM LMYLTDDVEG GETYFPLAGD GDCTCGGKIM KGISVKPTKG
DAVLFWSMGL DGQSDPRSIH GGCEVLSGEK WSATKWMRQK ATS
