P4H5_ARATH
ID P4H5_ARATH Reviewed; 291 AA.
AC Q24JN5; Q8LB05;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Prolyl 4-hydroxylase 5 {ECO:0000305};
DE Short=AtP4H5 {ECO:0000303|PubMed:21680836};
DE EC=1.14.11.2 {ECO:0000305};
GN Name=P4H5 {ECO:0000303|PubMed:21680836}; OrderedLocusNames=At2g17720;
GN ORFNames=T17A5.10;
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;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21680836; DOI=10.1126/science.1206657;
RA Velasquez S.M., Ricardi M.M., Dorosz J.G., Fernandez P.V., Nadra A.D.,
RA Pol-Fachin L., Egelund J., Gille S., Harholt J., Ciancia M., Verli H.,
RA Pauly M., Bacic A., Olsen C.E., Ulvskov P., Petersen B.L., Somerville C.,
RA Iusem N.D., Estevez J.M.;
RT "O-glycosylated cell wall proteins are essential in root hair growth.";
RL Science 332:1401-1403(2011).
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. Hydroxyprolines
CC are important constituent of many plant cell wall glycoproteins such as
CC extensins, hydroxyproline-rich glycoproteins, lectins and
CC arabinogalactan proteins. Possesses high affinity for leucine-rich
CC repeat and proline-rich extensins of root cell walls that are essential
CC for root hair development. Hydroxyprolines define the subsequent O-
CC glycosylation sites by arabinosyltransferases which elongate the O-
CC arabinosides on extensins. {ECO:0000269|PubMed:21680836}.
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:Q9ZW86};
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:21680836}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21680836}. Golgi apparatus membrane
CC {ECO:0000305|PubMed:21680836}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21680836}. Note=Predominantly localized in the
CC endoplasmic reticulum. {ECO:0000269|PubMed:21680836}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermal root hair cells
CC (trichoblasts). {ECO:0000269|PubMed:21680836}.
CC -!- DISRUPTION PHENOTYPE: Reduced root hair length and content of
CC hydroxyproline in root cell walls. {ECO:0000269|PubMed:21680836}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; CP002685; AEC06673.1; -; Genomic_DNA.
DR EMBL; BT024854; ABD65585.1; -; mRNA.
DR EMBL; AK229496; BAF01353.1; -; mRNA.
DR EMBL; AY087497; AAM65040.1; -; mRNA.
DR PIR; T08863; T08863.
DR RefSeq; NP_179363.1; NM_127326.5.
DR AlphaFoldDB; Q24JN5; -.
DR SMR; Q24JN5; -.
DR STRING; 3702.AT2G17720.1; -.
DR PaxDb; Q24JN5; -.
DR PRIDE; Q24JN5; -.
DR ProteomicsDB; 248729; -.
DR EnsemblPlants; AT2G17720.1; AT2G17720.1; AT2G17720.
DR GeneID; 816281; -.
DR Gramene; AT2G17720.1; AT2G17720.1; AT2G17720.
DR KEGG; ath:AT2G17720; -.
DR Araport; AT2G17720; -.
DR TAIR; locus:2827906; AT2G17720.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_1_2_1; -.
DR InParanoid; Q24JN5; -.
DR OMA; GKHAHTR; -.
DR OrthoDB; 1438683at2759; -.
DR PhylomeDB; Q24JN5; -.
DR BioCyc; ARA:AT2G17720-MON; -.
DR PRO; PR:Q24JN5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q24JN5; baseline and differential.
DR Genevisible; Q24JN5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000137; C:Golgi cis cisterna; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IBA:GO_Central.
DR GO; GO:0080147; P:root hair cell development; IMP: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 2: Evidence at transcript level;
KW Dioxygenase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="Prolyl 4-hydroxylase 5"
FT /id="PRO_0000429339"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..291
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 163..286
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 277
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 291 AA; 32691 MW; DC3DB2C428BD9B75 CRC64;
MASKSKQHLR YQPRKSVSRS TQAFTVLILL LVVILILLGL GILSLPNANR NSSKTNDLTN
IVRKSETSSG DEEGNGERWV EVISWEPRAV VYHNFLTNEE CEHLISLAKP SMVKSTVVDE
KTGGSKDSRV RTSSGTFLRR GHDEVVEVIE KRISDFTFIP VENGEGLQVL HYQVGQKYEP
HYDYFLDEFN TKNGGQRIAT VLMYLSDVDD GGETVFPAAR GNISAVPWWN ELSKCGKEGL
SVLPKKRDAL LFWNMRPDAS LDPSSLHGGC PVVKGNKWSS TKWFHVHEFK V
