P4H2_ARATH
ID P4H2_ARATH Reviewed; 299 AA.
AC F4JAU3; Q0WP28; Q8L8T9; Q9SQT3;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Prolyl 4-hydroxylase 2 {ECO:0000305};
DE Short=AtP4H-2 {ECO:0000303|PubMed:15528200};
DE Short=AtP4H2 {ECO:0000303|Ref.6};
DE EC=1.14.11.2 {ECO:0000269|PubMed:15528200};
GN Name=P4H2 {ECO:0000303|Ref.6}; OrderedLocusNames=At3g06300;
GN ORFNames=F24P17.24;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15528200; DOI=10.1074/jbc.m411109200;
RA Tiainen P., Myllyharju J., Koivunen P.;
RT "Characterization of a second Arabidopsis thaliana prolyl 4-hydroxylase
RT with distinct substrate specificity.";
RL J. Biol. Chem. 280:1142-1148(2005).
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. Has low affinity for the substrates tested
CC in vitro. {ECO:0000269|PubMed:15528200, 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:0000269|PubMed:15528200};
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=170 uM for 2-oxoglutarate {ECO:0000269|PubMed:15528200};
CC KM=30 uM for poly(L-proline) polypeptides of 5-10 kDa
CC {ECO:0000269|PubMed:15528200};
CC KM=1260 uM for (Ala-Thr-Pro-Pro-Pro-Val)3 peptide present in
CC arabinogalactan protein {ECO:0000269|PubMed:15528200};
CC KM=660 uM for Ser-Pro-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Val-Ser-Pro-
CC Pro-Pro-Pro-Val peptide present in extensin protein
CC {ECO:0000269|PubMed:15528200};
CC KM=380 uM for Ser-Pro-Pro-Pro-Val-Tyr-Lys-Ser-Pro-Pro-Pro-Pro-Val-
CC Lys-His-Tyr-Ser-Pro-Pro-Pro-Val peptide present in extensin protein
CC {ECO:0000269|PubMed:15528200};
CC KM=2800 uM for (Pro-Pro-Gly)10 {ECO:0000269|PubMed:15528200};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF08583.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM67123.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC011623; AAF08583.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74370.1; -; Genomic_DNA.
DR EMBL; AK229257; BAF01121.1; -; mRNA.
DR EMBL; AY088813; AAM67123.1; ALT_INIT; mRNA.
DR RefSeq; NP_566279.1; NM_111505.4.
DR AlphaFoldDB; F4JAU3; -.
DR SMR; F4JAU3; -.
DR STRING; 3702.AT3G06300.1; -.
DR PaxDb; F4JAU3; -.
DR PRIDE; F4JAU3; -.
DR ProteomicsDB; 248882; -.
DR EnsemblPlants; AT3G06300.1; AT3G06300.1; AT3G06300.
DR GeneID; 819804; -.
DR Gramene; AT3G06300.1; AT3G06300.1; AT3G06300.
DR KEGG; ath:AT3G06300; -.
DR Araport; AT3G06300; -.
DR TAIR; locus:2081106; AT3G06300.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_5_0_1; -.
DR InParanoid; F4JAU3; -.
DR OMA; SNPEYMV; -.
DR OrthoDB; 1438683at2759; -.
DR PRO; PR:F4JAU3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JAU3; baseline and differential.
DR Genevisible; F4JAU3; 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:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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:0005802; C:trans-Golgi network; 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; IDA:TAIR.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:TAIR.
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 InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10869; PTHR10869; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..299
FT /note="Prolyl 4-hydroxylase 2"
FT /id="PRO_0000429336"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..299
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 121..246
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 259..299
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT BINDING 139
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 141
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 237
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 259..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 266..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 275..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CONFLICT 51
FT /note="E -> G (in Ref. 3; BAF01121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 33019 MW; FDFB924205AA4F43 CRC64;
MSMSRLGLLL FVAILLVLLQ SSTCLISSPS SIINPSKVKQ VSSKPRAFVY EGFLTDLECD
HLISLAKENL QRSAVADNDN GESQVSDVRT SSGTFISKGK DPIVSGIEDK LSTWTFLPKE
NGEDLQVLRY EHGQKYDAHF DYFHDKVNIA RGGHRIATVL LYLSNVTKGG ETVFPDAQEF
SRRSLSENKD DLSDCAKKGI AVKPKKGNAL LFFNLQQDAI PDPFSLHGGC PVIEGEKWSA
TKWIHVDSFD KILTHDGNCT DVNESCERWA VLGECGKNPE YMVGTPEIPG NCRRSCKAC
