P4H9_ARATH
ID P4H9_ARATH Reviewed; 288 AA.
AC Q8VZJ7; O81759;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable prolyl 4-hydroxylase 9 {ECO:0000305};
DE Short=AtP4H9 {ECO:0000303|Ref.6};
DE EC=1.14.11.2 {ECO:0000305};
GN Name=P4H9 {ECO:0000303|Ref.6}; OrderedLocusNames=At4g33910;
GN ORFNames=F17I5.100;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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=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 [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 SUBCELLULAR LOCATION.
RX PubMed=22430844; DOI=10.1104/pp.111.193151;
RA Parsons H.T., Christiansen K., Knierim B., Carroll A., Ito J., Batth T.S.,
RA Smith-Moritz A.M., Morrison S., McInerney P., Hadi M.Z., Auer M.,
RA Mukhopadhyay A., Petzold C.J., Scheller H.V., Loque D., Heazlewood J.L.;
RT "Isolation and proteomic characterization of the Arabidopsis Golgi defines
RT functional and novel components involved in plant cell wall biosynthesis.";
RL Plant Physiol. 159:12-26(2012).
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).
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. {ECO:0000250|UniProtKB:Q9ZW86}.
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:0000250|UniProtKB:F4ILF8}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:F4ILF8}. Golgi apparatus
CC {ECO:0000305|PubMed:22430844}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19873.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80108.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031032; CAA19873.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80108.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86292.1; -; Genomic_DNA.
DR EMBL; AY064069; AAL36425.1; -; mRNA.
DR EMBL; AY096377; AAM20018.1; -; mRNA.
DR EMBL; AY086254; AAM64328.1; -; mRNA.
DR PIR; T05219; T05219.
DR RefSeq; NP_567941.1; NM_119550.3.
DR AlphaFoldDB; Q8VZJ7; -.
DR SMR; Q8VZJ7; -.
DR BioGRID; 14817; 1.
DR STRING; 3702.AT4G33910.1; -.
DR PaxDb; Q8VZJ7; -.
DR PRIDE; Q8VZJ7; -.
DR ProteomicsDB; 248813; -.
DR EnsemblPlants; AT4G33910.1; AT4G33910.1; AT4G33910.
DR GeneID; 829535; -.
DR Gramene; AT4G33910.1; AT4G33910.1; AT4G33910.
DR KEGG; ath:AT4G33910; -.
DR Araport; AT4G33910; -.
DR TAIR; locus:2118889; AT4G33910.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_1_1_1; -.
DR InParanoid; Q8VZJ7; -.
DR OMA; HHGMKVR; -.
DR OrthoDB; 1438683at2759; -.
DR PhylomeDB; Q8VZJ7; -.
DR BioCyc; ARA:AT4G33910-MON; -.
DR PRO; PR:Q8VZJ7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VZJ7; baseline and differential.
DR Genevisible; Q8VZJ7; 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; IDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA: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; IBA:GO_Central.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IBA:GO_Central.
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..288
FT /note="Probable prolyl 4-hydroxylase 9"
FT /id="PRO_0000429342"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..288
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 164..283
FT /note="Fe2OG dioxygenase"
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 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 274
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 288 AA; 32279 MW; 1A8BEF7A3135A534 CRC64;
MKSRLKSYRR KKLGLATVIV FCSLCFLFGF YGSTLLSQNV PRVKPRLRML DMVENGEEEA
SSMPHGVTGE ESIGSIPFQV LSWRPRAIYF PNFATAEQCQ AIIERAKVNL KPSALALRKG
ETAENTKGTR TSSGTFISAS EESTGALDFV ERKIARATMI PRSHGESFNI LRYELGQKYD
SHYDVFNPTE YGPQSSQRIA SFLLYLSDVE EGGETMFPFE NGSNMGIGYD YKQCIGLKVK
PRKGDGLLFY SVFPNGTIDQ TSLHGSCPVT KGEKWVATKW IRDQDQEE
