P4H4_ARATH
ID P4H4_ARATH Reviewed; 298 AA.
AC Q8LAN3; Q8RWK0;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable prolyl 4-hydroxylase 4 {ECO:0000305};
DE Short=AtP4H4 {ECO:0000303|Ref.5};
DE EC=1.14.11.2 {ECO:0000305};
GN Name=P4H4 {ECO:0000303|Ref.5}; OrderedLocusNames=At5g18900;
GN ORFNames=F17K4.150;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
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 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:F4JAU3}.
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:F4JAU3};
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:F4JAU3}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:F4JAU3}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; AC068655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92626.1; -; Genomic_DNA.
DR EMBL; AY093039; AAM13038.1; -; mRNA.
DR EMBL; AY128940; AAM91340.1; -; mRNA.
DR EMBL; AY087708; AAM65245.1; -; mRNA.
DR RefSeq; NP_197391.1; NM_121895.4.
DR AlphaFoldDB; Q8LAN3; -.
DR SMR; Q8LAN3; -.
DR STRING; 3702.AT5G18900.1; -.
DR PaxDb; Q8LAN3; -.
DR PRIDE; Q8LAN3; -.
DR ProteomicsDB; 248883; -.
DR EnsemblPlants; AT5G18900.1; AT5G18900.1; AT5G18900.
DR GeneID; 832008; -.
DR Gramene; AT5G18900.1; AT5G18900.1; AT5G18900.
DR KEGG; ath:AT5G18900; -.
DR Araport; AT5G18900; -.
DR TAIR; locus:2144960; AT5G18900.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_5_0_1; -.
DR InParanoid; Q8LAN3; -.
DR OMA; FIERLWT; -.
DR OrthoDB; 1438683at2759; -.
DR PhylomeDB; Q8LAN3; -.
DR BioCyc; ARA:AT5G18900-MON; -.
DR BRENDA; 1.14.11.2; 399.
DR PRO; PR:Q8LAN3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LAN3; baseline and differential.
DR Genevisible; Q8LAN3; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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 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 2: Evidence at transcript level;
KW Dioxygenase; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..298
FT /note="Probable prolyl 4-hydroxylase 4"
FT /id="PRO_0000429338"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..298
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 120..245
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 258..298
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 236
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 258..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 265..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 274..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CONFLICT 188
FT /note="K -> E (in Ref. 3; AAM13038/AAM91340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33061 MW; 6028AE013F262662 CRC64;
MARRGLLISF FAIFSVLLQS STSLISSSSV FVNPSKVKQV SSKPRAFVYE GFLTELECDH
MVSLAKASLK RSAVADNDSG ESKFSEVRTS SGTFISKGKD PIVSGIEDKI STWTFLPKEN
GEDIQVLRYE HGQKYDAHFD YFHDKVNIVR GGHRMATILM YLSNVTKGGE TVFPDAEIPS
RRVLSENKED LSDCAKRGIA VKPRKGDALL FFNLHPDAIP DPLSLHGGCP VIEGEKWSAT
KWIHVDSFDR IVTPSGNCTD MNESCERWAV LGECTKNPEY MVGTTELPGY CRRSCKAC
