P4H7_ARATH
ID P4H7_ARATH Reviewed; 316 AA.
AC Q8L970; Q8VZD7; Q9LSI6;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable prolyl 4-hydroxylase 7 {ECO:0000305};
DE Short=AtP4H7 {ECO:0000303|Ref.5};
DE EC=1.14.11.2 {ECO:0000305};
GN Name=P4H7 {ECO:0000303|Ref.5}; OrderedLocusNames=At3g28480;
GN ORFNames=MFJ20.17;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8L970-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02864.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026644; BAB02864.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77450.1; -; Genomic_DNA.
DR EMBL; AY065036; AAL57673.1; -; mRNA.
DR EMBL; BT001114; AAN64505.1; -; mRNA.
DR EMBL; AY088608; AAM66931.1; -; mRNA.
DR RefSeq; NP_566838.1; NM_113768.4. [Q8L970-1]
DR AlphaFoldDB; Q8L970; -.
DR SMR; Q8L970; -.
DR STRING; 3702.AT3G28480.2; -.
DR MetOSite; Q8L970; -.
DR PRIDE; Q8L970; -.
DR ProteomicsDB; 248731; -. [Q8L970-1]
DR EnsemblPlants; AT3G28480.1; AT3G28480.1; AT3G28480. [Q8L970-1]
DR GeneID; 822478; -.
DR Gramene; AT3G28480.1; AT3G28480.1; AT3G28480. [Q8L970-1]
DR KEGG; ath:AT3G28480; -.
DR Araport; AT3G28480; -.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_5_0_1; -.
DR OMA; AWTFLPI; -.
DR PhylomeDB; Q8L970; -.
DR BRENDA; 1.14.11.2; 399.
DR PRO; PR:Q8L970; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L970; baseline and differential.
DR Genevisible; Q8L970; 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: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 InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10869; PTHR10869; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00254; ShKT; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Dioxygenase; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..316
FT /note="Probable prolyl 4-hydroxylase 7"
FT /id="PRO_0000429341"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..316
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 139..261
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 274..314
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 252
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 274..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 281..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 290..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CONFLICT 123
FT /note="S -> N (in Ref. 3; AAL57673/AAN64505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35570 MW; DEDCA0D43F8CAEF0 CRC64;
MDSRIFLAFS LCFLFTLPLI SSAPNRFLTR SSNTRDGSVI KMKTSASSFG FDPTRVTQLS
WTPRVFLYEG FLSDEECDHF IKLAKGKLEK SMVADNDSGE SVESEVRTSS GMFLSKRQDD
IVSNVEAKLA AWTFLPEENG ESMQILHYEN GQKYEPHFDY FHDQANLELG GHRIATVLMY
LSNVEKGGET VFPMWKGKAT QLKDDSWTEC AKQGYAVKPR KGDALLFFNL HPNATTDSNS
LHGSCPVVEG EKWSATRWIH VKSFERAFNK QSGCMDENVS CEKWAKAGEC QKNPTYMVGS
DKDHGYCRKS CKACSS
