P4H6_ARATH
ID P4H6_ARATH Reviewed; 288 AA.
AC F4J0A8; Q84W84; Q9LSI5;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable prolyl 4-hydroxylase 6 {ECO:0000305};
DE Short=AtP4H6 {ECO:0000303|Ref.4};
DE EC=1.14.11.2 {ECO:0000305};
GN Name=P4H6 {ECO:0000303|Ref.4}; OrderedLocusNames=At3g28490;
GN ORFNames=MFJ20.18;
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] OF 36-288.
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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02865.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026644; BAB02865.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77452.1; -; Genomic_DNA.
DR EMBL; BT004123; AAO42145.1; -; mRNA.
DR RefSeq; NP_189490.2; NM_113769.3.
DR AlphaFoldDB; F4J0A8; -.
DR SMR; F4J0A8; -.
DR STRING; 3702.AT3G28490.1; -.
DR PaxDb; F4J0A8; -.
DR PRIDE; F4J0A8; -.
DR ProteomicsDB; 248730; -.
DR EnsemblPlants; AT3G28490.1; AT3G28490.1; AT3G28490.
DR GeneID; 822479; -.
DR Gramene; AT3G28490.1; AT3G28490.1; AT3G28490.
DR KEGG; ath:AT3G28490; -.
DR Araport; AT3G28490; -.
DR TAIR; locus:2088892; AT3G28490.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_5_0_1; -.
DR InParanoid; F4J0A8; -.
DR OMA; QDENWSA; -.
DR OrthoDB; 1438683at2759; -.
DR PRO; PR:F4J0A8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J0A8; baseline and differential.
DR Genevisible; F4J0A8; 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.
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..288
FT /note="Probable prolyl 4-hydroxylase 6"
FT /id="PRO_0000429340"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..288
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 116..238
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 248..288
FT /note="ShKT"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 229
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 248..288
FT /evidence="ECO:0000250"
FT DISULFID 255..281
FT /evidence="ECO:0000250"
FT DISULFID 264..285
FT /evidence="ECO:0000250"
SQ SEQUENCE 288 AA; 32448 MW; 387DC144A138C8AC CRC64;
MDSQYFLAFS LSLLLIFSQI SSFSFSVDPT RITQLSWTPR AFLYKGFLSD EECDHLIKLA
KGKLEKSMVV ADVDSGESED SEVRTSSGMF LTKRQDDIVA NVEAKLAAWT FLPEENGEAL
QILHYENGQK YDPHFDYFYD KKALELGGHR IATVLMYLSN VTKGGETVFP NWKGKTPQLK
DDSWSKCAKQ GYAVKPRKGD ALLFFNLHLN GTTDPNSLHG SCPVIEGEKW SATRWIHVRS
FGKKKLVCVD DHESCQEWAD AGECEKNPMY MVGSETSLGF CRKSCKAC
