P4H10_ARATH
ID P4H10_ARATH Reviewed; 289 AA.
AC F4JZ24; Q9FKX6;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Probable prolyl 4-hydroxylase 10 {ECO:0000305};
DE Short=AtP4H10 {ECO:0000303|Ref.3};
DE EC=1.14.11.2 {ECO:0000305};
GN Name=P4H10 {ECO:0000303|Ref.3}; OrderedLocusNames=At5g66060;
GN ORFNames=K2A18.14;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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:Q24JN5}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q24JN5}.
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=F4JZ24-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10411.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB011474; BAB10411.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98153.1; -; Genomic_DNA.
DR RefSeq; NP_201407.4; NM_126004.6. [F4JZ24-1]
DR AlphaFoldDB; F4JZ24; -.
DR SMR; F4JZ24; -.
DR STRING; 3702.AT5G66060.1; -.
DR PaxDb; F4JZ24; -.
DR PRIDE; F4JZ24; -.
DR ProteomicsDB; 248881; -. [F4JZ24-1]
DR EnsemblPlants; AT5G66060.1; AT5G66060.1; AT5G66060. [F4JZ24-1]
DR GeneID; 836738; -.
DR Gramene; AT5G66060.1; AT5G66060.1; AT5G66060. [F4JZ24-1]
DR KEGG; ath:AT5G66060; -.
DR Araport; AT5G66060; -.
DR TAIR; locus:2156852; AT5G66060.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_1_2_1; -.
DR InParanoid; F4JZ24; -.
DR OMA; RVNEYKI; -.
DR OrthoDB; 1438683at2759; -.
DR PRO; PR:F4JZ24; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZ24; baseline and differential.
DR Genevisible; F4JZ24; 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:0000137; C:Golgi cis 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 3: Inferred from homology;
KW Alternative splicing; Dioxygenase; Endoplasmic reticulum; Glycoprotein;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Probable prolyl 4-hydroxylase 10"
FT /id="PRO_0000429343"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..289
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 161..284
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 179
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 275
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 289 AA; 32598 MW; 4C4E512D432A15F6 CRC64;
MMARPRNHRP SARKSSHSTL VFAVLIMSTF VILILLAFGI LSVPSNNAGS SKANDLTSIV
RKTLQRSGED DSKNERWVEI ISWEPRASVY HNFLTKEECK YLIELAKPHM EKSTVVDEKT
GKSTDSRVRT SSGTFLARGR DKTIREIEKR ISDFTFIPVE HGEGLQVLHY EIGQKYEPHY
DYFMDEYNTR NGGQRIATVL MYLSDVEEGG ETVFPAAKGN YSAVPWWNEL SECGKGGLSV
KPKMGDALLF WSMTPDATLD PSSLHGGCAV IKGNKWSSTK WLRVHEYKV
