P4H13_ARATH
ID P4H13_ARATH Reviewed; 274 AA.
AC F4ILF8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Prolyl 4-hydroxylase 13 {ECO:0000305};
DE Short=AtP4H13 {ECO:0000303|Ref.3};
DE EC=1.14.11.2 {ECO:0000305};
GN Name=P4H13 {ECO:0000303|Ref.3}; OrderedLocusNames=At2g23096;
GN ORFNames=F21P24;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21680836; DOI=10.1126/science.1206657;
RA Velasquez S.M., Ricardi M.M., Dorosz J.G., Fernandez P.V., Nadra A.D.,
RA Pol-Fachin L., Egelund J., Gille S., Harholt J., Ciancia M., Verli H.,
RA Pauly M., Bacic A., Olsen C.E., Ulvskov P., Petersen B.L., Somerville C.,
RA Iusem N.D., Estevez J.M.;
RT "O-glycosylated cell wall proteins are essential in root hair growth.";
RL Science 332:1401-1403(2011).
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. Possesses high affinity for leucine-rich
CC repeat and proline-rich extensins of root cell walls that are essential
CC for root hair development. Hydroxyprolines define the subsequent O-
CC glycosylation sites by arabinosyltransferases which elongate the O-
CC arabinosides on extensins. {ECO:0000269|PubMed:21680836}.
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:0000305|PubMed:21680836}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21680836}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermal root hair cells
CC (trichoblasts) root hairless cells (atrichoblasts).
CC {ECO:0000269|PubMed:21680836}.
CC -!- DISRUPTION PHENOTYPE: Reduced root hair length and content of
CC hydroxyproline in root cell walls. {ECO:0000269|PubMed:21680836}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC07409.1; -; Genomic_DNA.
DR RefSeq; NP_850038.1; NM_179707.3.
DR AlphaFoldDB; F4ILF8; -.
DR SMR; F4ILF8; -.
DR STRING; 3702.AT2G23096.1; -.
DR PaxDb; F4ILF8; -.
DR PRIDE; F4ILF8; -.
DR EnsemblPlants; AT2G23096.1; AT2G23096.1; AT2G23096.
DR GeneID; 816841; -.
DR Gramene; AT2G23096.1; AT2G23096.1; AT2G23096.
DR KEGG; ath:AT2G23096; -.
DR Araport; AT2G23096; -.
DR TAIR; locus:1005716656; AT2G23096.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_1_1_1; -.
DR InParanoid; F4ILF8; -.
DR OMA; EAVIDMA; -.
DR OrthoDB; 1438683at2759; -.
DR PhylomeDB; F4ILF8; -.
DR PRO; PR:F4ILF8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4ILF8; baseline.
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 GO; GO:0080147; P:root hair cell development; IMP:TAIR.
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; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..274
FT /note="Prolyl 4-hydroxylase 13"
FT /id="PRO_0000429346"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..274
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 151..270
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 171
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 261
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 274 AA; 31424 MW; 2A1EC5F9DE823A51 CRC64;
MRSYGKEKKL VFPYVFIACC FFLAIFGFCF FNLFSQGISF SEIPTTRRSV NDETDSLDHG
SSVSNIPFHG LSWNPRVFYL PNFATKQQCE AVIDMAKPKL KPSTLALRKG ETAETTQNYR
SLHQHTDEDE SGVLAAIEEK IALATRFPKD YYESFNILRY QLGQKYDSHY DAFHSAEYGP
LISQRVVTFL LFLSSVEEGG ETMFPFENGR NMNGRYDYEK CVGLKVKPRQ GDAIFFYNLF
PNGTIDQTSL HGSCPVIKGE KWVATKWIRD QTYD
