GenomeNet

Database: UniProt
Entry: A0A1W4XI42_AGRPL
LinkDB: A0A1W4XI42_AGRPL
Original site: A0A1W4XI42_AGRPL 
ID   A0A1W4XI42_AGRPL        Unreviewed;       542 AA.
AC   A0A1W4XI42;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN   Name=LOC108741668 {ECO:0000313|RefSeq:XP_018332040.1,
GN   ECO:0000313|RefSeq:XP_025831160.1};
OS   Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC   Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX   NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018332040.1};
RN   [1] {ECO:0000313|RefSeq:XP_018332040.1, ECO:0000313|RefSeq:XP_025831160.1}
RP   IDENTIFICATION.
RC   TISSUE=Entire body {ECO:0000313|RefSeq:XP_018332040.1,
RC   ECO:0000313|RefSeq:XP_025831160.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC       hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other
CC       proteins. {ECO:0000256|ARBA:ARBA00002035}.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the P4HA family.
CC       {ECO:0000256|ARBA:ARBA00006511}.
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DR   RefSeq; XP_018332040.1; XM_018476538.1.
DR   RefSeq; XP_025831160.1; XM_025975375.1.
DR   STRING; 224129.A0A1W4XI42; -.
DR   EnsemblMetazoa; XM_018476538.1; XP_018332040.1; LOC108741668.
DR   EnsemblMetazoa; XM_025975375.1; XP_025831160.1; LOC108741668.
DR   GeneID; 108741668; -.
DR   KEGG; apln:108741668; -.
DR   Proteomes; UP000192223; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR   Gene3D; 6.10.140.1460; -; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR013547; Pro_4_hyd_alph_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF08336; P4Ha_N; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..542
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041056683"
FT   DOMAIN          414..522
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   542 AA;  62013 MW;  3D9AA9276A9209DE CRC64;
     MRLFAIRFAV ILFCQKVVLS ELYTALVDLK EVLYTEGVLI KTLETYIHAE TTKLKLLQRY
     VDLYKSQHQL ASEDVDTYVA NPINAYLLIK RLTADWRQVE SLLHMNLVQE TVANISAYKE
     YLKFPTDEDL NGAAVALTRL QDTYKLDTSS LARGELNGVK YSSELSATDC FELGRQSYNN
     GDFYHTQLWM TEADSRLGRE KNETIDKSEI LEYLAFSTFK LGDVPLALDL TNKLLEIYPN
     HPRAVNNKNY YESALAKTQG AHKKGDDNAY DVPIVSDMPV YSDSLDPPER TLYEQLCRGE
     VKTPVEITSK LKCYYYNKNR DPFLLLAPFK VEEAYKDPDI FIFHDVMYDE EIETIKNMAR
     PRFKRATVQN YKTGELETAQ YRISKSAWLK EIEHKHVANV CKRVVDMTGL TVETAEELQV
     VNYGIGGHYE PHFDFARRDE VNAFKSLGTG NRIATVLFYM SDVAQGGATV FPHLKLALWP
     KKGTAAFWYN LHSSGDGHIL TRHAACPVLA GSKWVSNKWI HEMGQEFRRP CDLQPPPPEL
     TI
//
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