ID A0A0V1HBS3_9BILA Unreviewed; 579 AA.
AC A0A0V1HBS3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN Name=phy-2 {ECO:0000313|EMBL:KRZ08254.1};
GN ORFNames=T11_13323 {ECO:0000313|EMBL:KRZ08254.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08254.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ08254.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08254.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ08254.1}.
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DR EMBL; JYDP01000089; KRZ08254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HBS3; -.
DR STRING; 268475.A0A0V1HBS3; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
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; 3.
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; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF207; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-2; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000055024};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..579
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006879021"
FT DOMAIN 456..562
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT COILED 50..77
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 579 AA; 67159 MW; D09BE178E918071E CRC64;
MATLHFIIFI TLMDWWYAMR SSAEVFTAMA DVENLIHTED NVVDVIEQYI ESDLRRLQRL
KSLAQEYRES KEKALKEGTD RLYNPVNAFL FIKKLTEEWN DVEQLMKSDH ADIYLQNITA
MRDSSMAKFP TEEDLTGAAE ALLRLQDVYK LDTHELSSGR IKGAKQGLEL DANGCFELGR
VAYNQKDYYH VILWMQEALN RVEHENPPSV DQAEILEYLA FGMYQQGNVK RALQLTKRLQ
RIKPDHPRAE GNVKWYLDML AKEGVSRVTD HDLPPIVNAR PNDQALPERK DFEALCRGEY
LLTEKQRSHL YCYYKRDTPF LILAPIKVEV MHWKPKIVIF RQVISANEIA VLKTLAYPRL
SRATVQNSET GELETAKYRI SKRCRILRRA TVHNKETGQL EHASYRISKS AWLKEHEHPV
VERIVKRIHD MTNLNMETAE DLQIANYGLG GHYDPHFDHA RIANYGIGGH YEPHFDMSTR
DEVDPYEHGH GNRIATALFY KEEVNAFKSL NTGNRIATVL FYGDAAFWFN LKSNGEGDMS
TRHAACPVLS GVKWVANKWI HERGQEFYRP CGLREDDYE
//