ID A0A0V1DBQ7_TRIBR Unreviewed; 1130 AA.
AC A0A0V1DBQ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:KRY58929.1};
GN ORFNames=T03_10089 {ECO:0000313|EMBL:KRY58929.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58929.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY58929.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY58929.1};
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:KRY58929.1}.
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DR EMBL; JYDI01000017; KRY58929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DBQ7; -.
DR Proteomes; UP000054653; 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; -; 2.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 4.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; 2.
DR Pfam; PF08336; P4Ha_N; 2.
DR SMART; SM00702; P4Hc; 2.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51471; FE2OG_OXY; 2.
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:UP000054653};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1130
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006876657"
FT DOMAIN 415..544
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 1005..1113
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 264..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 623..650
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1130 AA; 129702 MW; 94D33E6ADCC15873 CRC64;
MLNMIWPLTT ATLLLGAITP FSRGEVFTSM ANIDMLLQMG EDVSRIIDNY VEEDERRLEQ
LKKLSAEYKS HKVQVHGQES TDSVIVNPVE SFAIVKQLAD NWRYVEQLMK TNSAEKLIQN
FTHHTHNSVV RPPSEEDVIG MAVGLMRIQD VYKLDTHDMA EGKIRGVLDG RKLTAYDCLE
IARVAYNKQD FYHTLLWATE AWDRVQKEDE PTIDEATVLE YIAFAMFKQG NIEWAIHYTT
LIKQVDPNHP RASGNLKYYQ DLLDPEGKPR KIDPKKLPPP TNRRPDDLSI PERDVYEGLC
RSEYPIPDKD RAKLYCYYKR NRPYLKLAPI KVEVMHWKPK IVYFRGVISD EEIAVIKQLA
SPLLKRATVH NADTGQLETA SYRISKSAWL KDTEHEVVKR ISDRIDMMTD LTMETAELLQ
IANYGIGGHY DPHFDMSTRG ESDPYEEGTG NRIATVLFYT NDPYSFESLN AGNRIATVLF
YISQPEAGGG TVFTSHKITV EPSKYDAAFW FNVLQGGEPD MSTRHAACPV LAGTKWVANK
WIHERGQEFR RPFFSPGCVT SATRLLLLLK TPTMALLHII IFITLMDWWC VMRSSAEVFT
AMADVENLIH TEDNVVDVIE QYIESDLRRL QRLKSLAQEY RESKEKALKE GADRLYNPVN
AFLFIKKLTE EWNDVELLMK SDHADIYLQN ITAMRDSSLA KFPTEEDLTG AAEALLRLQD
VYKLDTHELS SGRIKGAKQG LELDANGCFE LGRVAYNQKD YYHVILWMQE ALNRVEHENP
PSVDQAEILE YLAYGMYQQG NVKRALQLTK RLQRIKPDHP RAEGNVKWYL DLLAKEGVSR
VTDHDLPPIV NARPNDQALP ERKDFEALCR GEYLLTEKQR SRLYCYYKRD TPFLNLAPIK
VEVMHWKPKI VIFRQVISAN EIAVLKTLAY PRLSRATVQN SETGELETAK YRISKRATVH
NKETGQLEHA SYRISKSAWL KEHEHPVVDR IVKRIHDMTN LNMETAEDLQ IANYGLGGHY
DPHFDHARKE EVNAFKSLNT GNRIATVLFY ISQPEAGGAT VFITHKLAIF PVEGDAAFWF
NLKPNGEGDM STRHAACPVL AGVKWVANKW IHERGQEFYR PCGLREDDYE
//
