ID A0A3B3RA37_9TELE Unreviewed; 532 AA.
AC A0A3B3RA37;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000014770.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000014770.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3RA37; -.
DR STRING; 1676925.ENSPKIP00000014770; -.
DR Ensembl; ENSPKIT00000039225.1; ENSPKIP00000014770.1; ENSPKIG00000001702.1.
DR GeneTree; ENSGT00940000157695; -.
DR OrthoDB; 2899308at2759; -.
DR Proteomes; UP000261540; 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; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF240; 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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..532
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017338141"
FT DOMAIN 411..517
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 532 AA; 60622 MW; 24220DE8707AF05B CRC64;
MRLAMFFCLS GALFCIPHIQ AEFYTSIGQM TELIFTEREL VHSLKEYICS AESKLAFIKS
WADKLDVLTQ VSTADPEGYL AHPVNAYKLM KRLNSEWPQL ETLVQQDLSS GFIANISLRR
QFFPDDEDER GAARALFRLQ DTYRLDSELL SSGQLPGVQY SSHLSADDCY SLGKTAYEEE
DHYHSVLWMQ EALRRLHTGE EAFVSQAEVL DYLSYSVYQM GDVHRTRELT RRLISADPTH
ERARGNLQHL ELILSNEATQ SSTMATAAKP ITLETYQRPP SHLSDREMYE ALCRGEGATM
TPQRRSKLFC RYQDRGRNPR LLVAPMKEED EWDSPHIVRY HDALSQAEIE RIKDLAKPKL
ARATIRDPVS GVLTVANYRV SKSAWLEHKV DPVIARVTRR IADVTGLSLE TAESLQVANY
GIGGQYEPHY DFSRRPFDSD LKIEGNRLAT YLNYLSDVEA GGATVFTDIG VALRPRQGTA
VFWHNLHRSG RGDLRTRHAA CPVLLGNKWV ANMWIHERGQ EFRRQCGLTE GD
//
