ID H0WJ74_OTOGA Unreviewed; 544 AA.
AC H0WJ74;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN Name=P4HA3 {ECO:0000313|Ensembl:ENSOGAP00000001529.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000001529.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000001529.2}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AAQR03001144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03001145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03001146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03001147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03001148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003780953.1; XM_003780905.2.
DR AlphaFoldDB; H0WJ74; -.
DR STRING; 30611.ENSOGAP00000001529; -.
DR Ensembl; ENSOGAT00000001714.2; ENSOGAP00000001529.2; ENSOGAG00000001712.2.
DR GeneID; 100960719; -.
DR KEGG; oga:100960719; -.
DR CTD; 283208; -.
DR eggNOG; KOG1591; Eukaryota.
DR GeneTree; ENSGT00940000158967; -.
DR HOGENOM; CLU_024155_1_0_1; -.
DR InParanoid; H0WJ74; -.
DR OMA; DVYMPAV; -.
DR OrthoDB; 2899308at2759; -.
DR TreeFam; TF313393; -.
DR Proteomes; UP000005225; 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; 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:SF223; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-3; 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:UP000005225};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..544
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003544249"
FT DOMAIN 422..529
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 544 AA; 61168 MW; 90DBBD101835986D CRC64;
MGPKALLAAL MTVLTLRPGD PAGAAARGDT FSALTSVARA LAPERRLLGL LRRYLRGEEA
RLRDLTRFYD KVLSLHEEST SPVANPLLAF TLIKRLQSDW RNIVHSLEAS ENIQALKDGY
EKVEQDLPAF EDLEGAARAL MRLQDVYMLN VKGLARGVFQ RVTGSAVTDL YSPRQLFSLT
ADDCFQVGKV AYDMGDYYHA IPWLEEAVSL FRGSYGEWKT EDEASLEDAL DHLAFAYFKA
GNVSWALSLS REFLLYSPDN KRMARNVLKY EKLLAESPNQ AVAETVMQRP NVPHLQTRDT
YEGLCQTLGS QPTHYQIPSL YCSYETNSSP YLLLQPIRKE VIHLEPFVAL YHDFVSDSEA
QKIRELAEPW LQRSVVASGE KQLQVDYRIS KSAWLKDTVD PMLVTLDHRI AALTGLDVQP
PYAEYLQVVN YGIGGHYEPH FDHATSPSSP LYRMKSGNRV ATFMIYLSSV EAGGATAFIY
ANFSVPVVKN AALFWWNLHR NGEGDSDTLH AGCPVLVGDK WVANKWIHEY GQEFRRPCSS
SPED
//
