ID T1IPB6_STRMM Unreviewed; 401 AA.
AC T1IPB6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR002865-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR002865-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) 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; JH431254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1IPB6; -.
DR STRING; 126957.T1IPB6; -.
DR EnsemblMetazoa; SMAR002865-RA; SMAR002865-PA; SMAR002865.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_024155_1_1_1; -.
DR OrthoDB; 520341at2759; -.
DR PhylomeDB; T1IPB6; -.
DR Proteomes; UP000014500; 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 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 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 PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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:UP000014500};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..401
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004579390"
FT DOMAIN 292..401
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT COILED 30..60
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 401 AA; 45490 MW; BD988B9A59E31378 CRC64;
MAASVLLFLL LIRGFNAEVF SSTAHLSTVL NAEREIIGQL ERYIENAEIK TDRLRRYIDE
FNDIQVRADV DEIVGNPLSA YQLVKRLTVD WGSVERLLYD NSWQARSGIG KWSTNLELQG
YHRHTFQQPI RGRTPAEIKG LLISTRTKYN LGNGLSYDDE TKNYQALCRG EQLRSDSIVA
SLNCYLSDRG HPSFYINPIK VEVHSHDPPL FTFHDVIYES EINFIKEFSK PLLERSTVLG
NDGNAREVSN VRTSQNAWLT DDAQDDYSRY QLKIIMDRLS RVTGLKIHGE QNSEAMQVAN
YGIGGHYEPH HDYLFKDKTP EQLANVSPIN YATGDRLATL MFYLSDVTRG GATVFPRIGA
AVWPRKGSAV FWYNLRKSGE SNPLTLHGAC PVLHGSKWGT K
//
