ID A0A1S3HBJ3_LINUN Unreviewed; 547 AA.
AC A0A1S3HBJ3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN Name=LOC106153822 {ECO:0000313|RefSeq:XP_013383378.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013383378.1};
RN [1] {ECO:0000313|RefSeq:XP_013383378.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013383378.1};
RG RefSeq;
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 RefSeq; XP_013383378.1; XM_013527924.1.
DR AlphaFoldDB; A0A1S3HBJ3; -.
DR STRING; 7574.A0A1S3HBJ3; -.
DR EnsemblMetazoa; g5905.t1; g5905.t1; g5905.
DR EnsemblMetazoa; XM_013527924.1; XP_013383378.1; LOC106153822.
DR GeneID; 106153822; -.
DR KEGG; lak:106153822; -.
DR InParanoid; A0A1S3HBJ3; -.
DR OMA; IATVMYY; -.
DR OrthoDB; 2899308at2759; -.
DR Proteomes; UP000085678; 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: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 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:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..547
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010310066"
FT DOMAIN 418..529
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 547 AA; 61607 MW; 0A721CCA2615EE8D CRC64;
MNNSIIIILT AVFSSYHYIA RAEVYSSTAD VVQLANNEQL LVGLLETYLD NELARIKELQ
THLEDIKKLL PENTETSIAN YAVNPVGAYS TIKRFAVTWT HFFAQISDLK HANNTALRGL
ATDIVSLGLS HHIWPQVVDL NGAVAALVRL QKMYQIPVKE LADGNIRGMK VSRLGPDDCL
RLGRAMLHSD YSSSSAALAI QWMEEAIRMH EQRHSANGEQ SLGDRSFQIE EAYSALADAH
AQLGNVTAAA NFAMKAFVKD PENSSLKEKF LKYEDMSSGS HSQKKISRRN TTDSMYERLC
RGDQWKDPKI EARLFCQYKN TLVPIRPVKE EVLYLDPRVS IFYDVITDKE AAILLELAKS
KMIRAPLGDV AGEKTSEQRI GKLTWLWDAD VNTTVAHLSK RVEEITGLST VIRDKLADAE
AWQIATYGIG GMFEPHHDFY VDEGWLNQLP SHLLNTGRRI ATFVFYLTDV QLGGATVFPE
INVRVPPVKN AAAFWYNLKR SGDMYHASMH AGCPVLYGQK WIANKWTRER GQIFRRRCGL
SPRATDE
//
