ID A0A1L8GVE2_XENLA Unreviewed; 537 AA.
AC A0A1L8GVE2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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};
GN Name=p4ha2.S {ECO:0000313|Xenbase:XB-GENE-17333117};
GN Synonyms=LOC108713277 {ECO:0000313|RefSeq:XP_018111684.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018111684.1};
RN [1] {ECO:0000313|RefSeq:XP_018111684.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018111684.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018111684.1};
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_018111684.1; XM_018256195.2.
DR AlphaFoldDB; A0A1L8GVE2; -.
DR STRING; 8355.A0A1L8GVE2; -.
DR PaxDb; 8355-A0A1L8GVE2; -.
DR GeneID; 108713277; -.
DR KEGG; xla:108713277; -.
DR CTD; 108713277; -.
DR Xenbase; XB-GENE-17333117; p4ha2.S.
DR OMA; EEHEIVH; -.
DR OrthoDB; 2899308at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 108713277; Expressed in zone of skin and 16 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000186698}.
SQ SEQUENCE 537 AA; 61561 MW; 0DDCA26C9D60ABA0 CRC64;
MELNAISLIL VSLCCIWQVQ AEVFTSTGHM TDLIYRERDL VQSLKEYIRE EEERLSKIKS
WATQLDELTS RSTADPEGYL GHPVNAYKLV KRFNTDWTSL ESLVLQDSTK GFIANLTFQK
EYFPTEEDEK GAAKALMRLQ DTYKLDPDII AKGKLPGTNY ISSLSADDTF GMGKIAYHDG
DYYHTVLWMQ QALKQLDEGE RAEISQVEVL DYLSYTVFQL GDVPRAVELT KRLLALDSNH
ERAGNNLKYF EKMQEKEKAE LKQNESTQTE TATRQPGVYS RPLDYLPERD VYEALCRGEG
VKMNPRRQKR LFCRYHNGNR NPYLILGPIK MEDEWDSPRI VRYLEVLSDE EIKKIKELAK
PRLARATVRD PKTGVLTVAS YRVSKSAWLE EEDDPVIGRV NSRMQAITGL TKDTAELLQV
ANYGMGGQYE PHFDFSRKEE PDVFKRLGTG NRVATYLNYM SDVEAGGATV FPDFGAAIWP
KKGTAVFWYN LFRSGEGDYR TRHAACPVLV GCKWVSNKWF HERGQEFLRP CGLTEVD
//
