ID A0A1U7RPD3_ALLSI Unreviewed; 538 AA.
AC A0A1U7RPD3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN Name=P4HA2 {ECO:0000313|RefSeq:XP_006023624.1,
GN ECO:0000313|RefSeq:XP_025059867.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006023624.1};
RN [1] {ECO:0000313|RefSeq:XP_006023624.1, ECO:0000313|RefSeq:XP_025059867.1}
RP IDENTIFICATION.
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_006023624.1; XM_006023562.3.
DR RefSeq; XP_006023625.1; XM_006023563.2.
DR RefSeq; XP_025059867.1; XM_025204082.1.
DR GeneID; 102373565; -.
DR KEGG; asn:102373565; -.
DR CTD; 8974; -.
DR eggNOG; KOG1591; Eukaryota.
DR OrthoDB; 2899308at2759; -.
DR Proteomes; UP000189705; 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 Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..538
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010815540"
FT DOMAIN 415..523
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 538 AA; 61905 MW; 3C93E42AEB929952 CRC64;
MMKPWMLLLL LTCISCTWPT QAEFFTSIGQ MTDLVYAEKD LVRSLKEYIR EEESKLSKIK
SWAEKMEAVT SKSTSDPEGY LAHPVNAYKL VKRLNTEWLE LENLVLQDTT NGFIANLTIQ
RQFFPTEEDE TGAAKALMRL QDTYKLDPET ISKGVLPGTK YRSSLTVDDC FGMGKTAYND
GDYYHTVLWM QQALKQHEEG EESSITKAEI LDYLSYAVFQ LGDLHRAMEL TRRLVSLDST
HERAGSNLRY FEKLLEKERM ATLLNKTSTR TEPVMQGGVY ERPPDYLPER EIYEGLCRGE
GVKMTPRRQK RLFCRYHDGN RNPHLLIAPF KEEDEWDSPH IVRYYDVMSD EEIEKIKELA
KPRLARATVR DPKTGVLTVA SYRVSKSSWL EEYDDPIVAK VNHRMQHITG LTVKTAELLQ
VANYGLGGQY EPHFDFSRKD EPDAFKRLGT GNRVATFLNY MSDVEAGGAT VFPDFGAAIW
PKKGTAVFWY NLFRSGEGDY RTRHAACPVL VGCKWVSNKW FHERGNEFLR PCGRTEVD
//