ID A0A3P8Q999_ASTCA Unreviewed; 538 AA.
AC A0A3P8Q999;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha-1 {ECO:0000256|ARBA:ARBA00040709};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
DE AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1 {ECO:0000256|ARBA:ARBA00042979};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000025956.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000025956.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000025956.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3P8Q999; -.
DR STRING; 8154.ENSACLP00000025956; -.
DR Ensembl; ENSACLT00000026572.1; ENSACLP00000025956.1; ENSACLG00000017635.1.
DR GeneTree; ENSGT00940000166406; -.
DR Proteomes; UP000265100; Chromosome 8.
DR Bgee; ENSACLG00000017635; Expressed in camera-type eye and 8 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 InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF101; PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1; 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.
DR PROSITE; PS50005; TPR; 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 Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..538
FT /note="Prolyl 4-hydroxylase subunit alpha-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018283419"
FT REPEAT 211..244
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 415..523
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 538 AA; 61857 MW; 6D0576776F4F8409 CRC64;
MALCGWWLIH FLIFTSCSAH DFFTSIGHMT DLLFTEKDLV TSLKDYIRAE ESKLEQIKKW
ADKLDVLSAA ATQDPEGFLG HPVNAFKLMK RLNTEWGELE SLVLTDVSDV FISNLTIQRQ
YFPNDDDQTG AAKALMRLQD TYQLDTNAIS TGELPGSSST SSAWSTLTVD DCYDLGKVVY
SEADYYHTEL WMAQALRQLD QGETSRAVDA VTVLDYLSYS VYQQGELERA LEFTRRLLDL
DPTHQRANGN LKYFEYQLAK QKKVEKVEEK EEESKVRQRR ESKDDYLPER KKYEQLCRGQ
GIKLTPRRQS RLFCRYYDNN RHPRYVIGPV QQEDEWDSPH IVRYHNIVSE KDMEKVKELA
KPRLRRATIS NPVTGVLETA HYRISKSAWL GAYEHPVVDK INQLIEDVTG LNVKTAEDLQ
VANYGLGGQY EPHFDFGRKD EPDAFEELGT GNRIATWLLY MTDVQAGGAT VFTDIGAAVK
PKKGTAVFWY NLYPSGEGDY RTRHAACPVL LGNKWVSNKW IHERGQEFRR RCSLNETD
//
