ID H2LKD8_ORYLA Unreviewed; 545 AA.
AC H2LKD8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
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};
GN Name=p4ha1b {ECO:0000313|Ensembl:ENSORLP00000006489.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000006489.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000006489.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000006489.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000006489.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000006489.2};
RG Ensembl;
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 AlphaFoldDB; H2LKD8; -.
DR Ensembl; ENSORLT00000006490.2; ENSORLP00000006489.2; ENSORLG00000005147.2.
DR eggNOG; KOG1591; Eukaryota.
DR GeneTree; ENSGT00940000156635; -.
DR HOGENOM; CLU_024155_1_1_1; -.
DR TreeFam; TF313393; -.
DR Proteomes; UP000001038; Chromosome 15.
DR Bgee; ENSORLG00000005147; Expressed in heart and 15 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 Reference proteome {ECO:0000313|Proteomes:UP000001038};
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..545
FT /note="Prolyl 4-hydroxylase subunit alpha-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017281762"
FT REPEAT 207..240
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 422..530
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 259..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 62848 MW; AF988471D59B482C CRC64;
MELPCWCLLL LSCLESLSAN NDFFTSIGQM TDLLYTEKDL VTSLKDYIRA EENKLEQVKR
WADRLDSLTS TATQDPEGFL GHPVNAFKLM KRLNTEWGNL ESLVLSDTTD GFISNLTIQR
QYFPTEEDQT GAAKALLRLQ DTYNLDANTI STGDLPGVKH KNRMTVEDCY ELGKVAYAEA
DYYHTELWMA QALRQLEEGE ESPLDKVTVL DYLSYAIYQQ GDLKRALEYT KKLLQLDPEH
QRANGNQKYF EFQLEKQEKQ DETAEKETQQ QDREKRDTTQ KKKKKQSQKS LSLIPERKKY
EMLCRGEGVR MTSRRQSRLF CRYYDNKHNP RFVLAPVKQQ DEWDRPYIVR YIDIISEAEM
DKIKQLAKPR LRRATVHDPQ TGKLTTAHYR VSKSAWLTAY EDPVVEKINQ RIEDLTGLEM
DTAEELQVAN YGVGGQYEPH FDFGRKDEPD AFKELGTGNR IATWLFYMSD VSAGGATVFP
DVGASVGPQK GTAVFWYNLF ASGEGDYSTR HAACPVLVGN KWVSNKWIHE RGQEWRRPCG
LSENE
//
