ID H2Q230_PANTR Unreviewed; 552 AA.
AC H2Q230;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 75.
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=P4HA1 {ECO:0000313|Ensembl:ENSPTRP00000004547.6,
GN ECO:0000313|VGNC:VGNC:12413};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000004547.6, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000004547.6, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000004547.6}
RP IDENTIFICATION.
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 -!- SUBUNIT: Heterotetramer of two alpha-1 chains and two beta chains
CC (P4HB)(the beta chain is the multi-functional PDI), where P4HB plays
CC the role of a structural subunit; this tetramer catalyzes the formation
CC of 4-hydroxyproline in collagen. {ECO:0000256|ARBA:ARBA00038608}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the P4HA family.
CC {ECO:0000256|ARBA:ARBA00006511}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACZ04041162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04041163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04041164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04041165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2Q230; -.
DR Ensembl; ENSPTRT00000004929.6; ENSPTRP00000004547.6; ENSPTRG00000002619.6.
DR VGNC; VGNC:12413; P4HA1.
DR GeneTree; ENSGT00940000156635; -.
DR HOGENOM; CLU_024155_1_1_1; -.
DR InParanoid; H2Q230; -.
DR Proteomes; UP000002277; Chromosome 10.
DR Bgee; ENSPTRG00000002619; Expressed in lung and 21 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IBA:GO_Central.
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:UP000002277};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..552
FT /note="Prolyl 4-hydroxylase subunit alpha-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014184226"
FT REPEAT 205..238
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 405..527
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 552 AA; 63094 MW; 726B713FBF873AA4 CRC64;
MIWYILIIGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE DKLEQIKKWA
EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LVLKDMSDGF ISNLTIQRQY
FPNDEDQVGA AKALLRLQDT YNLDTDTISK GNLPGVKHKS FLTAEDCFEL GKVAYTEADY
YHTELWMEQA LRQLDEGEIS TIDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR
ANGNLKYFEY IMAKEKDVNK SASDDQSDQK TTPKKKGVAV DYLPERQKYE MLCRGEGIKM
TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRA
ERATVHDPET GKMTTAHAWL SGYENPVVSR INMRIQDLTG LDVSTAEELQ VANYGVGGQY
EPHFDFARKD EPDAFKELGT GNRIATWLFY MSDVSAGGAT VFPEVGASVW PKKGTAVFWY
NLFASGEGDY STRHAACPVL VGNKWGKYFI YSTLYLVRIG MTNRLPFFSY CCTLMCLIYT
FPSLNFQEFT ID
//
