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Database: UniProt
Entry: A0A2R9A1U4_PANPA
LinkDB: A0A2R9A1U4_PANPA
Original site: A0A2R9A1U4_PANPA 
ID   A0A2R9A1U4_PANPA        Unreviewed;       487 AA.
AC   A0A2R9A1U4;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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|Ensembl:ENSPPAP00000011237.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000011237.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000011237.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000011237.1}
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   -!- 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   EMBL; AJFE02103208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02103209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02103210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9A1U4; -.
DR   Ensembl; ENSPPAT00000033892.1; ENSPPAP00000011237.1; ENSPPAG00000028815.1.
DR   GeneTree; ENSGT00940000157695; -.
DR   Proteomes; UP000240080; Chromosome 5.
DR   Bgee; ENSPPAG00000028815; Expressed in placenta and 6 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: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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000240080};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..487
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015345977"
FT   REPEAT          161..194
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          366..472
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   487 AA;  55512 MW;  8E94EFF369B97430 CRC64;
     MKLWVSALLM AWFGVLSCVQ AEFFTSIGHM TDLIYAEKEL VQSLKEYILV EEAKLSKIKS
     WANKMEALTS KSAADAEGYL AHPVNAYKLV KRLNTDWPAL EDLVLQDSAA GTKYQAMLSV
     DDCFGMGRSA YNEGDYYHTV LWMEQVLKQL DAGEEATTTK SQVLDYLSYA VFQLGDLHRA
     LELTRRLLSL DPSHERAGGN LRYFEQLLEE EREKTLSNQT EAELATPEGI YERPVDYLPE
     RDIYESLCRG EGVKLTPRRQ KRLFCRYHHG NRAPQLLIAP FKEEDEWDSP HIVRYYDVMS
     DEEIERIKEI AKPKLARATV RDPKTGVLTV ASYRVSKSSW LEEDDDPVVA RVNRRMQHIT
     GLTVKTAELL QVANYGVGGQ YEPHFDFSRR PFDSGLKTEG NRLATFLNYM SDVEAGGATV
     FPDLGAAIWP KKGTAVFWYN LLRSGEGDYR TRHAACPVLV GCKWVSNKWF HERGQEFLRP
     CGSTEVD
//
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