ID A0A3P9CPC2_9CICH Unreviewed; 735 AA.
AC A0A3P9CPC2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=procollagen-proline 3-dioxygenase {ECO:0000256|ARBA:ARBA00012262};
DE EC=1.14.11.7 {ECO:0000256|ARBA:ARBA00012262};
GN Name=P3H3 {ECO:0000313|Ensembl:ENSMZEP00005023879.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005023879.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005023879.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005023879.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the leprecan family.
CC {ECO:0000256|ARBA:ARBA00006487}.
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 AlphaFoldDB; A0A3P9CPC2; -.
DR STRING; 106582.ENSMZEP00005023879; -.
DR Ensembl; ENSMZET00005024663.1; ENSMZEP00005023879.1; ENSMZEG00005017868.1.
DR GeneTree; ENSGT00940000159164; -.
DR OrthoDB; 5398065at2759; -.
DR Proteomes; UP000265160; LG11.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0032963; P:collagen metabolic process; IEA:InterPro.
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; IPR039575; P3H.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14049; LEPRECAN 1; 1.
DR PANTHER; PTHR14049:SF15; PROCOLLAGEN-PROLINE 3-DIOXYGENASE; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 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:UP000265160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..735
FT /note="procollagen-proline 3-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018175228"
FT DOMAIN 559..673
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 688..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 735 AA; 82992 MW; 786E936A1A948CB8 CRC64;
MALQSGRLAV YVAFNCVILA LFSFTSTAWA GGSPNVMSLL QPYDFLYYSG VRAYFSGEWG
KAAELLEKSI VTRESLFGVR RQCYDDCMAA GTEALKKLDS EHGTMWDLWA LDWVQQKAEC
LRFCIGRSVT HVGQLPVSAD IEYEFGTRNP YNFLQVTYYK LEKLQRAASA AHTYFVANPS
HLEMRNNIEK YRRMEGVTEE DFQDRESHNE KHWVLYDAAL QLEANSEWKQ AAEKWKACVN
ETLRQTEECR VQCEVASQRL PEDRGVDSVD GVFEKAAALS LSLLSCRQSC VTQVATRPGR
ISAQEDFLPT QLEHLHIAQF KGGDISGALQ MLRSLLLFYP SDKDSLDNLQ LYHETLGGDT
ESQSTQPAQE IVRYINHSLQ EKKLLYFGME NLDFTFTDPD LWTPEEVVPE SLREIWRAEK
EKINEKMKVG EQQEEVDDSG FFAGGPVPRV GVTITMDDEM LNGTNRVVLD GVMTEKECDR
ILQLASVAGS LGDGYRGRRS PHTPHETFEG LTVLRAVKLA QEGLVNQSDA KLLHELGERV
RTVLHSYFRS PSGLFITFTH LVCRTAVTED QKGRLDLSHP VHVDNCLLEL ETKQCWKEPP
AFTHRDLSAI LYLNDNFDGG ELFFTNRDAK TVTARVKPSC GRLVGFSSGP VNPHGVTAVT
RGRRCALALW FTKEKLYRDR EREEAEAVWA ADGHSVVKTD EEKEGGATSS RDARSQVTKE
KKRERGRVTG GKDEL
//
