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Database: UniProt
Entry: A0A3B1JWW1_ASTMX
LinkDB: A0A3B1JWW1_ASTMX
Original site: A0A3B1JWW1_ASTMX 
ID   A0A3B1JWW1_ASTMX        Unreviewed;       509 AA.
AC   A0A3B1JWW1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE            EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000046763.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000046763.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; A0A3B1JWW1; -.
DR   STRING; 7994.ENSAMXP00000046763; -.
DR   Ensembl; ENSAMXT00000053006.1; ENSAMXP00000046763.1; ENSAMXG00000036173.1.
DR   GeneTree; ENSGT00940000157695; -.
DR   InParanoid; A0A3B1JWW1; -.
DR   OrthoDB; 520341at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000036173; Expressed in olfactory epithelium and 3 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   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10869:SF207; 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   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:UP000018467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..509
FT                   /note="procollagen-proline 4-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017315604"
FT   DOMAIN          389..494
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   509 AA;  56961 MW;  44939563571CB567 CRC64;
     MQVNWIIMLI SLWTFCSGMN EFYSSTDHMT RLISIKQDLS EGIGEYVAVL EKQMFLLRRA
     LLGLDRISNH PSEDPEKFVS NPLTAYKLIS QLRRAGDALE EIIRRNISQD LSAVESKSQV
     LPADADLDGV ALAMIRLQEL YQVDLKTMSG FESSLALDPD ETFHIGQVAQ QNRRFRSAAL
     WLQETLRKLD EDAGSLLTKH QVQQLLDSVS VQTENKPLPL GINQSLLTRD VEALLQMFDA
     DGVSELMEEL ERADLSAVIN QKFSEYQTLC RAAGGTQPTP LRAKKLSCRY TTGGGNPRLI
     YAPAKEEEEW DQPLILRYHN LLSEREMNLI KQLSRPKLDR AKVSDPVSGE KISTMVRVSK
     SAWLSEGESP VVARTNQKIA DITGLDLETA EDLQVANYGI GGQYEPHYDS AVNNDSYFQL
     RGGRIATVLI YLSDVEVGGA TVFPNVGAAL QPEKGSAVVW FNLLKNGSED SRTLHAACPV
     FIGSKWVANK WIHIRGQEFR RRCSLSRSD
//
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