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Database: UniProt
Entry: A0A3Q4BE91_MOLML
LinkDB: A0A3Q4BE91_MOLML
Original site: A0A3Q4BE91_MOLML 
ID   A0A3Q4BE91_MOLML        Unreviewed;       702 AA.
AC   A0A3Q4BE91;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 {ECO:0000256|ARBA:ARBA00040791};
DE            EC=1.14.11.4 {ECO:0000256|ARBA:ARBA00012264};
DE   AltName: Full=Lysyl hydroxylase 1 {ECO:0000256|ARBA:ARBA00042560};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000017305.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000017305.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC         lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC         COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00024166};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004367}; Lumenal side
CC       {ECO:0000256|ARBA:ARBA00004367}. Rough endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00037819}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00037819}; Lumenal side
CC       {ECO:0000256|ARBA:ARBA00037819}.
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DR   AlphaFoldDB; A0A3Q4BE91; -.
DR   STRING; 94237.ENSMMOP00000017305; -.
DR   Ensembl; ENSMMOT00000017593.1; ENSMMOP00000017305.1; ENSMMOG00000013171.1.
DR   OMA; CTYYFSM; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR001006; Procol_lys_dOase.
DR   PANTHER; PTHR10730:SF5; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE 1; 1.
DR   PANTHER; PTHR10730; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE/GLYCOSYLTRANSFERASE 25 FAMILY MEMBER; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE   4: Predicted;
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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          611..702
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   702 AA;  81433 MW;  A0FA9AA2578A7C05 CRC64;
     MLCLLEKLIV VTVATKETDG FKRFLRSAKH FNYTVLGRGQ KWKGGDYMGA PGGGQKVRLL
     KEALEEKEIQ DKIILFIDSY DVVFASGPKE LFKKFQQARH KVVFSSESLI WPDRHLEDKH
     PHVREGNRFL GSGGFIGYAA NVKEMVAEWT GEDNESDQLF FTKIYIDPAK RKSINITLDS
     KCRLFQNLHG SLDEVVLKFE DGRSRARNLL YNTLPSIIHG NGPTKLQINY LGNYIPNTWA
     FETGCMVCHK ELRPLTTLKS EYPLVVIGIF IQQPTPFVTV FFERLLKLQY PKNRLKLFIY
     NQEVHHERHV SSFLRDHGRL YQDVKFIGPE EEMDAAASRN MGFDMCRKDK DCEYFFSVDI
     EVVLKNENTL KILLEQNLPV VAPMITRAGR LWSNFWGALS EDGYYARSED YVDIVQGRRV
     GVWNVPYVSS VYLMKASLLR SELTDYELFN SHSLDPDMAY CHNVRSKGIF MYVTNMHTFG
     RILSTENYQT SHLHNDLWQI FVNPLDWQER YIHENYTRIT KDKLIETPCP DVYWFPIFSE
     VACNHIVEEM EHFGRWSGGN DTRIQGGYEN VPTIDIHMNQ VNFEKEWHKF LLEYVAPITE
     KMYPGYYTKA QFDLAFVVRY KPDEQPSLRP HHDASTFTIN IALNQVGPDY QGGGCRFLRY
     DCSIQAPRKG WALMHPGRLT HYHEGLPTTA GVRYIAVSFV DP
//
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