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Database: UniProt
Entry: A0A2K5WMZ3_MACFA
LinkDB: A0A2K5WMZ3_MACFA
Original site: A0A2K5WMZ3_MACFA 
ID   A0A2K5WMZ3_MACFA        Unreviewed;       705 AA.
AC   A0A2K5WMZ3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=procollagen-lysine 5-dioxygenase {ECO:0000256|ARBA:ARBA00012264};
DE            EC=1.14.11.4 {ECO:0000256|ARBA:ARBA00012264};
GN   Name=PLOD2 {ECO:0000313|Ensembl:ENSMFAP00000038390.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000038390.1, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000038390.1, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000038390.1}
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}.
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DR   RefSeq; XP_005546072.1; XM_005546015.2.
DR   AlphaFoldDB; A0A2K5WMZ3; -.
DR   Ensembl; ENSMFAT00000012645.2; ENSMFAP00000038390.1; ENSMFAG00000038516.2.
DR   GeneID; 101866274; -.
DR   CTD; 5352; -.
DR   VEuPathDB; HostDB:ENSMFAG00000038516; -.
DR   GeneTree; ENSGT01030000234558; -.
DR   OrthoDB; 5386101at2759; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   Bgee; ENSMFAG00000038516; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
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:SF6; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE 2; 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   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:UP000233100};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          612..705
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   705 AA;  81427 MW;  D81C8DE43A0B86A0 CRC64;
     MATSDFVLMK RREKVLGQGE EWRGGDGINS IGGGQKVRLM KEVMEHYADQ DDLVVMFTEC
     FDVIFAGGPE EVLKKFQKAN HKVVFAADGI LWPDKRLADK YPVVHIGKRY LNSGGFIGYA
     PYINRIVQQW NLQDNDDDQL FYTKIYIDPL KREAINITLD HKCKIFQTLN GAVDEVVLKF
     ENGKARAKNT FYETLPVAIN GNGPTKILLN YFGNYVPNSW TQGNGCTLCE FDTIDLSAVD
     VHPNVTIGVF IEQPTPFLPR FLDILLTLDY PKEALKLFIH NKEVYHEKDI KVFFDKAKHE
     IKTIKIVGPE ENLSQAEARN MGMDFCRQDE KCDYYFSVDA DVVLTNPRTL KILIEQNRKI
     IAPLVTRHGK LWSNFWGALS PDGYYARSED YVDIVQGNRV GVWNVPYMAN VYLIKGKTLR
     LEMNERNYFV RDKLDPDMAL CRNAREMTLQ REKDSPTPET FQMLSPPKGV FMYISNRHEF
     GRLLSTANYN TSHYNNDLWQ IFENPVDWKE KYINRDYSKI FTENIVEQPC PDVFWFPIFS
     EKACDELVEE MEHYGKWSGG KHHDSRISGG YENVPTDDIH MKQVDLENVW LHFIREFIAP
     VTLKVFAGYY TKGFALLNFV VKYSPERQRS LRPHHDASTF TINIALNNVG EDFQGGGCKF
     LRYNCSIESP RKGWSFMHPG RLTHLHEGLP VKNGTRYIAV SFIDP
//
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