UniProt: A0A2I3TVD2

Database: UniProt
Entry: A0A2I3TVD2_PANTR

LinkDB:  A0A2I3TVD2_PANTR 
Original site:  A0A2I3TVD2_PANTR

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
All databases (17)   

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ID   A0A2I3TVD2_PANTR        Unreviewed;       737 AA.
AC   A0A2I3TVD2;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=procollagen-lysine 5-dioxygenase {ECO:0000256|ARBA:ARBA00012264};
DE            EC=1.14.11.4 {ECO:0000256|ARBA:ARBA00012264};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000093194.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000093194.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A2I3TVD2; -.
DR   Ensembl; ENSPTRT00000081878.1; ENSPTRP00000093194.1; ENSPTRG00000051360.1.
DR   GeneTree; ENSGT01030000234558; -.
DR   OMA; ERCKRSA; -.
DR   Proteomes; UP000002277; Unplaced.
DR   Bgee; ENSPTRG00000051360; Expressed in liver and 15 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   CDD; cd23002; GT_LH3; 1.
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:SF7; MULTIFUNCTIONAL PROCOLLAGEN LYSINE HYDROXYLASE AND GLYCOSYLTRANSFERASE LH3; 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:UP000002277};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..737
FT                   /note="procollagen-lysine 5-dioxygenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014134011"
FT   DOMAIN          646..737
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   737 AA;  84517 MW;  B5EDF526B5FABFAB CRC64;
     MTSSGPGPRF LLLLPLLLPP AASASDRPRG RDPVNPEKLL VITVATAETE GYLRFLRSAE
     FFNYTVQTLG LGEEWRGGDV ARTVGGGQKV RWLKKEMEKY ADREDMIIMF VDSYDVILAG
     SPTELLKKFV QSGSRLLFSA ESFCWPEWGL AEQYPEVGTG KRFLNSGGFI GFATTIHQIV
     RQWKYKDDDD DQLFYTRLYL DPGLREKLSL NLDHKSRIFQ NLNGALDEVV LKFDRNRVRI
     RNVAYDTLPI VVHGNGPTKL QLNYLGNYVP NGWTPEGGCG FCNQDRRDSG LGGGGGIPPP
     RVFLPTPFLP RFLQRLLLLD YPPDRVTLFL HNNEVFHEPH IADSWPQLQD HFSAVKLVGP
     EEALSPGEAR DMAMDLCRQD PECEFYFSLD ADTVLTNLQT LRILIEENRW KVIAPMLSRH
     GKLWSNFWGA LSPDEYYARS EDYVELVQRK RVGVWNVPYI SQAYVIRGDT LRMELPQRDV
     FSGSDTDPDM AFCKSFRDKG IFLHLSNQHE FGRLLATSRY DTEHLHPDLW QIFDNPVDWK
     EQYIHENYSR ALEGEGIVEQ PCPDVYWFPL LSEQMCDELV AEMEHYGQWS GGRHEDSRLA
     GGYENVPTVD IHMKQVGYED QWLQLLRTYV GPMTESLFPG YHTKARAVMN FVVRYRPDEQ
     PSLRPHHDSS TFTLNVALNH KGLDYEGGGC RFLRYDCVIS SPRKGWALLH PGRLTHYHEG
     LPTTWGTRYI MVSFVDP
//

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