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UniProtKB/Swiss-Prot entry O60568


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PLOD3_HUMAN
Primary accession number O60568
Secondary accession number Q540C3
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 75)
Name and origin of the protein
Protein name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 [Precursor]
Synonyms EC 1.14.11.4
Lysyl hydroxylase 3
LH3
Gene name
Name: PLOD3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.273.21.12881; PubMed=9582318 [NCBI, ExPASy, EBI, Israel, Japan]
Valtavaara M., Szpirer C., Szpirer J., Myllylae R.;
"Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3).";
J. Biol. Chem. 273:12881-12886(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.95.18.10482; PubMed=9724729 [NCBI, ExPASy, EBI, Israel, Japan]
Passoja K., Rautavuoma K., Ala-Kokko L., Kosonen T., Kivirikko K.I.;
"Cloning and characterization of a third human lysyl hydroxylase isoform.";
Proc. Natl. Acad. Sci. U.S.A. 95:10482-10486(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0945-053X(99)00058-X; PubMed=10686427 [NCBI, ExPASy, EBI, Israel, Japan]
Rautavuoma K., Passoja K., Helaakoski T., Kivirikko K.I.;
"Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3).";
Matrix Biol. 19:73-79(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Lian Z., Feitelson M.;
"A gene upregulated by HBVX and is similar to LH3.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF046889; AAC39753.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF068229; AAC34808.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF207069; AAF63701.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY220458; AAO61775.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004876; AAD45831.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011674; AAH11674.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001075.1; -.
UniGene Hs.153357
3D structure databases
ModBase O60568.
Protein-protein interaction databases
IntAct O60568; 6.
Organism-specific databases
GeneCards GC07M100635; -.
H-InvDB HIX0006947; -.
HGNC HGNC:9083; PLOD3.
GenAtlas PLOD3.
HPA HPA001236; -.
MIM 603066; gene. [NCBI / EBI]
PharmGKB PA33413; -.
GeneCards O60568.
Gene expression databases
ArrayExpress O60568; -.
CleanEx HS_PLOD3; -.
GermOnline ENSG00000106397; Homo sapiens.
Ontologies
GO
GO:0030867; Cellular component: rough endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0031418; Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702; Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0008475; Molecular function: procollagen-lysine 5-dioxygenase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006464; Biological process: protein modification process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR005123; 2OG-FeII_Oase.
IPR006620; Pro_4_hyd_alph.
IPR001006; Procol_lys_dOase.
Graphical view of domain structure.
Pfam PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.
ProDom PD011578; ProcolLys_dioxy; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00702; P4Hc; 1.
SMART graphical view of domain structure.
PROSITE PS01325; LYS_HYDROXYLASE; 1.
Proteomic databases
PeptideAtlas O60568; -.
Proteomics databases
PRIDE O60568; -.
Genome annotation databases
Ensembl ENSG00000106397; Homo sapiens. [Contig view]
GeneID 8985; -.
KEGG hsa:8985; -.
Phylogenomic databases
HOGENOM O60568; -.
HOVERGEN O60568; -.
Other
DrugBank DB00139; Succinic acid.
DB00126; Vitamin C.
NextBio 33693; -.
SOURCE PLOD3; Homo sapiens.
ProtoNet O60568.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase; Polymorphism; Signal; Vitamin C.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    24  24     Potential. 
CHAIN   25   738  714     Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3. PRO_0000024686
DOMAIN   565   738  174     PKHD. 
ACT_SITE   729   729        Potential. 
METAL   667   667        Iron (By similarity). 
METAL   669   669        Iron (By similarity). 
METAL   719   719        Iron (By similarity). 
CARBOHYD   63    63        N-linked (GlcNAc...) (Potential). 
CARBOHYD   548   548        N-linked (GlcNAc...) (Potential). 
VARIANT   151   151  1     A -> V (in dbSNP:rs35627324 [NCBI]). VAR_051708 
VARIANT   286   286  1     R -> W (in dbSNP:rs1134907 [NCBI]). VAR_012075 
Sequence information
Length: 738 AA [This is the length of the unprocessed precursor] Molecular weight: 84785 Da [This is the MW of the unprocessed precursor] CRC64: 08424B46985941F9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTSSGPGPRF LLLLPLLLPP AASASDRPRG RDPVNPEKLL VITVATAETE GYLRFLRSAE 

        70         80         90        100        110        120 
FFNYTVRTLG LGEEWRGGDV ARTVGGGQKV RWLKKEMEKY ADREDMIIMF VDSYDVILAG 

       130        140        150        160        170        180 
SPTELLKKFV QSGSRLLFSA ESFCWPEWGL AEQYPEVGTG KRFLNSGGFI GFATTIHQIV 

       190        200        210        220        230        240 
RQWKYKDDDD DQLFYTRLYL DPGLREKLSL NLDHKSRIFQ NLNGALDEVV LKFDRNRVRI 

       250        260        270        280        290        300 
RNVAYDTLPI VVHGNGPTKL QLNYLGNYVP NGWTPEGGCG FCNQDRRTLP GGQPPPRVFL 

       310        320        330        340        350        360 
AVFVEQPTPF LPRFLQRLLL LDYPPDRVTL FLHNNEVFHE PHIADSWPQL QDHFSAVKLV 

       370        380        390        400        410        420 
GPEEALSPGE ARDMAMDLCR QDPECEFYFS LDADAVLTNL QTLRILIEEN RKVIAPMLSR 

       430        440        450        460        470        480 
HGKLWSNFWG ALSPDEYYAR SEDYVELVQR KRVGVWNVPY ISQAYVIRGD TLRMELPQRD 

       490        500        510        520        530        540 
VFSGSDTDPD MAFCKSFRDK GIFLHLSNQH EFGRLLATSR YDTEHLHPDL WQIFDNPVDW 

       550        560        570        580        590        600 
KEQYIHENYS RALEGEGIVE QPCPDVYWFP LLSEQMCDEL VAEMEHYGQW SGGRHEDSRL 

       610        620        630        640        650        660 
AGGYENVPTV DIHMKQVGYE DQWLQLLRTY VGPMTESLFP GYHTKARAVM NFVVRYRPDE 

       670        680        690        700        710        720 
QPSLRPHHDS STFTLNVALN HKGLDYEGGG CRFLRYDCVI SSPRKGWALL HPGRLTHYHE 

       730 
GLPTTWGTRY IMVSFVDP 

O60568 in FASTA format

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