CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016836
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prolyl 3-hydroxylase 2 
Protein Synonyms/Alias
 Leprecan-like protein 1 
Gene Name
 Leprel1 
Gene Synonyms/Alias
 P3h2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
532LFYDISEKARKIVESubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Shows prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types II, IV and V (By similarity). 
Sequence Annotation
 REPEAT 42 75 TPR 1.
 REPEAT 144 177 TPR 2.
 REPEAT 205 238 TPR 3.
 REPEAT 301 334 TPR 4.
 DOMAIN 552 666 Fe2OG dioxygenase.
 MOTIF 700 703 Prevents secretion from ER (Potential).
 ACT_SITE 657 657 By similarity.
 METAL 575 575 Iron.
 METAL 577 577 Iron.
 METAL 647 647 Iron.
 CARBOHYD 444 444 N-linked (GlcNAc...) (Potential).
 CARBOHYD 544 544 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Iron; Metal-binding; Oxidoreductase; Reference proteome; Repeat; Signal; TPR repeat; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 703 AA 
Protein Sequence
MRESTWVSLL LLLLLPTPQR GGPQDGRRSP EPEPERGPLQ PFDLLYASGV AAYYSGDYER 60
AVRDLEAALS SHRRLRDIRT RCARHCAARR PLAPPGAGPG AELPFFRAVL ERARCSRSCQ 120
SQRLGGPASR HRVSEDVRSD FQRRVPYNYL QRAYIKLNQL EKAMEAAHTF FMANPEHMEM 180
QQDLEDYKAT ARVEAPLLDR EAKPHLESYN AGVKHYEADD FESAIKYFEQ ALREYFNEDM 240
ECRALCEGPQ RFEEYEYLGY KGGLYEAIAD HYMQVLVCQH ECVRELATRP GRLSPIENFL 300
PLHYDYLQFA YYRVGEYVKA LECAKAYLMF HPDNEDVLDN VDFYESLLDD STDPASIEAR 360
EDLTAFVKRH KLEAELIKLA AEGLGFSYAE PNYWISYGGR QDENRVPSGV NMDGAEVHGL 420
SMGKKSPPKI GRDLREGGPL LYENITFVYN SEQLNGTQRV LLDNVLSQEQ CRELHSVANG 480
IMLVGDGYRG KTSPHTPNEK FEGATVLKAL KFGYEGRVPL KSARLFYDIS EKARKIVESY 540
FMLNSTLYFS YTHMVCRTAL SGQQDRRNDL SHPIHADNCL LDPEANECWK EPPAYTFRDY 600
SALLYMNDDF DGGEFIFTEM DAKTVTASIK PKCGRMISFS SGGENPHGVK AVTRGQRCAV 660
ALWFTLDPLY RELERIQADE VIAILDQEQR GKHGLNINPK DEL 703 
Gene Ontology
 GO:0005604; C:basement membrane; IDA:UniProtKB.
 GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
 GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0019797; F:procollagen-proline 3-dioxygenase activity; ISS:UniProtKB.
 GO:0032963; P:collagen metabolic process; ISS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
 GO:0019511; P:peptidyl-proline hydroxylation; ISS:UniProtKB. 
Interpro
 IPR005123; Oxoglu/Fe-dep_dioxygenase.
 IPR006620; Pro_4_hyd_alph.
 IPR011990; TPR-like_helical.
 IPR013105; TPR_2. 
Pfam
 PF13640; 2OG-FeII_Oxy_3
 PF07719; TPR_2 
SMART
 SM00702; P4Hc 
PROSITE
 PS00014; ER_TARGET
 PS51471; FE2OG_OXY
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS