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Q9R1J8

- P3H1_RAT

UniProt

Q9R1J8 - P3H1_RAT

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Protein

Prolyl 3-hydroxylase 1

Gene

Lepre1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts (By similarity).By similarity

Catalytic activityi

L-proline-[procollagen] + 2-oxoglutarate + O2 = trans-3-hydroxy-L-proline-[procollagen] + succinate + CO2.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi579 – 5791Iron
Metal bindingi581 – 5811Iron
Metal bindingi651 – 6511Iron
Active sitei661 – 6611By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. L-ascorbic acid binding Source: UniProtKB-KW
  3. procollagen-proline 3-dioxygenase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl 3-hydroxylase 1 (EC:1.14.11.7)
Alternative name(s):
Leucine- and proline-enriched proteoglycan 1
Short name:
Leprecan-1
Gene namesi
Name:Lepre1
Synonyms:P3h1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi628823. Lepre1.

Subcellular locationi

Endoplasmic reticulum 1 PublicationPROSITE-ProRule annotation. Secretedextracellular spaceextracellular matrix 1 Publication
Note: Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG).

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. endoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Sequence AnalysisAdd
BLAST
Chaini15 – 728714Prolyl 3-hydroxylase 1PRO_0000240354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

O-glycosylated; chondroitin sulfate.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9R1J8.
PRIDEiQ9R1J8.

Expressioni

Tissue specificityi

Expressed in basement membranes of cardiac muscle, skeletal muscle, central nervous system, intestinal tract, trachea, ear, skin, liver and kidney. In kidney, localizes to the glomerular basement membrane, mesangial matrix and Bowman's capsule of the nephron. In the renal parenchyma, expressed in the basement membranes of tubules and blood vessels. In the ear and trachea, localizes to the perimeter of resident chondrocytes in lacunae.1 Publication

Gene expression databases

GenevestigatoriQ9R1J8.

Interactioni

Protein-protein interaction databases

IntActiQ9R1J8. 1 interaction.
MINTiMINT-1775508.

Structurei

3D structure databases

ProteinModelPortaliQ9R1J8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati25 – 5834TPR 1Add
BLAST
Repeati135 – 16834TPR 2Add
BLAST
Repeati197 – 23034TPR 3Add
BLAST
Repeati293 – 32634TPR 4Add
BLAST
Domaini556 – 670115Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili393 – 43139Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi725 – 7284Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the leprecan family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
Contains 4 TPR repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, Signal, TPR repeat

Phylogenomic databases

eggNOGiNOG269251.
HOGENOMiHOG000231087.
HOVERGENiHBG053224.
InParanoidiQ9R1J8.
KOiK08134.
PhylomeDBiQ9R1J8.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51471. FE2OG_OXY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R1J8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVAVAAAAAS RATAESEPEW NVAAPDLLYA EGTAAYARGD WPGVVLNMER
60 70 80 90 100
ALRSRAALRA LRLRCRTRCA TELPWAPDLD LGPASSLNHD PGAAALHDLR
110 120 130 140 150
FFGALLRRAA CLRRCLGPPS AHLLSEELDL EFNKRSPYNY LQVAYFKINK
160 170 180 190 200
LEKAVAAAHT FFVGNPEHME MRQNLDYYQT MSGVKEEDFK DLEAKPHMHE
210 220 230 240 250
FRLGVRLYSE EKPLEAVPHL EAALQEYFVA DEECRALCEG PYDYDGYNYL
260 270 280 290 300
DYSADLFQAI TDHYVQVLSC KQNCVTELAS HPSREKPFED FLPSHYNYLQ
310 320 330 340 350
FAYYNIGNYT QAIECAKTYL LFFPNDEVMS QNLAYYTAVL GEEEASSISP
360 370 380 390 400
RENAQEYRHR SLLEKELLFF AYDIFGIPFV DPDSWTPEEV IPKRLQEKQK
410 420 430 440 450
SERETAVRIS QEIGNLMKEI ETLVEEKTKE SLDVSRLTRE GGPLLYEGIN
460 470 480 490 500
LTMNSKVLNG SQRVVMDGVI SDDECQELQR LTNAAATSGD GYRGQTSPHT
510 520 530 540 550
PNEKFYGVTV LKALKLGQEG KVPLQSAHMY YNVTEKVRRV MESYFRLDTP
560 570 580 590 600
LYFSYSHLVC RTAIEESQAE RKDSSHPVHV DNCILNAESL VCIKEPPAYT
610 620 630 640 650
FRDYSAILYL NGDFDGGNFY FTELDAKTVT AEVQPQCGRA VGFSSGTENP
660 670 680 690 700
HGVKAVTRGQ RCAIALWFTL DPRHSERDRV QADDLVKMLF SPEEVDLPQE
710 720
QPLPDQQGSP KPGEESLSDR ESQPKDEL
Length:728
Mass (Da):82,390
Last modified:May 1, 2000 - v1
Checksum:i06AFE6972BF3EE1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087433 mRNA. Translation: AAD51875.1.
RefSeqiNP_446119.1. NM_053667.1.
UniGeneiRn.13741.

Genome annotation databases

GeneIDi114200.
KEGGirno:114200.
UCSCiRGD:628823. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087433 mRNA. Translation: AAD51875.1 .
RefSeqi NP_446119.1. NM_053667.1.
UniGenei Rn.13741.

3D structure databases

ProteinModelPortali Q9R1J8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9R1J8. 1 interaction.
MINTi MINT-1775508.

Proteomic databases

PaxDbi Q9R1J8.
PRIDEi Q9R1J8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 114200.
KEGGi rno:114200.
UCSCi RGD:628823. rat.

Organism-specific databases

CTDi 64175.
RGDi 628823. Lepre1.

Phylogenomic databases

eggNOGi NOG269251.
HOGENOMi HOG000231087.
HOVERGENi HBG053224.
InParanoidi Q9R1J8.
KOi K08134.
PhylomeDBi Q9R1J8.

Miscellaneous databases

NextBioi 618365.
PROi Q9R1J8.

Gene expression databases

Genevestigatori Q9R1J8.

Family and domain databases

Gene3Di 1.25.40.10. 3 hits.
InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR011990. TPR-like_helical_dom.
[Graphical view ]
Pfami PF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view ]
SMARTi SM00702. P4Hc. 1 hit.
[Graphical view ]
PROSITEi PS00014. ER_TARGET. 1 hit.
PS51471. FE2OG_OXY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular characterization of a novel basement membrane-associated proteoglycan, leprecan."
    Wassenhove-McCarthy D.J., McCarthy K.J.
    J. Biol. Chem. 274:25004-25017(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Fibroblast.

Entry informationi

Entry nameiP3H1_RAT
AccessioniPrimary (citable) accession number: Q9R1J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3