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Q9EQP5

- PRELP_RAT

UniProt

Q9EQP5 - PRELP_RAT

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Protein

Prolargin

Gene

Prelp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

May anchor basement membranes to the underlying connective tissue.By similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. heparin binding Source: RGD

GO - Biological processi

  1. cell aging Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196475. Keratan sulfate biosynthesis.
REACT_198617. Keratan sulfate degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolargin
Alternative name(s):
Proline-arginine-rich end leucine-rich repeat protein
Gene namesi
Name:Prelp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 13

Organism-specific databases

RGDi620226. Prelp.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 377356ProlarginPRO_0000032746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi327 ↔ 368By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9EQP5.
PRIDEiQ9EQP5.

Expressioni

Gene expression databases

GenevestigatoriQ9EQP5.

Interactioni

Subunit structurei

Binds the basement membrane heparan sulfate proteoglycan perlecan and triple helical collagens type I and type II.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004241.

Structurei

3D structure databases

ProteinModelPortaliQ9EQP5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati90 – 10920LRR 1Add
BLAST
Repeati110 – 13324LRR 2Add
BLAST
Repeati134 – 15724LRR 3Add
BLAST
Repeati158 – 17821LRR 4Add
BLAST
Repeati179 – 20224LRR 5Add
BLAST
Repeati203 – 22826LRR 6Add
BLAST
Repeati229 – 24921LRR 7Add
BLAST
Repeati250 – 27324LRR 8Add
BLAST
Repeati274 – 29825LRR 9Add
BLAST
Repeati299 – 31820LRR 10Add
BLAST
Repeati319 – 35739LRR 11Add
BLAST
Repeati358 – 37720LRR 12Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 8417Cys-richAdd
BLAST
Compositional biasi192 – 1976Poly-Leu

Domaini

The basic N-terminal Arg/Pro-rich region binds heparin and heparan sulfate. Binds collagens type I and type II through its leucine-rich repeat domain (By similarity).By similarity

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiQ9EQP5.
KOiK08125.
OMAiDTFQGLK.
OrthoDBiEOG741Z2B.
PhylomeDBiQ9EQP5.
TreeFamiTF334562.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR027216. Prolargin.
[Graphical view]
PANTHERiPTHR24371:SF15. PTHR24371:SF15. 1 hit.
PfamiPF00560. LRR_1. 3 hits.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 10 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9EQP5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRASFFWFLP LLLILASVAQ GQPRPKPGIR RKPKPRPTPS FPQPHEPAEP
60 70 80 90 100
TDLPPPLPPG PPSVFPDCPR ECYCPPDFPS ALYCDSRNLR KVPIIPPRIH
110 120 130 140 150
YLYLQNNFIT ELPVESFKNA TGLRWINLDN NRIRKVDQRV LEKLPGLAFL
160 170 180 190 200
YMDKNQLEEV PSALPRNLEQ LRLSQNLISR IPPGVFSKLE NLLLLDLQHN
210 220 230 240 250
RLSDGVFKAD TFQGLKNLMQ LNLAHNILRR MPPKVPPAIH QLYLDSNKIE
260 270 280 290 300
TIPSGYFKDF PNLAFIRMNY NKLSDRGLPK NSFNISNLLV LHLSHNKISN
310 320 330 340 350
VPAISNKLEH LYLNNNSIEK INGTQICPSN LVAFHDFSSD LENVPHLRYL
360 370
RLDGNFLKPP IPLDLMMCFR LLQSVVI
Length:377
Mass (Da):43,179
Last modified:March 1, 2001 - v1
Checksum:i79CBE62534753C46
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF163569 mRNA. Translation: AAG23724.1.
BC072487 mRNA. Translation: AAH72487.1.
RefSeqiNP_445837.1. NM_053385.1.
XP_006249953.1. XM_006249891.2.
UniGeneiRn.112602.

Genome annotation databases

EnsembliENSRNOT00000004241; ENSRNOP00000004241; ENSRNOG00000003120.
GeneIDi84400.
KEGGirno:84400.
UCSCiRGD:620226. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF163569 mRNA. Translation: AAG23724.1 .
BC072487 mRNA. Translation: AAH72487.1 .
RefSeqi NP_445837.1. NM_053385.1.
XP_006249953.1. XM_006249891.2.
UniGenei Rn.112602.

3D structure databases

ProteinModelPortali Q9EQP5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000004241.

Proteomic databases

PaxDbi Q9EQP5.
PRIDEi Q9EQP5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000004241 ; ENSRNOP00000004241 ; ENSRNOG00000003120 .
GeneIDi 84400.
KEGGi rno:84400.
UCSCi RGD:620226. rat.

Organism-specific databases

CTDi 5549.
RGDi 620226. Prelp.

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00760000118969.
HOGENOMi HOG000234447.
HOVERGENi HBG108061.
InParanoidi Q9EQP5.
KOi K08125.
OMAi DTFQGLK.
OrthoDBi EOG741Z2B.
PhylomeDBi Q9EQP5.
TreeFami TF334562.

Enzyme and pathway databases

Reactomei REACT_196475. Keratan sulfate biosynthesis.
REACT_198617. Keratan sulfate degradation.

Miscellaneous databases

NextBioi 616827.
PROi Q9EQP5.

Gene expression databases

Genevestigatori Q9EQP5.

Family and domain databases

InterProi IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR027216. Prolargin.
[Graphical view ]
PANTHERi PTHR24371:SF15. PTHR24371:SF15. 1 hit.
Pfami PF00560. LRR_1. 3 hits.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view ]
SMARTi SM00013. LRRNT. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 10 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The amino-terminal part of PRELP binds to heparin and heparan sulfate."
    Bengtsson E., Aspberg A., Heinegaard D., Sommarin Y., Spillmann D.
    J. Biol. Chem. 275:40695-40702(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Chondrosarcoma.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiPRELP_RAT
AccessioniPrimary (citable) accession number: Q9EQP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 97 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