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Q9EQP5 (PRELP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolargin
Alternative name(s):
Proline-arginine-rich end leucine-rich repeat protein
Gene names
Name:Prelp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Secretedextracellular spaceextracellular matrix.

Domain

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.

Sequence similarities

Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily.

Contains 12 LRR (leucine-rich) repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 377356Prolargin
PRO_0000032746

Regions

Repeat90 – 10920LRR 1
Repeat110 – 13324LRR 2
Repeat134 – 15724LRR 3
Repeat158 – 17821LRR 4
Repeat179 – 20224LRR 5
Repeat203 – 22826LRR 6
Repeat229 – 24921LRR 7
Repeat250 – 27324LRR 8
Repeat274 – 29825LRR 9
Repeat299 – 31820LRR 10
Repeat319 – 35739LRR 11
Repeat358 – 37720LRR 12
Compositional bias68 – 8417Cys-rich
Compositional bias192 – 1976Poly-Leu

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation2841N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Disulfide bond327 ↔ 368 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9EQP5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 79CBE62534753C46

FASTA37743,179
        10         20         30         40         50         60 
MRASFFWFLP LLLILASVAQ GQPRPKPGIR RKPKPRPTPS FPQPHEPAEP TDLPPPLPPG 

        70         80         90        100        110        120 
PPSVFPDCPR ECYCPPDFPS ALYCDSRNLR KVPIIPPRIH YLYLQNNFIT ELPVESFKNA 

       130        140        150        160        170        180 
TGLRWINLDN NRIRKVDQRV LEKLPGLAFL YMDKNQLEEV PSALPRNLEQ LRLSQNLISR 

       190        200        210        220        230        240 
IPPGVFSKLE NLLLLDLQHN RLSDGVFKAD TFQGLKNLMQ LNLAHNILRR MPPKVPPAIH 

       250        260        270        280        290        300 
QLYLDSNKIE TIPSGYFKDF PNLAFIRMNY NKLSDRGLPK NSFNISNLLV LHLSHNKISN 

       310        320        330        340        350        360 
VPAISNKLEH LYLNNNSIEK INGTQICPSN LVAFHDFSSD LENVPHLRYL RLDGNFLKPP 

       370 
IPLDLMMCFR LLQSVVI 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF163569 mRNA. Translation: AAG23724.1.
BC072487 mRNA. Translation: AAH72487.1.
RefSeqNP_445837.1. NM_053385.1.
XP_006249953.1. XM_006249891.1.
UniGeneRn.112602.

3D structure databases

ProteinModelPortalQ9EQP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000004241.

Proteomic databases

PaxDbQ9EQP5.
PRIDEQ9EQP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004241; ENSRNOP00000004241; ENSRNOG00000003120.
GeneID84400.
KEGGrno:84400.
UCSCRGD:620226. rat.

Organism-specific databases

CTD5549.
RGD620226. Prelp.

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00600000084286.
HOGENOMHOG000234447.
HOVERGENHBG108061.
InParanoidQ9EQP5.
KOK08125.
OMADTFQGLK.
OrthoDBEOG741Z2B.
PhylomeDBQ9EQP5.
TreeFamTF334562.

Gene expression databases

GenevestigatorQ9EQP5.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
IPR027216. Prolargin.
[Graphical view]
PANTHERPTHR24371:SF15. PTHR24371:SF15. 1 hit.
PfamPF00560. LRR_1. 3 hits.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio616827.
PROQ9EQP5.

Entry information

Entry namePRELP_RAT
AccessionPrimary (citable) accession number: Q9EQP5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families