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P51888 (PRELP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
Synonyms:SLRR2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Tissue specificity

Connective tissue.

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 – 2020 Potential
Chain21 – 382362Prolargin
PRO_0000032744

Regions

Repeat95 – 11420LRR 1
Repeat115 – 13824LRR 2
Repeat139 – 16224LRR 3
Repeat163 – 18321LRR 4
Repeat184 – 20724LRR 5
Repeat208 – 23326LRR 6
Repeat234 – 25421LRR 7
Repeat255 – 27824LRR 8
Repeat279 – 30325LRR 9
Repeat304 – 32320LRR 10
Repeat324 – 36239LRR 11
Repeat363 – 38220LRR 12
Compositional bias73 – 8917Cys-rich
Compositional bias197 – 2026Poly-Leu

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Ref.7
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3271N-linked (GlcNAc...) Ref.7
Disulfide bond332 ↔ 373 By similarity

Natural variations

Natural variant331G → R.
Corresponds to variant rs41313926 [ dbSNP | Ensembl ].
VAR_061804
Natural variant1571M → V.
Corresponds to variant rs2233726 [ dbSNP | Ensembl ].
VAR_052012
Natural variant3341N → S.
Corresponds to variant rs2233732 [ dbSNP | Ensembl ].
VAR_052013
Natural variant3481N → H.
Corresponds to variant rs9439 [ dbSNP | Ensembl ].
VAR_011976

Sequences

Sequence LengthMass (Da)Tools
P51888 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A1C4E166B7515695

FASTA38243,810
        10         20         30         40         50         60 
MRSPLCWLLP LLILASVAQG QPTRRPRPGT GPGRRPRPRP RPTPSFPQPD EPAEPTDLPP 

        70         80         90        100        110        120 
PLPPGPPSIF PDCPRECYCP PDFPSALYCD SRNLRKVPVI PPRIHYLYLQ NNFITELPVE 

       130        140        150        160        170        180 
SFQNATGLRW INLDNNRIRK IDQRVLEKLP GLVFLYMEKN QLEEVPSALP RNLEQLRLSQ 

       190        200        210        220        230        240 
NHISRIPPGV FSKLENLLLL DLQHNRLSDG VFKPDTFHGL KNLMQLNLAH NILRKMPPRV 

       250        260        270        280        290        300 
PTAIHQLYLD SNKIETIPNG YFKSFPNLAF IRLNYNKLTD RGLPKNSFNI SNLLVLHLSH 

       310        320        330        340        350        360 
NRISSVPAIN NRLEHLYLNN NSIEKINGTQ ICPNDLVAFH DFSSDLENVP HLRYLRLDGN 

       370        380 
YLKPPIPLDL MMCFRLLQSV VI 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of a basic leucine-rich repeat protein, PRELP, found in connective tissues."
Bengtsson E., Neame P.J., Heinegaard D., Sommarin Y.
J. Biol. Chem. 270:25639-25644(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The gene organization, chromosome location, and expression of a 55-kDa matrix protein (PRELP) of human articular cartilage."
Grover J., Chen X.-N., Korenberg J.R., Recklies A.D., Roughley P.J.
Genomics 38:109-117(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Pancreas and Spleen.
[7]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124 AND ASN-327.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29089 mRNA. Translation: AAC50230.1.
U41344, U41343 Genomic DNA. Translation: AAC18782.1.
CR542270 mRNA. Translation: CAG47066.1.
AL391817 Genomic DNA. Translation: CAI17033.1.
CH471067 Genomic DNA. Translation: EAW91481.1.
BC032498 mRNA. Translation: AAH32498.1.
CCDSCCDS1438.1.
PIRI39068.
RefSeqNP_002716.1. NM_002725.3.
NP_958505.1. NM_201348.1.
UniGeneHs.632481.

3D structure databases

ProteinModelPortalP51888.
SMRP51888. Positions 56-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111540. 6 interactions.
IntActP51888. 2 interactions.
STRING9606.ENSP00000343924.

PTM databases

PhosphoSiteP51888.

Polymorphism databases

DMDM1709586.

Proteomic databases

PaxDbP51888.
PeptideAtlasP51888.
PRIDEP51888.

Protocols and materials databases

DNASU5549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343110; ENSP00000343924; ENSG00000188783.
GeneID5549.
KEGGhsa:5549.
UCSCuc001gzs.3. human.

Organism-specific databases

CTD5549.
GeneCardsGC01P203444.
HGNCHGNC:9357. PRELP.
HPAHPA062623.
MIM601914. gene.
neXtProtNX_P51888.
PharmGKBPA33729.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000234447.
HOVERGENHBG108061.
InParanoidP51888.
KOK08125.
OMADTFQGLK.
OrthoDBEOG741Z2B.
PhylomeDBP51888.
TreeFamTF334562.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP51888.
BgeeP51888.
CleanExHS_PRELP.
GenevestigatorP51888.

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. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRELP. human.
GeneWikiPRELP.
GenomeRNAi5549.
NextBio21502.
PMAP-CutDBP51888.
PROP51888.
SOURCESearch...

Entry information

Entry namePRELP_HUMAN
AccessionPrimary (citable) accession number: P51888
Secondary accession number(s): Q6FG38
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM