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P51888

- PRELP_HUMAN

UniProt

P51888 - PRELP_HUMAN

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Protein

Prolargin

Gene
PRELP, SLRR2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: ProtInc
  2. heparin binding Source: Ensembl

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cell aging Source: Ensembl
  3. glycosaminoglycan metabolic process Source: Reactome
  4. keratan sulfate biosynthetic process Source: Reactome
  5. keratan sulfate catabolic process Source: Reactome
  6. keratan sulfate metabolic process Source: Reactome
  7. skeletal system development Source: ProtInc
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_121120. Keratan sulfate biosynthesis.
REACT_121313. 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
Synonyms:SLRR2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9357. PRELP.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. Golgi lumen Source: Reactome
  4. lysosomal lumen Source: Reactome
  5. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33729.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed predictionAdd
BLAST
Chaini21 – 382362ProlarginPRO_0000032744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
Glycosylationi289 – 2891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi320 – 3201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi327 – 3271N-linked (GlcNAc...)1 Publication
Disulfide bondi332 ↔ 373 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP51888.
PeptideAtlasiP51888.
PRIDEiP51888.

PTM databases

PhosphoSiteiP51888.

Miscellaneous databases

PMAP-CutDBP51888.

Expressioni

Tissue specificityi

Connective tissue.

Gene expression databases

ArrayExpressiP51888.
BgeeiP51888.
CleanExiHS_PRELP.
GenevestigatoriP51888.

Organism-specific databases

HPAiHPA062623.

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

BioGridi111540. 6 interactions.
IntActiP51888. 2 interactions.
STRINGi9606.ENSP00000343924.

Structurei

3D structure databases

ProteinModelPortaliP51888.
SMRiP51888. Positions 56-362.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati95 – 11420LRR 1Add
BLAST
Repeati115 – 13824LRR 2Add
BLAST
Repeati139 – 16224LRR 3Add
BLAST
Repeati163 – 18321LRR 4Add
BLAST
Repeati184 – 20724LRR 5Add
BLAST
Repeati208 – 23326LRR 6Add
BLAST
Repeati234 – 25421LRR 7Add
BLAST
Repeati255 – 27824LRR 8Add
BLAST
Repeati279 – 30325LRR 9Add
BLAST
Repeati304 – 32320LRR 10Add
BLAST
Repeati324 – 36239LRR 11Add
BLAST
Repeati363 – 38220LRR 12Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi73 – 8917Cys-richAdd
BLAST
Compositional biasi197 – 2026Poly-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.

Sequence similaritiesi

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiCOG4886.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiP51888.
KOiK08125.
OMAiDTFQGLK.
OrthoDBiEOG741Z2B.
PhylomeDBiP51888.
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. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P51888-1 [UniParc]FASTAAdd to Basket

« Hide

MRSPLCWLLP LLILASVAQG QPTRRPRPGT GPGRRPRPRP RPTPSFPQPD    50
EPAEPTDLPP PLPPGPPSIF PDCPRECYCP PDFPSALYCD SRNLRKVPVI 100
PPRIHYLYLQ NNFITELPVE SFQNATGLRW INLDNNRIRK IDQRVLEKLP 150
GLVFLYMEKN QLEEVPSALP RNLEQLRLSQ NHISRIPPGV FSKLENLLLL 200
DLQHNRLSDG VFKPDTFHGL KNLMQLNLAH NILRKMPPRV PTAIHQLYLD 250
SNKIETIPNG YFKSFPNLAF IRLNYNKLTD RGLPKNSFNI SNLLVLHLSH 300
NRISSVPAIN NRLEHLYLNN NSIEKINGTQ ICPNDLVAFH DFSSDLENVP 350
HLRYLRLDGN YLKPPIPLDL MMCFRLLQSV VI 382
Length:382
Mass (Da):43,810
Last modified:October 1, 1996 - v1
Checksum:iA1C4E166B7515695
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331G → R.
Corresponds to variant rs41313926 [ dbSNP | Ensembl ].
VAR_061804
Natural varianti157 – 1571M → V.
Corresponds to variant rs2233726 [ dbSNP | Ensembl ].
VAR_052012
Natural varianti334 – 3341N → S.
Corresponds to variant rs2233732 [ dbSNP | Ensembl ].
VAR_052013
Natural varianti348 – 3481N → H.
Corresponds to variant rs9439 [ dbSNP | Ensembl ].
VAR_011976

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1438.1.
PIRiI39068.
RefSeqiNP_002716.1. NM_002725.3.
NP_958505.1. NM_201348.1.
UniGeneiHs.632481.

Genome annotation databases

EnsembliENST00000343110; ENSP00000343924; ENSG00000188783.
GeneIDi5549.
KEGGihsa:5549.
UCSCiuc001gzs.3. human.

Polymorphism databases

DMDMi1709586.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1438.1.
PIRi I39068.
RefSeqi NP_002716.1. NM_002725.3.
NP_958505.1. NM_201348.1.
UniGenei Hs.632481.

3D structure databases

ProteinModelPortali P51888.
SMRi P51888. Positions 56-362.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111540. 6 interactions.
IntActi P51888. 2 interactions.
STRINGi 9606.ENSP00000343924.

PTM databases

PhosphoSitei P51888.

Polymorphism databases

DMDMi 1709586.

Proteomic databases

PaxDbi P51888.
PeptideAtlasi P51888.
PRIDEi P51888.

Protocols and materials databases

DNASUi 5549.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343110 ; ENSP00000343924 ; ENSG00000188783 .
GeneIDi 5549.
KEGGi hsa:5549.
UCSCi uc001gzs.3. human.

Organism-specific databases

CTDi 5549.
GeneCardsi GC01P203444.
HGNCi HGNC:9357. PRELP.
HPAi HPA062623.
MIMi 601914. gene.
neXtProti NX_P51888.
PharmGKBi PA33729.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000234447.
HOVERGENi HBG108061.
InParanoidi P51888.
KOi K08125.
OMAi DTFQGLK.
OrthoDBi EOG741Z2B.
PhylomeDBi P51888.
TreeFami TF334562.

Enzyme and pathway databases

Reactomei REACT_121120. Keratan sulfate biosynthesis.
REACT_121313. Keratan sulfate degradation.

Miscellaneous databases

ChiTaRSi PRELP. human.
GeneWikii PRELP.
GenomeRNAii 5549.
NextBioi 21502.
PMAP-CutDB P51888.
PROi P51888.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51888.
Bgeei P51888.
CleanExi HS_PRELP.
Genevestigatori P51888.

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. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view ]
SMARTi SM00013. LRRNT. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 11 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPRELP_HUMAN
AccessioniPrimary (citable) accession number: P51888
Secondary accession number(s): Q6FG38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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