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Protein

Prolargin

Gene

PRELP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • extracellular matrix structural constituent Source: ProtInc
  • heparin binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_121120. Keratan sulfate biosynthesis.
REACT_121313. Keratan sulfate degradation.
REACT_268431. Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
REACT_268786. Defective CHST6 causes MCDC1.

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9357. PRELP.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular vesicle Source: UniProtKB
  • Golgi lumen Source: Reactome
  • lysosomal lumen Source: Reactome
  • proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33729.

Polymorphism and mutation databases

BioMutaiPRELP.
DMDMi1709586.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

BgeeiP51888.
CleanExiHS_PRELP.
GenevisibleiP51888. HS.

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. 13 interactions.
IntActiP51888. 2 interactions.
STRINGi9606.ENSP00000343924.

Structurei

3D structure databases

ProteinModelPortaliP51888.
SMRiP51888. Positions 56-372.
ModBaseiSearch...
MobiDBiSearch...

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).By similarity

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiP51888.
KOiK08125.
OMAiKMPPKVP.
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

        10         20         30         40         50
MRSPLCWLLP LLILASVAQG QPTRRPRPGT GPGRRPRPRP RPTPSFPQPD
60 70 80 90 100
EPAEPTDLPP PLPPGPPSIF PDCPRECYCP PDFPSALYCD SRNLRKVPVI
110 120 130 140 150
PPRIHYLYLQ NNFITELPVE SFQNATGLRW INLDNNRIRK IDQRVLEKLP
160 170 180 190 200
GLVFLYMEKN QLEEVPSALP RNLEQLRLSQ NHISRIPPGV FSKLENLLLL
210 220 230 240 250
DLQHNRLSDG VFKPDTFHGL KNLMQLNLAH NILRKMPPRV PTAIHQLYLD
260 270 280 290 300
SNKIETIPNG YFKSFPNLAF IRLNYNKLTD RGLPKNSFNI SNLLVLHLSH
310 320 330 340 350
NRISSVPAIN NRLEHLYLNN NSIEKINGTQ ICPNDLVAFH DFSSDLENVP
360 370 380
HLRYLRLDGN YLKPPIPLDL MMCFRLLQSV VI
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP51888.
SMRiP51888. Positions 56-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111540. 13 interactions.
IntActiP51888. 2 interactions.
STRINGi9606.ENSP00000343924.

PTM databases

PhosphoSiteiP51888.

Polymorphism and mutation databases

BioMutaiPRELP.
DMDMi1709586.

Proteomic databases

PaxDbiP51888.
PeptideAtlasiP51888.
PRIDEiP51888.

Protocols and materials databases

DNASUi5549.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5549.
GeneCardsiGC01P203444.
HGNCiHGNC:9357. PRELP.
HPAiHPA062623.
MIMi601914. gene.
neXtProtiNX_P51888.
PharmGKBiPA33729.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiP51888.
KOiK08125.
OMAiKMPPKVP.
OrthoDBiEOG741Z2B.
PhylomeDBiP51888.
TreeFamiTF334562.

Enzyme and pathway databases

ReactomeiREACT_121120. Keratan sulfate biosynthesis.
REACT_121313. Keratan sulfate degradation.
REACT_268431. Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
REACT_268786. Defective CHST6 causes MCDC1.

Miscellaneous databases

ChiTaRSiPRELP. human.
GeneWikiiPRELP.
GenomeRNAii5549.
NextBioi21502.
PMAP-CutDBP51888.
PROiP51888.
SOURCEiSearch...

Gene expression databases

BgeeiP51888.
CleanExiHS_PRELP.
GenevisibleiP51888. HS.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.