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P51888

- PRELP_HUMAN

UniProt

P51888 - PRELP_HUMAN

Protein

Prolargin

Gene

PRELP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33729.

    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

    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.
    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.
    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

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    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

    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: October 1, 2014
    This is version 132 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