PRELP_HUMAN
ID PRELP_HUMAN Reviewed; 382 AA.
AC P51888; Q6FG38;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Prolargin;
DE AltName: Full=Proline-arginine-rich end leucine-rich repeat protein;
DE Flags: Precursor;
GN Name=PRELP; Synonyms=SLRR2A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7592739; DOI=10.1074/jbc.270.43.25639;
RA Bengtsson E., Neame P.J., Heinegaard D., Sommarin Y.;
RT "The primary structure of a basic leucine-rich repeat protein, PRELP, found
RT in connective tissues.";
RL J. Biol. Chem. 270:25639-25644(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8954791; DOI=10.1006/geno.1996.0605;
RA Grover J., Chen X.-N., Korenberg J.R., Recklies A.D., Roughley P.J.;
RT "The gene organization, chromosome location, and expression of a 55-kDa
RT matrix protein (PRELP) of human articular cartilage.";
RL Genomics 38:109-117(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124 AND ASN-327.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: May anchor basement membranes to the underlying connective
CC tissue. {ECO:0000250}.
CC -!- SUBUNIT: Binds the basement membrane heparan sulfate proteoglycan
CC perlecan and triple helical collagens type I and type II.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Connective tissue.
CC -!- DOMAIN: The basic N-terminal Arg/Pro-rich region binds heparin and
CC heparan sulfate. Binds collagens type I and type II through its
CC leucine-rich repeat domain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; U29089; AAC50230.1; -; mRNA.
DR EMBL; U41344; AAC18782.1; -; Genomic_DNA.
DR EMBL; U41343; AAC18782.1; JOINED; Genomic_DNA.
DR EMBL; CR542270; CAG47066.1; -; mRNA.
DR EMBL; AL391817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91481.1; -; Genomic_DNA.
DR EMBL; BC032498; AAH32498.1; -; mRNA.
DR CCDS; CCDS1438.1; -.
DR PIR; I39068; I39068.
DR RefSeq; NP_002716.1; NM_002725.3.
DR RefSeq; NP_958505.1; NM_201348.1.
DR AlphaFoldDB; P51888; -.
DR SMR; P51888; -.
DR BioGRID; 111540; 38.
DR IntAct; P51888; 9.
DR MINT; P51888; -.
DR STRING; 9606.ENSP00000343924; -.
DR GlyConnect; 1637; 35 N-Linked glycans (3 sites).
DR GlyGen; P51888; 7 sites, 34 N-linked glycans (3 sites), 4 O-linked glycans (3 sites).
DR iPTMnet; P51888; -.
DR PhosphoSitePlus; P51888; -.
DR BioMuta; PRELP; -.
DR DMDM; 1709586; -.
DR EPD; P51888; -.
DR jPOST; P51888; -.
DR MassIVE; P51888; -.
DR PaxDb; P51888; -.
DR PeptideAtlas; P51888; -.
DR PRIDE; P51888; -.
DR ProteomicsDB; 56449; -.
DR TopDownProteomics; P51888; -.
DR Antibodypedia; 34545; 144 antibodies from 21 providers.
DR DNASU; 5549; -.
DR Ensembl; ENST00000343110.3; ENSP00000343924.2; ENSG00000188783.6.
DR GeneID; 5549; -.
DR KEGG; hsa:5549; -.
DR MANE-Select; ENST00000343110.3; ENSP00000343924.2; NM_002725.4; NP_002716.1.
DR UCSC; uc001gzs.4; human.
DR CTD; 5549; -.
DR DisGeNET; 5549; -.
DR GeneCards; PRELP; -.
DR HGNC; HGNC:9357; PRELP.
DR HPA; ENSG00000188783; Low tissue specificity.
DR MIM; 601914; gene.
DR neXtProt; NX_P51888; -.
DR OpenTargets; ENSG00000188783; -.
DR PharmGKB; PA33729; -.
DR VEuPathDB; HostDB:ENSG00000188783; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160163; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; P51888; -.
DR OMA; LAFIRMN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P51888; -.
DR TreeFam; TF334562; -.
DR PathwayCommons; P51888; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-2022857; Keratan sulfate degradation.
DR Reactome; R-HSA-3656225; Defective CHST6 causes MCDC1.
DR Reactome; R-HSA-3656243; Defective ST3GAL3 causes MCT12 and EIEE15.
DR Reactome; R-HSA-3656244; Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
DR SignaLink; P51888; -.
DR BioGRID-ORCS; 5549; 3 hits in 1067 CRISPR screens.
DR ChiTaRS; PRELP; human.
DR GeneWiki; PRELP; -.
DR GenomeRNAi; 5549; -.
DR Pharos; P51888; Tbio.
DR PRO; PR:P51888; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P51888; protein.
DR Bgee; ENSG00000188783; Expressed in saphenous vein and 170 other tissues.
DR Genevisible; P51888; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; ISS:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR027216; Prolargin.
DR PANTHER; PTHR45712:SF8; PTHR45712:SF8; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 11.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Leucine-rich repeat; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..382
FT /note="Prolargin"
FT /id="PRO_0000032744"
FT REPEAT 95..114
FT /note="LRR 1"
FT REPEAT 115..138
FT /note="LRR 2"
FT REPEAT 139..162
FT /note="LRR 3"
FT REPEAT 163..183
FT /note="LRR 4"
FT REPEAT 184..207
FT /note="LRR 5"
FT REPEAT 208..233
FT /note="LRR 6"
FT REPEAT 234..254
FT /note="LRR 7"
FT REPEAT 255..278
FT /note="LRR 8"
FT REPEAT 279..303
FT /note="LRR 9"
FT REPEAT 304..323
FT /note="LRR 10"
FT REPEAT 324..362
FT /note="LRR 11"
FT REPEAT 363..382
FT /note="LRR 12"
FT REGION 19..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 332..373
FT /evidence="ECO:0000250"
FT VARIANT 33
FT /note="G -> R (in dbSNP:rs41313926)"
FT /id="VAR_061804"
FT VARIANT 157
FT /note="M -> V (in dbSNP:rs2233726)"
FT /id="VAR_052012"
FT VARIANT 334
FT /note="N -> S (in dbSNP:rs2233732)"
FT /id="VAR_052013"
FT VARIANT 348
FT /note="N -> H (in dbSNP:rs9439)"
FT /id="VAR_011976"
SQ SEQUENCE 382 AA; 43810 MW; A1C4E166B7515695 CRC64;
MRSPLCWLLP LLILASVAQG QPTRRPRPGT GPGRRPRPRP RPTPSFPQPD EPAEPTDLPP
PLPPGPPSIF PDCPRECYCP PDFPSALYCD SRNLRKVPVI PPRIHYLYLQ NNFITELPVE
SFQNATGLRW INLDNNRIRK IDQRVLEKLP GLVFLYMEKN QLEEVPSALP RNLEQLRLSQ
NHISRIPPGV FSKLENLLLL DLQHNRLSDG VFKPDTFHGL KNLMQLNLAH NILRKMPPRV
PTAIHQLYLD SNKIETIPNG YFKSFPNLAF IRLNYNKLTD RGLPKNSFNI SNLLVLHLSH
NRISSVPAIN NRLEHLYLNN NSIEKINGTQ ICPNDLVAFH DFSSDLENVP HLRYLRLDGN
YLKPPIPLDL MMCFRLLQSV VI
