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   24-JAN-2024, entry version 196.
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   DOMAIN.
RX   PubMed=11007795; DOI=10.1074/jbc.m007917200;
RA   Bengtsson E., Aspberg A., Heinegaard D., Sommarin Y., Spillmann D.;
RT   "The amino-terminal part of PRELP binds to heparin and heparan sulfate.";
RL   J. Biol. Chem. 275:40695-40702(2000).
RN   [8]
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|UniProtKB:Q9GKN8}.
CC   -!- SUBUNIT: Binds the basement membrane heparan sulfate proteoglycan
CC       perlecan and triple helical collagens type I and type II.
CC       {ECO:0000250|UniProtKB:Q9GKN8}.
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 (PubMed:11007795). Binds collagens type I and type II
CC       through its leucine-rich repeat domain (By similarity).
CC       {ECO:0000250|UniProtKB:Q9GKN8, ECO:0000269|PubMed:11007795}.
CC   -!- PTM: Glycosylated; contains heparan sulfate.
CC       {ECO:0000250|UniProtKB:Q9GKN8}.
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   GlyCosmos; P51888; 7 sites, 38 glycans.
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; 9606-ENSP00000343924; -.
DR   PeptideAtlas; P51888; -.
DR   ProteomicsDB; 56449; -.
DR   TopDownProteomics; P51888; -.
DR   Antibodypedia; 34545; 169 antibodies from 22 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   AGR; HGNC:9357; -.
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; ELRWVNL; -.
DR   OrthoDB; 521898at2759; -.
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; 4 hits in 1157 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 172 other cell types or tissues.
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; Ribonuclease Inhibitor; 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   PANTHER; PTHR45712; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF8; PROLARGIN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   SMART; SM00364; LRR_BAC; 4.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 11.
DR   Genevisible; P51888; HS.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Heparan sulfate; Heparin-binding; Leucine-rich repeat;
KW   Proteoglycan; Reference proteome; Repeat; Secreted; 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
//