ID PRELP_RAT Reviewed; 377 AA. AC Q9EQP5; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 148. DE RecName: Full=Prolargin; DE AltName: Full=Proline-arginine-rich end leucine-rich repeat protein; DE Flags: Precursor; GN Name=Prelp; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Chondrosarcoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; 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). 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 -!- 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. {ECO:0000250|UniProtKB:P51888, CC ECO:0000250|UniProtKB:Q9GKN8}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF163569; AAG23724.1; -; mRNA. DR EMBL; BC072487; AAH72487.1; -; mRNA. DR RefSeq; NP_445837.1; NM_053385.1. DR RefSeq; XP_006249953.1; XM_006249891.3. DR RefSeq; XP_008767794.1; XM_008769572.1. DR AlphaFoldDB; Q9EQP5; -. DR SMR; Q9EQP5; -. DR STRING; 10116.ENSRNOP00000004241; -. DR GlyCosmos; Q9EQP5; 4 sites, No reported glycans. DR GlyGen; Q9EQP5; 4 sites. DR iPTMnet; Q9EQP5; -. DR PhosphoSitePlus; Q9EQP5; -. DR SwissPalm; Q9EQP5; -. DR PaxDb; 10116-ENSRNOP00000004241; -. DR Ensembl; ENSRNOT00000004241.5; ENSRNOP00000004241.2; ENSRNOG00000003120.6. DR Ensembl; ENSRNOT00055037488; ENSRNOP00055030572; ENSRNOG00055021862. DR Ensembl; ENSRNOT00060030046; ENSRNOP00060024251; ENSRNOG00060017584. DR Ensembl; ENSRNOT00065032526; ENSRNOP00065025956; ENSRNOG00065019334. DR GeneID; 84400; -. DR KEGG; rno:84400; -. DR UCSC; RGD:620226; rat. DR AGR; RGD:620226; -. DR CTD; 5549; -. DR RGD; 620226; Prelp. DR eggNOG; KOG0619; Eukaryota. DR GeneTree; ENSGT00940000160163; -. DR InParanoid; Q9EQP5; -. DR OMA; ELRWVNL; -. DR OrthoDB; 521898at2759; -. DR PhylomeDB; Q9EQP5; -. DR TreeFam; TF334562; -. DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis. DR Reactome; R-RNO-2022857; Keratan sulfate degradation. DR PRO; PR:Q9EQP5; -. DR Proteomes; UP000002494; Chromosome 13. DR Bgee; ENSRNOG00000003120; Expressed in lung and 19 other cell types or tissues. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0008201; F:heparin binding; IDA:RGD. DR GO; GO:0090398; P:cellular senescence; ISO:RGD. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2. 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; 2. DR Pfam; PF01462; LRRNT; 1. DR SMART; SM00364; LRR_BAC; 5. DR SMART; SM00369; LRR_TYP; 8. DR SMART; SM00013; LRRNT; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 10. DR Genevisible; Q9EQP5; RN. PE 2: Evidence at transcript level; KW Disulfide bond; Extracellular matrix; Glycoprotein; Heparan sulfate; KW Heparin-binding; Leucine-rich repeat; Proteoglycan; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..377 FT /note="Prolargin" FT /id="PRO_0000032746" FT REPEAT 90..109 FT /note="LRR 1" FT REPEAT 110..133 FT /note="LRR 2" FT REPEAT 134..157 FT /note="LRR 3" FT REPEAT 158..178 FT /note="LRR 4" FT REPEAT 179..202 FT /note="LRR 5" FT REPEAT 203..228 FT /note="LRR 6" FT REPEAT 229..249 FT /note="LRR 7" FT REPEAT 250..273 FT /note="LRR 8" FT REPEAT 274..298 FT /note="LRR 9" FT REPEAT 299..318 FT /note="LRR 10" FT REPEAT 319..357 FT /note="LRR 11" FT REPEAT 358..377 FT /note="LRR 12" FT REGION 22..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..61 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 119 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 284 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 315 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 322 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 327..368 FT /evidence="ECO:0000250" SQ SEQUENCE 377 AA; 43179 MW; 79CBE62534753C46 CRC64; MRASFFWFLP LLLILASVAQ GQPRPKPGIR RKPKPRPTPS FPQPHEPAEP TDLPPPLPPG PPSVFPDCPR ECYCPPDFPS ALYCDSRNLR KVPIIPPRIH YLYLQNNFIT ELPVESFKNA TGLRWINLDN NRIRKVDQRV LEKLPGLAFL YMDKNQLEEV PSALPRNLEQ LRLSQNLISR IPPGVFSKLE NLLLLDLQHN RLSDGVFKAD TFQGLKNLMQ LNLAHNILRR MPPKVPPAIH QLYLDSNKIE TIPSGYFKDF PNLAFIRMNY NKLSDRGLPK NSFNISNLLV LHLSHNKISN VPAISNKLEH LYLNNNSIEK INGTQICPSN LVAFHDFSSD LENVPHLRYL RLDGNFLKPP IPLDLMMCFR LLQSVVI //