ID   PRELP_BOVIN             Reviewed;         381 AA.
AC   Q9GKN8;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Prolargin;
DE   AltName: Full=Proline-arginine-rich end leucine-rich repeat protein;
DE   Flags: Precursor;
GN   Name=PRELP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Articular cartilage;
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   FUNCTION.
RX   PubMed=11847210; DOI=10.1074/jbc.m108285200;
RA   Bengtsson E., Moergelin M., Sasaki T., Timpl R., Heinegaard D., Aspberg A.;
RT   "The leucine-rich repeat protein PRELP binds perlecan and collagens and may
RT   function as a basement membrane anchor.";
RL   J. Biol. Chem. 277:15061-15068(2002).
CC   -!- FUNCTION: May anchor basement membranes to the underlying connective
CC       tissue. {ECO:0000269|PubMed:11847210}.
CC   -!- SUBUNIT: Binds the basement membrane heparan sulfate proteoglycan
CC       perlecan and triple helical collagens type I and type II.
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.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; AF163568; AAG23723.1; -; mRNA.
DR   RefSeq; NP_776859.1; NM_174434.3.
DR   AlphaFoldDB; Q9GKN8; -.
DR   SMR; Q9GKN8; -.
DR   STRING; 9913.ENSBTAP00000023709; -.
DR   PaxDb; Q9GKN8; -.
DR   PeptideAtlas; Q9GKN8; -.
DR   PRIDE; Q9GKN8; -.
DR   GeneID; 282000; -.
DR   KEGG; bta:282000; -.
DR   CTD; 5549; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q9GKN8; -.
DR   OrthoDB; 826997at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 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   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   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..381
FT                   /note="Prolargin"
FT                   /id="PRO_0000032743"
FT   REPEAT          94..113
FT                   /note="LRR 1"
FT   REPEAT          114..137
FT                   /note="LRR 2"
FT   REPEAT          138..161
FT                   /note="LRR 3"
FT   REPEAT          162..182
FT                   /note="LRR 4"
FT   REPEAT          183..206
FT                   /note="LRR 5"
FT   REPEAT          207..232
FT                   /note="LRR 6"
FT   REPEAT          233..253
FT                   /note="LRR 7"
FT   REPEAT          254..277
FT                   /note="LRR 8"
FT   REPEAT          278..302
FT                   /note="LRR 9"
FT   REPEAT          303..322
FT                   /note="LRR 10"
FT   REPEAT          323..361
FT                   /note="LRR 11"
FT   REPEAT          362..381
FT                   /note="LRR 12"
FT   REGION          19..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..65
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        331..372
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  43683 MW;  23DA99C01BB772A0 CRC64;
     MRSSLCWLLT LLLILATAAQ GQPTRRPRPR PRPRPRPRLR PTPSFPQPDE PTEPTDLPPP
     LPPGPPSVFP DCPRECYCPP DFPSALYCDS RNLRKVPVIP SRIHYLYLQN NFITELPVES
     FKNATGLRWI NLDNNRIRKV DQRVLEKLPS LVFLYLEKNQ LEEVPAALPR NLEQLRLSQN
     QISRIPPGVF SKLENLLLLD LQHNKLSDGV FKPDTFQGLK NLMQLNLAHN TLRKMPPKVP
     SAIHQLYLDS NRIEAIPSGY FKGFPNLAFI RLNYNQLSDR GLPKNSFNIS NLLVLHLSHN
     RISSVPAISS RLEHLYLNNN SIEKINGTQI CPNNIVAFHD FSSDLEHVPH LRYLRLDGNY
     LKPPIPLDLM MCFRLLQSVV I