PRELP_MOUSE
ID PRELP_MOUSE Reviewed; 378 AA.
AC Q9JK53;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Prolargin;
DE AltName: Full=Proline-arginine-rich end leucine-rich repeat protein;
DE Flags: Precursor;
GN Name=Prelp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11731272; DOI=10.1016/s0945-053x(01)00165-2;
RA Grover J., Roughley P.J.;
RT "Characterization and expression of murine PRELP.";
RL Matrix Biol. 20:555-564(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Expressed in cartilage throughout both fetal
CC development and postnatal life. It is also expressed in the developing
CC embryo prior to skeletogenesis. In adult, highest expression in lung,
CC lower levels in cardiac and skeletal muscle.
CC -!- DOMAIN: The basic N-terminal Arg/Pro-rich binds heparin and heparan
CC sulfate. Binds collagens type I and type II through its leucine-rich
CC 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; AF261888; AAF72994.2; -; Genomic_DNA.
DR EMBL; AF261887; AAF72994.2; JOINED; Genomic_DNA.
DR EMBL; BC019775; AAH19775.1; -; mRNA.
DR CCDS; CCDS15300.1; -.
DR RefSeq; NP_473418.3; NM_054077.4.
DR RefSeq; XP_006529147.1; XM_006529084.3.
DR RefSeq; XP_006529148.1; XM_006529085.3.
DR AlphaFoldDB; Q9JK53; -.
DR SMR; Q9JK53; -.
DR STRING; 10090.ENSMUSP00000048803; -.
DR GlyGen; Q9JK53; 4 sites.
DR PhosphoSitePlus; Q9JK53; -.
DR MaxQB; Q9JK53; -.
DR PaxDb; Q9JK53; -.
DR PRIDE; Q9JK53; -.
DR ProteomicsDB; 291791; -.
DR Antibodypedia; 34545; 144 antibodies from 21 providers.
DR DNASU; 116847; -.
DR Ensembl; ENSMUST00000048432; ENSMUSP00000048803; ENSMUSG00000041577.
DR GeneID; 116847; -.
DR KEGG; mmu:116847; -.
DR UCSC; uc007crc.3; mouse.
DR CTD; 5549; -.
DR MGI; MGI:2151110; Prelp.
DR VEuPathDB; HostDB:ENSMUSG00000041577; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160163; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; Q9JK53; -.
DR OMA; LAFIRMN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9JK53; -.
DR TreeFam; TF334562; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR BioGRID-ORCS; 116847; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Prelp; mouse.
DR PRO; PR:Q9JK53; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JK53; protein.
DR Bgee; ENSMUSG00000041577; Expressed in humerus cartilage element and 189 other tissues.
DR ExpressionAtlas; Q9JK53; baseline and differential.
DR Genevisible; Q9JK53; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0090398; P:cellular senescence; IDA:MGI.
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; 10.
PE 1: Evidence at protein 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..378
FT /note="Prolargin"
FT /id="PRO_0000032745"
FT REPEAT 91..110
FT /note="LRR 1"
FT REPEAT 111..134
FT /note="LRR 2"
FT REPEAT 135..158
FT /note="LRR 3"
FT REPEAT 159..179
FT /note="LRR 4"
FT REPEAT 180..203
FT /note="LRR 5"
FT REPEAT 204..229
FT /note="LRR 6"
FT REPEAT 230..250
FT /note="LRR 7"
FT REPEAT 251..274
FT /note="LRR 8"
FT REPEAT 275..299
FT /note="LRR 9"
FT REPEAT 300..319
FT /note="LRR 10"
FT REPEAT 320..358
FT /note="LRR 11"
FT REPEAT 359..378
FT /note="LRR 12"
FT REGION 22..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 328..369
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 43293 MW; 81654FB9D5F55186 CRC64;
MRASFFWLLP LLLILASVAQ GQPTRPKPGI RRKPKPRPTP RFPQAPEPAE PTDLPPPLPP
GPPSVFPDCP RECYCPPDFP SALYCDSRNL RRVPVIPPRI HYLYLQNNFI TELPLESFQN
ATGLRWVNLD NNRIRKVDQR VLGKLPSLAF LYMEKNQLEE VPSALPRNLE QLRLSQNLIS
RIPPGVFSKL ENLLLLDLQH NRLSDGVFKA DTFQGLKNLM QLNLAHNILR KMPPKVPQAI
HQLYLDSNKI ETIPNGYFKD FPNLAFIRMN YNKLSDRGLP KNSFNISNLL VLHLSHNKIS
NVPAISNKLE HLYLNNNSIE KINGTQICPN NLVAFHDFSS DLENVPHLRY LRLDGNFLKP
PIPLDLMMCF RLLQSVVI
