PRELP_RAT
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 03-AUG-2022, entry version 141.
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}.
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 -!- 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; 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 GlyGen; Q9EQP5; 4 sites.
DR iPTMnet; Q9EQP5; -.
DR PhosphoSitePlus; Q9EQP5; -.
DR PaxDb; Q9EQP5; -.
DR PRIDE; Q9EQP5; -.
DR Ensembl; ENSRNOT00000004241; ENSRNOP00000004241; ENSRNOG00000003120.
DR GeneID; 84400; -.
DR KEGG; rno:84400; -.
DR UCSC; RGD:620226; rat.
DR CTD; 5549; -.
DR RGD; 620226; Prelp.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160163; -.
DR InParanoid; Q9EQP5; -.
DR OMA; LAFIRMN; -.
DR OrthoDB; 826997at2759; -.
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 tissues.
DR Genevisible; Q9EQP5; RN.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0031012; C:extracellular matrix; TAS:RGD.
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; IDA:RGD.
DR GO; GO:0090398; P:cellular senescence; ISO:RGD.
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; 2.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 10.
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..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
