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Database: UniProt
Entry: PRELP_RAT
LinkDB: PRELP_RAT
Original site: 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   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}.
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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   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   Genevisible; Q9EQP5; RN.
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.
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
//
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