Q9EQP5 (PRELP_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prolargin

Alternative name(s):
Proline-arginine-rich end leucine-rich repeat protein

Gene names

Name:

Prelp

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May anchor basement membranes to the underlying connective tissue By similarity.
Subunit structure	Binds the basement membrane heparan sulfate proteoglycan perlecan and triple helical collagens type I and type II By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix.
Domain	The basic N-terminal Arg/Pro-rich region binds heparin and heparan sulfate. Binds collagens type I and type II through its leucine-rich repeat domain By similarity.
Sequence similarities	Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily. Contains 12 LRR (leucine-rich) repeats.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell aging Inferred from electronic annotation. Source: Compara
Cellular_component	proteinaceous extracellular matrix Traceable author statement Ref.1. Source: RGD
Molecular_function	extracellular matrix structural constituent Inferred from electronic annotation. Source: InterPro heparin binding Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 377	356	Prolargin		PRO_0000032746
Regions
	Repeat	90 – 109	20	LRR 1
	Repeat	110 – 133	24	LRR 2
	Repeat	134 – 157	24	LRR 3
	Repeat	158 – 178	21	LRR 4
	Repeat	179 – 202	24	LRR 5
	Repeat	203 – 228	26	LRR 6
	Repeat	229 – 249	21	LRR 7
	Repeat	250 – 273	24	LRR 8
	Repeat	274 – 298	25	LRR 9
	Repeat	299 – 318	20	LRR 10
	Repeat	319 – 357	39	LRR 11
	Repeat	358 – 377	20	LRR 12
	Compositional bias	68 – 84	17	Cys-rich
	Compositional bias	192 – 197	6	Poly-Leu
Amino acid modifications
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	284	1	N-linked (GlcNAc...) Potential
	Glycosylation	315	1	N-linked (GlcNAc...) Potential
	Glycosylation	322	1	N-linked (GlcNAc...) Potential
	Disulfide bond	327 ↔ 368		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9EQP5 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 79CBE62534753C46	FASTA	377	43,179
	10 20 30 40 50 60 MRASFFWFLP LLLILASVAQ GQPRPKPGIR RKPKPRPTPS FPQPHEPAEP TDLPPPLPPG 70 80 90 100 110 120 PPSVFPDCPR ECYCPPDFPS ALYCDSRNLR KVPIIPPRIH YLYLQNNFIT ELPVESFKNA 130 140 150 160 170 180 TGLRWINLDN NRIRKVDQRV LEKLPGLAFL YMDKNQLEEV PSALPRNLEQ LRLSQNLISR 190 200 210 220 230 240 IPPGVFSKLE NLLLLDLQHN RLSDGVFKAD TFQGLKNLMQ LNLAHNILRR MPPKVPPAIH 250 260 270 280 290 300 QLYLDSNKIE TIPSGYFKDF PNLAFIRMNY NKLSDRGLPK NSFNISNLLV LHLSHNKISN 310 320 330 340 350 360 VPAISNKLEH LYLNNNSIEK INGTQICPSN LVAFHDFSSD LENVPHLRYL RLDGNFLKPP 370 IPLDLMMCFR LLQSVVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The amino-terminal part of PRELP binds to heparin and heparan sulfate." Bengtsson E., Aspberg A., Heinegaard D., Sommarin Y., Spillmann D. J. Biol. Chem. 275:40695-40702(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Chondrosarcoma.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF163569 mRNA. Translation: AAG23724.1. BC072487 mRNA. Translation: AAH72487.1.
IPI	IPI00190287.
RefSeq	NP_445837.1. NM_053385.1.
UniGene	Rn.112602.
3D structure databases
ProteinModelPortal	Q9EQP5.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000004241.
Proteomic databases
PaxDb	Q9EQP5.
PRIDE	Q9EQP5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000004241; ENSRNOP00000004241; ENSRNOG00000003120.
GeneID	84400.
KEGG	rno:84400.
UCSC	RGD:620226. rat.
Organism-specific databases
CTD	5549.
RGD	620226. Prelp.
Phylogenomic databases
eggNOG	COG4886.
GeneTree	ENSGT00600000084286.
HOGENOM	HOG000234447.
HOVERGEN	HBG108061.
InParanoid	Q9EQP5.
KO	K08125.
OMA	NKLEHLY.
OrthoDB	EOG44F69H.
Gene expression databases
Genevestigator	Q9EQP5.
GermOnline	ENSRNOG00000003120. Rattus norvegicus.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR000372. LRR-contain_N. IPR027216. Prolargin. [Graphical view]
PANTHER	PTHR24371:SF15. PTHR24371:SF15. 1 hit.
Pfam	PF00560. LRR_1. 2 hits. PF01462. LRRNT. 1 hit. [Graphical view]
SMART	SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 10 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	616827.

Entry information

Entry name

PRELP_RAT

Accession

Primary (citable) accession number: Q9EQP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program