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Protein

Prolargin

Gene

Prelp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

May anchor basement membranes to the underlying connective tissue.By similarity

GO - Molecular functioni

  • extracellular matrix structural constituent Source: InterPro
  • heparin binding Source: RGD

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-2022854. Keratan sulfate biosynthesis.
R-RNO-2022857. Keratan sulfate degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolargin
Alternative name(s):
Proline-arginine-rich end leucine-rich repeat protein
Gene namesi
Name:Prelp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi620226. Prelp.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: GO_Central
  • extracellular space Source: GO_Central
  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000003274622 – 377ProlarginAdd BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi119N-linked (GlcNAc...)Sequence analysis1
Glycosylationi284N-linked (GlcNAc...)Sequence analysis1
Glycosylationi315N-linked (GlcNAc...)Sequence analysis1
Glycosylationi322N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi327 ↔ 368By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9EQP5.
PRIDEiQ9EQP5.

PTM databases

iPTMnetiQ9EQP5.
PhosphoSitePlusiQ9EQP5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000003120.
GenevisibleiQ9EQP5. RN.

Interactioni

Subunit structurei

Binds the basement membrane heparan sulfate proteoglycan perlecan and triple helical collagens type I and type II.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004241.

Structurei

3D structure databases

ProteinModelPortaliQ9EQP5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati90 – 109LRR 1Add BLAST20
Repeati110 – 133LRR 2Add BLAST24
Repeati134 – 157LRR 3Add BLAST24
Repeati158 – 178LRR 4Add BLAST21
Repeati179 – 202LRR 5Add BLAST24
Repeati203 – 228LRR 6Add BLAST26
Repeati229 – 249LRR 7Add BLAST21
Repeati250 – 273LRR 8Add BLAST24
Repeati274 – 298LRR 9Add BLAST25
Repeati299 – 318LRR 10Add BLAST20
Repeati319 – 357LRR 11Add BLAST39
Repeati358 – 377LRR 12Add BLAST20

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi68 – 84Cys-richAdd BLAST17
Compositional biasi192 – 197Poly-Leu6

Domaini

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).By similarity

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiQ9EQP5.
KOiK08125.
OMAiRKMPPKV.
PhylomeDBiQ9EQP5.
TreeFamiTF334562.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR027216. Prolargin.
[Graphical view]
PANTHERiPTHR24373:SF152. PTHR24373:SF152. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 10 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EQP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRASFFWFLP LLLILASVAQ GQPRPKPGIR RKPKPRPTPS FPQPHEPAEP
60 70 80 90 100
TDLPPPLPPG PPSVFPDCPR ECYCPPDFPS ALYCDSRNLR KVPIIPPRIH
110 120 130 140 150
YLYLQNNFIT ELPVESFKNA TGLRWINLDN NRIRKVDQRV LEKLPGLAFL
160 170 180 190 200
YMDKNQLEEV PSALPRNLEQ LRLSQNLISR IPPGVFSKLE NLLLLDLQHN
210 220 230 240 250
RLSDGVFKAD TFQGLKNLMQ LNLAHNILRR MPPKVPPAIH QLYLDSNKIE
260 270 280 290 300
TIPSGYFKDF PNLAFIRMNY NKLSDRGLPK NSFNISNLLV LHLSHNKISN
310 320 330 340 350
VPAISNKLEH LYLNNNSIEK INGTQICPSN LVAFHDFSSD LENVPHLRYL
360 370
RLDGNFLKPP IPLDLMMCFR LLQSVVI
Length:377
Mass (Da):43,179
Last modified:March 1, 2001 - v1
Checksum:i79CBE62534753C46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF163569 mRNA. Translation: AAG23724.1.
BC072487 mRNA. Translation: AAH72487.1.
RefSeqiNP_445837.1. NM_053385.1.
XP_006249953.1. XM_006249891.3.
XP_008767794.1. XM_008769572.1.
UniGeneiRn.112602.

Genome annotation databases

EnsembliENSRNOT00000004241; ENSRNOP00000004241; ENSRNOG00000003120.
ENSRNOT00000076610; ENSRNOP00000068464; ENSRNOG00000003120.
ENSRNOT00000079116; ENSRNOP00000075732; ENSRNOG00000003120.
GeneIDi84400.
KEGGirno:84400.
UCSCiRGD:620226. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF163569 mRNA. Translation: AAG23724.1.
BC072487 mRNA. Translation: AAH72487.1.
RefSeqiNP_445837.1. NM_053385.1.
XP_006249953.1. XM_006249891.3.
XP_008767794.1. XM_008769572.1.
UniGeneiRn.112602.

3D structure databases

ProteinModelPortaliQ9EQP5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004241.

PTM databases

iPTMnetiQ9EQP5.
PhosphoSitePlusiQ9EQP5.

Proteomic databases

PaxDbiQ9EQP5.
PRIDEiQ9EQP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004241; ENSRNOP00000004241; ENSRNOG00000003120.
ENSRNOT00000076610; ENSRNOP00000068464; ENSRNOG00000003120.
ENSRNOT00000079116; ENSRNOP00000075732; ENSRNOG00000003120.
GeneIDi84400.
KEGGirno:84400.
UCSCiRGD:620226. rat.

Organism-specific databases

CTDi5549.
RGDi620226. Prelp.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiQ9EQP5.
KOiK08125.
OMAiRKMPPKV.
PhylomeDBiQ9EQP5.
TreeFamiTF334562.

Enzyme and pathway databases

ReactomeiR-RNO-2022854. Keratan sulfate biosynthesis.
R-RNO-2022857. Keratan sulfate degradation.

Miscellaneous databases

PROiQ9EQP5.

Gene expression databases

BgeeiENSRNOG00000003120.
GenevisibleiQ9EQP5. RN.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR027216. Prolargin.
[Graphical view]
PANTHERiPTHR24373:SF152. PTHR24373:SF152. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 10 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRELP_RAT
AccessioniPrimary (citable) accession number: Q9EQP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.