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P97333 (NRP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuropilin-1
Alternative name(s):
A5 protein
CD_antigen=CD304
Gene names
Name:Nrp1
Synonyms:Nrp
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length923 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis By similarity.

Subunit structure

Homodimer, and heterodimer with NRP2. Binds PLXNB1 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Nervous system.

Domain

The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding By similarity.

Sequence similarities

Belongs to the neuropilin family.

Contains 2 CUB domains.

Contains 2 F5/8 type C domains.

Contains 1 MAM domain.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Neurogenesis
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Heparin-binding
Metal-binding
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Heparan sulfate
Phosphoprotein
Proteoglycan
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processaxon guidance

Inferred from direct assay. Source: MGI

axonal fasciculation

Inferred from mutant phenotype. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: InterPro

cell migration

Inferred from mutant phenotype. Source: MGI

dendrite development

Inferred from mutant phenotype. Source: MGI

dichotomous subdivision of terminal units involved in salivary gland branching

Inferred from mutant phenotype. Source: MGI

heart development

Inferred from genetic interaction. Source: MGI

negative regulation of axon extension involved in axon guidance

Inferred from direct assay. Source: MGI

patterning of blood vessels

Inferred from mutant phenotype. Source: MGI

sympathetic nervous system development

Inferred from mutant phenotype. Source: MGI

trigeminal nerve morphogenesis

Inferred from mutant phenotype. Source: MGI

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neurofilament

Inferred from direct assay. Source: MGI

plasma membrane

Traceable author statement. Source: Reactome

   Molecular functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

semaphorin receptor activity

Inferred from physical interaction. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 923902Neuropilin-1
PRO_0000021860

Regions

Topological domain22 – 856835Extracellular Potential
Transmembrane857 – 87923Helical; Potential
Topological domain880 – 92344Cytoplasmic Potential
Domain27 – 141115CUB 1
Domain147 – 265119CUB 2
Domain275 – 424150F5/8 type C 1
Domain431 – 583153F5/8 type C 2
Domain645 – 811167MAM

Sites

Metal binding1951Calcium By similarity
Metal binding2091Calcium By similarity
Metal binding2501Calcium By similarity

Amino acid modifications

Modified residue9201Phosphotyrosine By similarity
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Ref.4
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Ref.4
Glycosylation6121O-linked (Xyl...) (chondroitin sulfate); alternate By similarity
Glycosylation6121O-linked (Xyl...) (heparan sulfate); alternate By similarity
Glycosylation8421N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 54 Probable
Disulfide bond82 ↔ 104 Probable
Disulfide bond147 ↔ 173 By similarity
Disulfide bond206 ↔ 228 By similarity
Disulfide bond275 ↔ 424 By similarity
Disulfide bond431 ↔ 583 By similarity

Experimental info

Sequence conflict681M → I in BAA08789. Ref.1
Sequence conflict1701S → C in BAA08789. Ref.1
Sequence conflict6011D → H in BAA08789. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P97333 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 23209818C5C42137

FASTA923103,000
        10         20         30         40         50         60 
MERGLPLLCA TLALALALAG AFRSDKCGGT IKIENPGYLT SPGYPHSYHP SEKCEWLIQA 

        70         80         90        100        110        120 
PEPYQRIMIN FNPHFDLEDR DCKYDYVEVI DGENEGGRLW GKFCGKIAPS PVVSSGPFLF 

       130        140        150        160        170        180 
IKFVSDYETH GAGFSIRYEI FKRGPECSQN YTAPTGVIKS PGFPEKYPNS LECTYIIFAP 

       190        200        210        220        230        240 
KMSEIILEFE SFDLEQDSNP PGGMFCRYDR LEIWDGFPEV GPHIGRYCGQ KTPGRIRSSS 

       250        260        270        280        290        300 
GVLSMVFYTD SAIAKEGFSA NYSVLQSSIS EDFKCMEALG MESGEIHSDQ ITASSQYGTN 

       310        320        330        340        350        360 
WSVERSRLNY PENGWTPGED SYKEWIQVDL GLLRFVTAVG TQGAISKETK KKYYVKTYRV 

       370        380        390        400        410        420 
DISSNGEDWI SLKEGNKAII FQGNTNPTDV VLGVFSKPLI TRFVRIKPVS WETGISMRFE 

       430        440        450        460        470        480 
VYGCKITDYP CSGMLGMVSG LISDSQITAS NQADRNWMPE NIRLVTSRTG WALPPSPHPY 

       490        500        510        520        530        540 
TNEWLQVDLG DEKIVRGVII QGGKHRENKV FMRKFKIAYS NNGSDWKTIM DDSKRKAKSF 

       550        560        570        580        590        600 
EGNNNYDTPE LRTFSPLSTR FIRIYPERAT HSGLGLRMEL LGCEVEAPTA GPTTPNGNPV 

       610        620        630        640        650        660 
DECDDDQANC HSGTGDDFQL TGGTTVLATE KPTIIDSTIQ SEFPTYGFNC EFGWGSHKTF 

       670        680        690        700        710        720 
CHWEHDSHAQ LRWSVLTSKT GPIQDHTGDG NFIYSQADEN QKGKVARLVS PVVYSQSSAH 

       730        740        750        760        770        780 
CMTFWYHMSG SHVGTLRVKL RYQKPEEYDQ LVWMVVGHQG DHWKEGRVLL HKSLKLYQVI 

       790        800        810        820        830        840 
FEGEIGKGNL GGIAVDDISI NNHISQEDCA KPTDLDKKNT EIKIDETGST PGYEGEGEGD 

       850        860        870        880        890        900 
KNISRKPGNV LKTLDPILIT IIAMSALGVL LGAVCGVVLY CACWHNGMSE RNLSALENYN 

       910        920 
FELVDGVKLK KDKLNPQSNY SEA

« Hide

References

« Hide 'large scale' references
[1]"Developmentally regulated expression of a cell surface protein, neuropilin, in the mouse nervous system."
Kawakami A., Kitsukawa T., Takagi S., Fujisawa H.
J. Neurobiol. 29:1-17(1996) [PubMed: 8748368] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Embryonic brain.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed: 19656770] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-522, MASS SPECTROMETRY.
Tissue: Myoblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D50086 mRNA. Translation: BAA08789.1.
CH466525 Genomic DNA. Translation: EDL11828.1.
BC060129 mRNA. Translation: AAH60129.1.
IPIIPI00123996.
RefSeqNP_032763.2. NM_008737.2.
UniGeneMm.271745.

3D structure databases

ProteinModelPortalP97333.
SMRP97333. Positions 25-586, 647-811.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-39360N.
IntActP97333. 1 interaction.
MINTMINT-99860.
STRINGP97333.

PTM databases

PhosphoSiteP97333.

Proteomic databases

PRIDEP97333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026917; ENSMUSP00000026917; ENSMUSG00000025810.
GeneID18186.
KEGGmmu:18186.

Organism-specific databases

CTD8829.
MGIMGI:106206. Nrp1.

Phylogenomic databases

eggNOGroNOG12180.
HOGENOMHBG714573.
HOVERGENHBG000502.
InParanoidP97333.
OrthoDBEOG4FN4H1.

Enzyme and pathway databases

ReactomeREACT_115433. Developmental Biology.
REACT_115492. Developmental Biology.

Gene expression databases

ArrayExpressP97333.
BgeeP97333.
CleanExMM_NRP1.
GenevestigatorP97333.
GermOnlineENSMUSG00000025810. Mus musculus.

Family and domain databases

InterProIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008985. ConA-like_lec_gl.
IPR000859. CUB.
IPR008979. Galactose-bd-like.
IPR000998. MAM_dom.
IPR014648. Neuropilin.
IPR022579. Neuropilin1_C.
[Graphical view]
Gene3DG3DSA:2.60.120.290. CUB. 2 hits.
KOK06724.
PfamPF00431. CUB. 2 hits.
PF11980. DUF3481. 1 hit.
PF00754. F5_F8_type_C. 2 hits.
PF00629. MAM. 1 hit.
[Graphical view]
PIRSFPIRSF036960. Neuropilin. 1 hit.
PRINTSPR00020. MAMDOMAIN.
SMARTSM00042. CUB. 2 hits.
SM00231. FA58C. 2 hits.
SM00137. MAM. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
SSF49854. CUB. 2 hits.
SSF49785. Gal_bind_like. 2 hits.
PROSITEPS01180. CUB. 2 hits.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio293506.
SOURCESearch...

Entry information

Entry nameNRP1_MOUSE
AccessionPrimary (citable) accession number: P97333
Secondary accession number(s): Q6PAR3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents