Nrp1

Functionⁱ

Cell-surface 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. Mediates the chemorepulsant activity of semaphorins. Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (By similarity).

Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity).

Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (By similarity).

By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	195	CalciumBy similarity	1
Metal bindingⁱ	209	CalciumBy similarity	1
Metal bindingⁱ	250	CalciumBy similarity	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

actin cytoskeleton reorganization Source: RGD
angiogenesis Source: RGD
angiogenesis involved in coronary vascular morphogenesis Source: RGD
artery morphogenesis Source: RGD
axonal fasciculation Source: RGD
axon extension involved in axon guidance Source: RGD
axon guidance Source: RGD
axonogenesis involved in innervation Source: RGD
basal dendrite arborization Source: RGD
basal dendrite development Source: RGD
branching involved in blood vessel morphogenesis Source: RGD
branchiomotor neuron axon guidance Source: RGD
cell migration Source: RGD
cell migration involved in sprouting angiogenesis Source: RGD
cellular response to hepatocyte growth factor stimulus Source: RGD
cellular response to vascular endothelial growth factor stimulus Source: RGD
commissural neuron axon guidance Source: RGD
coronary artery morphogenesis Source: RGD
dendrite development Source: RGD
dichotomous subdivision of terminal units involved in salivary gland branching Source: RGD
dorsal root ganglion morphogenesis Source: RGD
endothelial cell chemotaxis Source: RGD
endothelial cell migration Source: RGD
facial nerve structural organization Source: RGD
facioacoustic ganglion development Source: RGD
gonadotrophin-releasing hormone neuronal migration to the hypothalamus Source: RGD
heart development Source: RGD
hepatocyte growth factor receptor signaling pathway Source: RGD
integrin-mediated signaling pathway Source: RGD
motor neuron axon guidance Source: RGD
motor neuron migration Source: UniProtKB
negative regulation of axon extension Source: RGD
negative regulation of axon extension involved in axon guidance
Source: RGD
Inferred from mutant phenotypeⁱ
- Ref.1
  "Neuropilin is a semaphorin III receptor."
  Kolodkin A.L., Levengood D.V., Rowe E.G., Tai Y.-T., Giger R.J., Ginty D.D.
  Cell 90:753-762(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
negative regulation of extrinsic apoptotic signaling pathway Source: RGD
negative regulation of neuron apoptotic process Source: RGD
nerve development Source: RGD
nervous system development
Source: RGD
Non-traceable author statementⁱ
- Ref.1
  "Neuropilin is a semaphorin III receptor."
  Kolodkin A.L., Levengood D.V., Rowe E.G., Tai Y.-T., Giger R.J., Ginty D.D.
  Cell 90:753-762(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
neural crest cell migration involved in autonomic nervous system development Source: RGD
neuron development Source: RGD
neuron migration Source: RGD
neuropilin signaling pathway Source: RGD
otic placode development Source: RGD
outflow tract septum morphogenesis Source: RGD
platelet-derived growth factor receptor signaling pathway Source: RGD
positive chemotaxis Source: RGD
positive regulation of actin cytoskeleton reorganization Source: RGD
positive regulation of angiogenesis Source: RGD
positive regulation of axon extension involved in axon guidance Source: RGD
positive regulation of cell migration involved in sprouting angiogenesis Source: RGD
positive regulation of endothelial cell migration Source: RGD
positive regulation of ERK1 and ERK2 cascade Source: RGD
positive regulation of filopodium assembly Source: RGD
positive regulation of focal adhesion assembly Source: RGD
positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
positive regulation of phosphorylation Source: RGD
positive regulation of retinal ganglion cell axon guidance Source: RGD
positive regulation of stress fiber assembly Source: RGD
positive regulation of substrate adhesion-dependent cell spreading Source: RGD
postsynapse organization Source: RGD
protein localization to early endosome Source: RGD
regulation of axon extension involved in axon guidance Source: RGD
regulation of Cdc42 protein signal transduction Source: RGD
regulation of retinal ganglion cell axon guidance Source: RGD
renal artery morphogenesis Source: RGD
response to wounding
Source: RGD
Inferred from expression patternⁱ
- "Distribution and cellular localization of insulin-regulated aminopeptidase in the rat central nervous system."
  Fernando R.N., Larm J., Albiston A.L., Chai S.Y.
  J Comp Neurol 487:372-390(2005) [PubMed] [Europe PMC] [Abstract]
retinal ganglion cell axon guidance Source: RGD
retina vasculature morphogenesis in camera-type eye Source: RGD
semaphorin-plexin signaling pathway Source: RGD
semaphorin-plexin signaling pathway involved in axon guidance Source: RGD
semaphorin-plexin signaling pathway involved in neuron projection guidance Source: RGD
sensory neuron axon guidance Source: RGD
sprouting angiogenesis Source: RGD
substrate adhesion-dependent cell spreading Source: RGD
substrate-dependent cell migration, cell extension Source: RGD
sympathetic ganglion development Source: RGD
sympathetic nervous system development Source: RGD
sympathetic neuron projection extension Source: RGD
sympathetic neuron projection guidance Source: RGD
toxin transport Source: RGD
trigeminal ganglion development Source: RGD
trigeminal nerve morphogenesis Source: RGD
trigeminal nerve structural organization Source: RGD
vascular endothelial growth factor receptor signaling pathway Source: RGD
VEGF-activated neuropilin signaling pathway Source: RGD
VEGF-activated neuropilin signaling pathway involved in axon guidance Source: RGD
ventral trunk neural crest cell migration Source: RGD
vestibulocochlear nerve structural organization Source: RGD
viral entry into host cell Source: RGD

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Developmental protein, Heparin-binding, Receptor
Biological process	Angiogenesis, Differentiation, Neurogenesis
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

Reactomeⁱ	R-RNO-194306, Neurophilin interactions with VEGF and VEGFR R-RNO-399954, Sema3A PAK dependent Axon repulsion R-RNO-399955, SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion R-RNO-399956, CRMPs in Sema3A signaling R-RNO-445144, Signal transduction by L1

Reactomeⁱ

R-RNO-194306, Neurophilin interactions with VEGF and VEGFR
R-RNO-399954, Sema3A PAK dependent Axon repulsion
R-RNO-399955, SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion
R-RNO-399956, CRMPs in Sema3A signaling
R-RNO-445144, Signal transduction by L1

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Neuropilin-1 Alternative name(s): Vascular endothelial cell growth factor 165 receptor CD_antigen: CD304
Gene namesⁱ	Name:Nrp1
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 19

Organism-specific databases

Rat genome database More...RGDⁱ	621588, Nrp1

RGDⁱ

621588, Nrp1

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	22 – 855	ExtracellularSequence analysisAdd BLAST	834
Transmembraneⁱ	856 – 880	HelicalSequence analysisAdd BLAST	25
Topological domainⁱ	881 – 922	CytoplasmicSequence analysisAdd BLAST	42

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Membrane, Mitochondrion

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL3309098

ChEMBLⁱ

CHEMBL3309098

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 21	Sequence analysisAdd BLAST		21
ChainⁱPRO_0000021861	22 – 922	Neuropilin-1Add BLAST		901

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	27 ↔ 54	1 Publication
Disulfide bondⁱ	82 ↔ 104	1 Publication
Disulfide bondⁱ	147 ↔ 173	By similarity
Glycosylationⁱ	150	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	206 ↔ 228	By similarity
Glycosylationⁱ	261	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	275 ↔ 424	1 Publication
Glycosylationⁱ	300	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	431 ↔ 583	1 Publication
Glycosylationⁱ	522	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	612	O-linked (Xyl...) (chondroitin sulfate) serine; alternateBy similarity	1
Glycosylationⁱ	612	O-linked (Xyl...) (heparan sulfate) serine; alternateBy similarity	1
Glycosylationⁱ	841	N-linked (GlcNAc...) asparagineSequence analysis	1
Modified residueⁱ	893	PhosphoserineBy similarity	1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Heparan sulfate, Phosphoprotein, Proteoglycan

Proteomic databases

PaxDbⁱ	Q9QWJ9
PRIDEⁱ	Q9QWJ9

PTM databases

GlyGenⁱ	Q9QWJ9, 6 sites
iPTMnetⁱ	Q9QWJ9
PhosphoSitePlusⁱ	Q9QWJ9
SwissPalmⁱ	Q9QWJ9

Expressionⁱ

Tissue specificityⁱ

Inductionⁱ

Increased in dorsal root ganglia in response to injury caused by dorsal rhizotomy (PubMed:28270793). Increased in dorsal root ganglia in response to both sciatic nerve crush and transection injury (PubMed:28270793).1 Publication

Gene expression databases

Bgeeⁱ	ENSRNOG00000010744, Expressed in lung and 20 other tissues
Genevisibleⁱ	Q9QWJ9, RN

Interactionⁱ

Subunit structureⁱ

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

Interacts with FER.

Interacts with VEGFA (By similarity).

Interacts with ABCB8/MITOSUR in mitochondria (By similarity).

By similarity

GO - Molecular functionⁱ

growth factor binding Source: RGD
protein kinase binding Source: RGD
vascular endothelial growth factor binding Source: RGD

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	251596, 3 interactors
Database of interacting proteins More...DIPⁱ	DIP-44935N
IntActⁱ	Q9QWJ9, 2 interactors
STRINGⁱ	10116.ENSRNOP00000014492

Chemistry databases

BindingDBⁱ

Q9QWJ9

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	281 – 283	Combined sources	3
Helixⁱ	288 – 290	Combined sources	3
Beta strandⁱ	291 – 294	Combined sources	4
Helixⁱ	299 – 301	Combined sources	3
Helixⁱ	303 – 305	Combined sources	3
Beta strandⁱ	326 – 342	Combined sources	17
Turnⁱ	347 – 349	Combined sources	3
Beta strandⁱ	352 – 368	Combined sources	17
Beta strandⁱ	385 – 389	Combined sources	5
Beta strandⁱ	391 – 414	Combined sources	24
Beta strandⁱ	417 – 424	Combined sources	8
Helixⁱ	426 – 428	Combined sources	3
Beta strandⁱ	429 – 431	Combined sources	3
Beta strandⁱ	432 – 434	Combined sources	3
Turnⁱ	437 – 439	Combined sources	3
Helixⁱ	442 – 444	Combined sources	3
Beta strandⁱ	445 – 449	Combined sources	5
Helixⁱ	459 – 462	Combined sources	4
Turnⁱ	464 – 466	Combined sources	3
Beta strandⁱ	467 – 469	Combined sources	3
Beta strandⁱ	471 – 473	Combined sources	3
Beta strandⁱ	485 – 501	Combined sources	17
Beta strandⁱ	503 – 505	Combined sources	3
Beta strandⁱ	508 – 510	Combined sources	3
Beta strandⁱ	512 – 525	Combined sources	14
Beta strandⁱ	534 – 537	Combined sources	4
Beta strandⁱ	544 – 547	Combined sources	4
Beta strandⁱ	550 – 570	Combined sources	21
Beta strandⁱ	573 – 583	Combined sources	11

Show more details

3D structure databases

SMRⁱ	Q9QWJ9
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q9QWJ9

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	27 – 141	CUB 1PROSITE-ProRule annotationAdd BLAST	115
Domainⁱ	147 – 265	CUB 2PROSITE-ProRule annotationAdd BLAST	119
Domainⁱ	275 – 424	F5/8 type C 1PROSITE-ProRule annotationAdd BLAST	150
Domainⁱ	431 – 583	F5/8 type C 2PROSITE-ProRule annotationAdd BLAST	153
Domainⁱ	645 – 811	MAMPROSITE-ProRule annotationAdd BLAST	167

Domainⁱ

The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding. F5/8 domains mediate the recognition and binding to R/KXXR/K CendR motifs.By similarity

Sequence similaritiesⁱ

Belongs to the neuropilin family.Curated

Keywords - Domainⁱ

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG502QUEH, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000157169
HOGENOMⁱ	CLU_015228_6_1_1
InParanoidⁱ	Q9QWJ9
OMAⁱ	HPYTNEW
Database of Orthologous Groups More...OrthoDBⁱ	124611at2759
PhylomeDBⁱ	Q9QWJ9
TreeFamⁱ	TF316506

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00041, CUB, 2 hits cd00057, FA58C, 2 hits cd06263, MAM, 1 hit
Gene3Dⁱ	2.60.120.260, 2 hits 2.60.120.290, 2 hits
InterProⁱ	View protein in InterPro IPR013320, ConA-like_dom_sf IPR000859, CUB_dom IPR000421, FA58C IPR008979, Galactose-bd-like_sf IPR000998, MAM_dom IPR014648, Neuropilin IPR022579, Neuropilin_C IPR027146, NRP1 IPR035914, Sperma_CUB_dom_sf
PANTHERⁱ	PTHR46806:SF4, PTHR46806:SF4, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00431, CUB, 2 hits PF11980, DUF3481, 1 hit PF00754, F5_F8_type_C, 2 hits PF00629, MAM, 1 hit
PIRSFⁱ	PIRSF036960, Neuropilin, 1 hit
PRINTSⁱ	PR00020, MAMDOMAIN
SMARTⁱ	View protein in SMART SM00042, CUB, 2 hits SM00231, FA58C, 2 hits SM00137, MAM, 1 hit
SUPFAMⁱ	SSF49785, SSF49785, 2 hits SSF49854, SSF49854, 2 hits SSF49899, SSF49899, 1 hit
PROSITEⁱ	View protein in PROSITE PS01180, 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

Sequenceⁱ

Sequence statusⁱ: Complete.

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

Q9QWJ9-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MERGLPLLCA TLALALALAG AFRSDKCGGT IKIENPGYLT SPGYPHSYHP 
        60         70         80         90        100
SEKCEWLIQA PEPYQRIMIN FNPHFDLEDR DCKYDYVEVI DGENEGGRLW 
       110        120        130        140        150
GKFCGKIAPS PVVSSGPFLF IKFVSDYETH GAGFSIRYEI FKRGPECSQN 
       160        170        180        190        200
YTAPTGVIKS PGFPEKYPNS LECTYIIFAP KMSEIILEFE SFDLEQDSNP 
       210        220        230        240        250
PGGVFCRYDR LEIWDGFPEV GPHIGRYCGQ KTPGRIRSSS GILSMVFYTD 
       260        270        280        290        300
SAIAKEGFSA NYSVLQSSIS EDFKCMEALG MESGEIHSDQ ITASSQYGTN 
       310        320        330        340        350
WSVERSRLNY PENGWTPGED SYREWIQVDL GLLRFVTAVG TQGAISKETK 
       360        370        380        390        400
KKYYVKTYRV DISSNGEDWI TLKEGNKAII FQGNTNPTDV VFGVFPKPLI 
       410        420        430        440        450
TRFVRIKPAS WETGISMRFE VYGCKITDYP CSGMLGMVSG LISDSQITAS 
       460        470        480        490        500
NQGDRNWMPE NIRLVTSRTG WALPPSPHPY INEWLQVDLG DEKIVRGVII 
       510        520        530        540        550
QGGKHRENKV FMRKFKIAYS NNGSDWKMIM DDSKRKAKSF EGNNNYDTPE 
       560        570        580        590        600
LRAFTPLSTR FIRIYPERAT HSGLGLRMEL LGCEVEVPTA GPTTPNGNPV 
       610        620        630        640        650
DECDDDQANC HSGTGDDFQL TGGTTVLATE KPTIIDSTIQ SEFPTYGFNC 
       660        670        680        690        700
EFGWGSHKTF CHWEHDSHAQ LRWRVLTSKT GPIQDHTGDG NFIYSQADEN 
       710        720        730        740        750
QKGKVARLVS PVVYSQSSAH CMTFWYHMSG SHVGTLRVKL HYQKPEEYDQ 
       760        770        780        790        800
LVWMVVGHQG DHWKEGRVLL HKSLKLYQVI FEGEIGKGNL GGIAVDDISI 
       810        820        830        840        850
NNHIPQEDCA KPTDLDKKNT EIKIDETGST PGYEEGKGDK NISRKPGNVL 
       860        870        880        890        900
KTLDPILITI IAMSALGVLL GAVCGVVLYC ACWHNGMSER NLSALENYNF 
       910        920 
ELVDGVKLKK DKLNPQSNYS EA

Length:922

Mass (Da):103,082

Last modified:May 1, 2000 - v1

Checksum:ⁱCC6F82AD098B0F2E

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF016296 mRNA Translation: AAC53337.1 BC085689 mRNA Translation: AAH85689.1
NCBI Reference Sequences More...RefSeqⁱ	NP_659566.1, NM_145098.2 XP_006255887.1, XM_006255825.3

Genome annotation databases

Ensemblⁱ	ENSRNOT00000014492; ENSRNOP00000014492; ENSRNOG00000010744 ENSRNOT00000080465; ENSRNOP00000075034; ENSRNOG00000010744
GeneIDⁱ	246331
KEGGⁱ	rno:246331
UCSC genome browser More...UCSCⁱ	RGD:621588, rat

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9QWJ9	Neuropilin-1	)	MOUSE		923	UniRef90_P97333
Neuropilin		RHIFE		928
Neuropilin		pale spear-nosed bat		928
Neuropilin		CALJA		927
Neuropilin		PTEVA		926
+159

Protein	Similar proteins		Species	Score	Length	Source
Q9QWJ9	Neuropilin-1	)	MOUSE		923	UniRef50_P97333
Neuropilin-1		CHICK		914
Neuropilin		pale spear-nosed bat		928
Neuropilin		RHIFE		928
Neuropilin		CALJA		927
+778

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF016296 mRNA Translation: AAC53337.1 BC085689 mRNA Translation: AAH85689.1
RefSeqⁱ	NP_659566.1, NM_145098.2 XP_006255887.1, XM_006255825.3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2ORX	X-ray	2.40	A	273-586	[»]
	2ORZ	X-ray	2.15	A	273-586	[»]
SMRⁱ	Q9QWJ9
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	251596, 3 interactors
DIPⁱ	DIP-44935N
IntActⁱ	Q9QWJ9, 2 interactors
STRINGⁱ	10116.ENSRNOP00000014492

Chemistry databases

BindingDBⁱ	Q9QWJ9
ChEMBLⁱ	CHEMBL3309098

PTM databases

GlyGenⁱ	Q9QWJ9, 6 sites
iPTMnetⁱ	Q9QWJ9
PhosphoSitePlusⁱ	Q9QWJ9
SwissPalmⁱ	Q9QWJ9

Proteomic databases

PaxDbⁱ	Q9QWJ9
PRIDEⁱ	Q9QWJ9

Genome annotation databases

Ensemblⁱ	ENSRNOT00000014492; ENSRNOP00000014492; ENSRNOG00000010744 ENSRNOT00000080465; ENSRNOP00000075034; ENSRNOG00000010744
GeneIDⁱ	246331
KEGGⁱ	rno:246331
UCSCⁱ	RGD:621588, rat

Organism-specific databases

CTDⁱ	8829
RGDⁱ	621588, Nrp1

Phylogenomic databases

eggNOGⁱ	ENOG502QUEH, Eukaryota
GeneTreeⁱ	ENSGT00940000157169
HOGENOMⁱ	CLU_015228_6_1_1
InParanoidⁱ	Q9QWJ9
OMAⁱ	HPYTNEW
OrthoDBⁱ	124611at2759
PhylomeDBⁱ	Q9QWJ9
TreeFamⁱ	TF316506

Enzyme and pathway databases

Reactomeⁱ	R-RNO-194306, Neurophilin interactions with VEGF and VEGFR R-RNO-399954, Sema3A PAK dependent Axon repulsion R-RNO-399955, SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion R-RNO-399956, CRMPs in Sema3A signaling R-RNO-445144, Signal transduction by L1

Reactomeⁱ

R-RNO-194306, Neurophilin interactions with VEGF and VEGFR
R-RNO-399954, Sema3A PAK dependent Axon repulsion
R-RNO-399955, SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion
R-RNO-399956, CRMPs in Sema3A signaling
R-RNO-445144, Signal transduction by L1

Miscellaneous databases

EvolutionaryTraceⁱ	Q9QWJ9
Protein Ontology More...PROⁱ	PR:Q9QWJ9

Gene expression databases

Bgeeⁱ	ENSRNOG00000010744, Expressed in lung and 20 other tissues
Genevisibleⁱ	Q9QWJ9, RN

Family and domain databases

CDDⁱ	cd00041, CUB, 2 hits cd00057, FA58C, 2 hits cd06263, MAM, 1 hit
Gene3Dⁱ	2.60.120.260, 2 hits 2.60.120.290, 2 hits
InterProⁱ	View protein in InterPro IPR013320, ConA-like_dom_sf IPR000859, CUB_dom IPR000421, FA58C IPR008979, Galactose-bd-like_sf IPR000998, MAM_dom IPR014648, Neuropilin IPR022579, Neuropilin_C IPR027146, NRP1 IPR035914, Sperma_CUB_dom_sf
PANTHERⁱ	PTHR46806:SF4, PTHR46806:SF4, 1 hit
Pfamⁱ	View protein in Pfam PF00431, CUB, 2 hits PF11980, DUF3481, 1 hit PF00754, F5_F8_type_C, 2 hits PF00629, MAM, 1 hit
PIRSFⁱ	PIRSF036960, Neuropilin, 1 hit
PRINTSⁱ	PR00020, MAMDOMAIN
SMARTⁱ	View protein in SMART SM00042, CUB, 2 hits SM00231, FA58C, 2 hits SM00137, MAM, 1 hit
SUPFAMⁱ	SSF49785, SSF49785, 2 hits SSF49854, SSF49854, 2 hits SSF49899, SSF49899, 1 hit
PROSITEⁱ	View protein in PROSITE PS01180, 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
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NRP1_RAT
Accessionⁱ	Q9QWJ9Primary (citable) accession number: Q9QWJ9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
	Last sequence update:	May 1, 2000
	Last modified:	June 2, 2021
	This is version 172 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9QWJ9 (NRP1_RAT)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Neuropilin-1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Mitochondrion

Plasma membrane

Cytoskeleton

Cytosol

Endosome

Mitochondrion

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ