NRP2_MOUSE
ID NRP2_MOUSE Reviewed; 931 AA.
AC O35375; B1AT44; O35373; O35374; O35376; O35377; O35378;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Neuropilin-2;
DE AltName: Full=Vascular endothelial cell growth factor 165 receptor 2;
DE Flags: Precursor;
GN Name=Nrp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A0; A17; A22; A5; B0 AND B5).
RC STRAIN=BALB/cJ;
RX PubMed=9331348; DOI=10.1016/s0896-6273(00)80371-2;
RA Chen H., Chedotal A., He Z.-G., Goodman C.S., Tessier-Lavigne M.;
RT "Neuropilin-2, a novel member of the neuropilin family, is a high affinity
RT receptor for the semaphorins Sema E and Sema IV but not Sema III.";
RL Neuron 19:547-559(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and
CC VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
CC -!- SUBUNIT: Heterodimer with NRP1. Binds PLXNB1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60462}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:O60462}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=A22;
CC IsoId=O35375-1; Sequence=Displayed;
CC Name=A0;
CC IsoId=O35375-2; Sequence=VSP_004344;
CC Name=A5;
CC IsoId=O35375-3; Sequence=VSP_004345;
CC Name=A17;
CC IsoId=O35375-4; Sequence=VSP_004343;
CC Name=B0;
CC IsoId=O35375-5; Sequence=VSP_004346;
CC Name=B5;
CC IsoId=O35375-6; Sequence=VSP_004347;
CC -!- TISSUE SPECIFICITY: Expressed in developing CNS, PNS and in some
CC nonneural tissues including limb buds, developing bones, muscles,
CC intestinal epithelium, kidney, lung and submandibular gland.
CC -!- DEVELOPMENTAL STAGE: The expression pattern is very dynamic and is
CC developmentally regulated.
CC -!- DOMAIN: The tandem CUB domains mediate binding to semaphorin, while the
CC tandem F5/8 domains are responsible for heparin and VEGF binding.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}.
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DR EMBL; AF022856; AAC53379.1; -; mRNA.
DR EMBL; AF022854; AAC53377.1; -; mRNA.
DR EMBL; AF022855; AAC53378.1; -; mRNA.
DR EMBL; AF022857; AAC53380.1; -; mRNA.
DR EMBL; AF022858; AAC53381.1; -; mRNA.
DR EMBL; AF022861; AAC53382.1; -; mRNA.
DR EMBL; AL645727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14995.1; -. [O35375-3]
DR CCDS; CCDS35589.1; -. [O35375-1]
DR CCDS; CCDS35590.1; -. [O35375-4]
DR CCDS; CCDS35591.1; -. [O35375-2]
DR CCDS; CCDS35592.1; -. [O35375-6]
DR CCDS; CCDS35593.1; -. [O35375-5]
DR RefSeq; NP_001070871.1; NM_001077403.1. [O35375-1]
DR AlphaFoldDB; O35375; -.
DR SMR; O35375; -.
DR BioGRID; 201849; 12.
DR STRING; 10090.ENSMUSP00000109794; -.
DR GlyGen; O35375; 4 sites.
DR iPTMnet; O35375; -.
DR PhosphoSitePlus; O35375; -.
DR SwissPalm; O35375; -.
DR CPTAC; non-CPTAC-3486; -.
DR MaxQB; O35375; -.
DR PaxDb; O35375; -.
DR PeptideAtlas; O35375; -.
DR PRIDE; O35375; -.
DR ProteomicsDB; 293740; -. [O35375-1]
DR ProteomicsDB; 293741; -. [O35375-2]
DR ProteomicsDB; 293742; -. [O35375-3]
DR ProteomicsDB; 293743; -. [O35375-4]
DR ProteomicsDB; 293744; -. [O35375-5]
DR ProteomicsDB; 293745; -. [O35375-6]
DR ABCD; O35375; 5 sequenced antibodies.
DR Antibodypedia; 34173; 448 antibodies from 35 providers.
DR DNASU; 18187; -.
DR Ensembl; ENSMUST00000027112; ENSMUSP00000027112; ENSMUSG00000025969. [O35375-6]
DR Ensembl; ENSMUST00000063594; ENSMUSP00000069379; ENSMUSG00000025969. [O35375-4]
DR Ensembl; ENSMUST00000075144; ENSMUSP00000074642; ENSMUSG00000025969. [O35375-3]
DR Ensembl; ENSMUST00000102822; ENSMUSP00000099886; ENSMUSG00000025969. [O35375-2]
DR Ensembl; ENSMUST00000114155; ENSMUSP00000109792; ENSMUSG00000025969. [O35375-5]
DR Ensembl; ENSMUST00000114157; ENSMUSP00000109794; ENSMUSG00000025969. [O35375-1]
DR GeneID; 18187; -.
DR KEGG; mmu:18187; -.
DR UCSC; uc007bfj.1; mouse. [O35375-6]
DR UCSC; uc007bfl.1; mouse. [O35375-1]
DR UCSC; uc007bfn.1; mouse. [O35375-3]
DR UCSC; uc007bfo.1; mouse. [O35375-2]
DR CTD; 8828; -.
DR MGI; MGI:1100492; Nrp2.
DR VEuPathDB; HostDB:ENSMUSG00000025969; -.
DR eggNOG; ENOG502QVB7; Eukaryota.
DR GeneTree; ENSGT00940000155270; -.
DR HOGENOM; CLU_015228_6_1_1; -.
DR InParanoid; O35375; -.
DR OMA; XYDFIEI; -.
DR PhylomeDB; O35375; -.
DR TreeFam; TF316506; -.
DR Reactome; R-MMU-194306; Neurophilin interactions with VEGF and VEGFR.
DR BioGRID-ORCS; 18187; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Nrp2; mouse.
DR PRO; PR:O35375; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35375; protein.
DR Bgee; ENSMUSG00000025969; Expressed in vault of skull and 268 other tissues.
DR ExpressionAtlas; O35375; baseline and differential.
DR Genevisible; O35375; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017154; F:semaphorin receptor activity; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:InterPro.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IMP:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:1904835; P:dorsal root ganglion morphogenesis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021612; P:facial nerve structural organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903375; P:facioacoustic ganglion development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IMP:BHF-UCL.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IMP:MGI.
DR GO; GO:0021675; P:nerve development; IMP:BHF-UCL.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:BHF-UCL.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:1902285; P:semaphorin-plexin signaling pathway involved in neuron projection guidance; IMP:BHF-UCL.
DR GO; GO:0097374; P:sensory neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0061549; P:sympathetic ganglion development; IMP:BHF-UCL.
DR GO; GO:0097490; P:sympathetic neuron projection extension; IMP:BHF-UCL.
DR GO; GO:0097491; P:sympathetic neuron projection guidance; IMP:BHF-UCL.
DR GO; GO:0061551; P:trigeminal ganglion development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0036484; P:trunk neural crest cell migration; IMP:MGI.
DR GO; GO:0036486; P:ventral trunk neural crest cell migration; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021649; P:vestibulocochlear nerve structural organization; IMP:ParkinsonsUK-UCL.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00057; FA58C; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR014648; Neuropilin.
DR InterPro; IPR027143; Neuropilin-2.
DR InterPro; IPR022579; Neuropilin_C.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806:SF2; PTHR46806:SF2; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF11980; DUF3481; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF00629; MAM; 1.
DR PIRSF; PIRSF036960; Neuropilin; 1.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00231; FA58C; 2.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Heparin-binding; Membrane; Metal-binding;
KW Neurogenesis; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..931
FT /note="Neuropilin-2"
FT /id="PRO_0000021864"
FT TOPO_DOM 21..864
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 865..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..142
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 149..267
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 277..427
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 434..592
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 642..802
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..55
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT DISULFID 83..105
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT DISULFID 149..175
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT DISULFID 208..230
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT DISULFID 277..427
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT DISULFID 434..592
FT /evidence="ECO:0000250|UniProtKB:O60462"
FT VAR_SEQ 809..830
FT /note="Missing (in isoform A0)"
FT /evidence="ECO:0000303|PubMed:9331348"
FT /id="VSP_004344"
FT VAR_SEQ 809..813
FT /note="Missing (in isoform A17)"
FT /evidence="ECO:0000303|PubMed:9331348"
FT /id="VSP_004343"
FT VAR_SEQ 810..931
FT /note="EDFKVDIPETHGGEGYEDEIDDEYEGDWSNSSSSTSGAGDPSSGKEKSWLYT
FT LDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKV
FT KINHQKCCSEA -> GTLPPGTEPTVDTVPVQPIPAYWYYVMAAGGAVLVLASVVLALV
FT LHYHRFRYAAKKTDHSITYKTSHYTNGAPLAVEPTLTIKLEQERGSHC (in
FT isoform B0)"
FT /evidence="ECO:0000303|PubMed:9331348"
FT /id="VSP_004346"
FT VAR_SEQ 814..931
FT /note="VDIPETHGGEGYEDEIDDEYEGDWSNSSSSTSGAGDPSSGKEKSWLYTLDPI
FT LITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKINH
FT QKCCSEA -> GGTLPPGTEPTVDTVPVQPIPAYWYYVMAAGGAVLVLASVVLALVLHY
FT HRFRYAAKKTDHSITYKTSHYTNGAPLAVEPTLTIKLEQERGSHC (in isoform
FT B5)"
FT /evidence="ECO:0000303|PubMed:9331348"
FT /id="VSP_004347"
FT VAR_SEQ 814..830
FT /note="Missing (in isoform A5)"
FT /evidence="ECO:0000303|PubMed:9331348"
FT /id="VSP_004345"
FT CONFLICT 32
FT /note="L -> P (in Ref. 1; AAC53377/AAC53378/AAC53379/
FT AAC53380/AAC53381/AAC53382)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="I -> G (in Ref. 1; AAC53377/AAC53378/AAC53382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 104631 MW; 08AA821E696A2885 CRC64;
MDMFPLTWVF LALYFSGHEV RSQQDPPCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWIVY
APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSVL
YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL
AKPRMEIILQ FLTFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSKLRS
STGILSLTFH TDMAVAKDGF SARYYLIHQE PPENFQCNVP LGMESGRIAN EQISASSTFS
DGRWTPQQSR LHGDDNGWTP NLDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQKGYYVKS
YKLEVSTNGE DWMVYRHGKN HKIFQANNDA TEVVLNKLHM PLLTRFIRIR PQTWHLGIAL
RLELFGCRVT DAPCSNMLGM LSGLIADTQI SASSTREYLW SPSAARLVSS RSGWFPRNPQ
AQPGEEWLQV DLGTPKTVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGKDWEYIQD
PRTQQTKLFE GNMHYDTPDI RRFDPVPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT
VETLGPTVKS EETTTPYPMD EDATECGENC SFEDDKDLQL PSGFNCNFDF PEETCGWVYD
HAKWLRSTWI SSANPNDRTF PDDKNFLKLQ SDGRREGQYG RLISPPVHLP RSPVCMEFQY
QAMGGHGVAL QVVREASQES KLLWVIREDQ GSEWKHGRII LPSYDMEYQI VFEGVIGKGR
SGEISIDDIR ISTDVPLENC MEPISAFAGE DFKVDIPETH GGEGYEDEID DEYEGDWSNS
SSSTSGAGDP SSGKEKSWLY TLDPILITII AMSSLGVLLG ATCAGLLLYC TCSYSGLSSR
SCTTLENYNF ELYDGLKHKV KINHQKCCSE A
