NRP2_RAT
ID NRP2_RAT Reviewed; 925 AA.
AC O35276;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Neuropilin-2;
DE AltName: Full=Vascular endothelial cell growth factor 165 receptor 2;
DE Flags: Precursor;
GN Name=Nrp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=9288754; DOI=10.1016/s0092-8674(00)80535-8;
RA Kolodkin A.L., Levengood D.V., Rowe E.G., Tai Y.-T., Giger R.J.,
RA Ginty D.D.;
RT "Neuropilin is a semaphorin III receptor.";
RL Cell 90:753-762(1997).
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION BY INJURY.
RX PubMed=28270793; DOI=10.3389/fneur.2017.00049;
RA Lindholm T., Risling M., Carlstedt T., Hammarberg H., Wallquist W.,
RA Cullheim S., Skoeld M.K.;
RT "Expression of Semaphorins, Neuropilins, VEGF, and Tenascins in Rat and
RT Human Primary Sensory Neurons after a Dorsal Root Injury.";
RL Front. Neurol. 8:49-49(2017).
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 -!- TISSUE SPECIFICITY: Found in certain neuronal populations of the CNS,
CC including dorsal root ganglia, and in other non-neuronal tissues
CC including mesenchymal tissue lining in the ribs.
CC {ECO:0000269|PubMed:28270793, ECO:0000269|PubMed:9288754}.
CC -!- INDUCTION: Increased in dorsal root ganglia in response to injury
CC caused by dorsal rhizotomy (PubMed:28270793). Increased in dorsal root
CC ganglia in response to sciatic transection injury (PubMed:28270793).
CC Transiently increased in dorsal root ganglia in response to sciatic
CC nerve crush injury, returning to comparable levels 42 days post-injury
CC (PubMed:28270793). {ECO:0000269|PubMed:28270793}.
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; AF016297; AAC53338.1; -; mRNA.
DR RefSeq; NP_110496.1; NM_030869.3.
DR AlphaFoldDB; O35276; -.
DR SMR; O35276; -.
DR STRING; 10116.ENSRNOP00000047206; -.
DR GlyGen; O35276; 5 sites.
DR jPOST; O35276; -.
DR PaxDb; O35276; -.
DR PRIDE; O35276; -.
DR GeneID; 81527; -.
DR KEGG; rno:81527; -.
DR UCSC; RGD:621442; rat.
DR CTD; 8828; -.
DR RGD; 621442; Nrp2.
DR VEuPathDB; HostDB:ENSRNOG00000031232; -.
DR eggNOG; ENOG502QVB7; Eukaryota.
DR HOGENOM; CLU_015228_6_1_1; -.
DR InParanoid; O35276; -.
DR OMA; XYDFIEI; -.
DR OrthoDB; 124611at2759; -.
DR PhylomeDB; O35276; -.
DR Reactome; R-RNO-194306; Neurophilin interactions with VEGF and VEGFR.
DR PRO; PR:O35276; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000031232; Expressed in lung and 18 other tissues.
DR Genevisible; O35276; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017154; F:semaphorin receptor activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IEP:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:1904835; P:dorsal root ganglion morphogenesis; ISO:RGD.
DR GO; GO:0021612; P:facial nerve structural organization; ISO:RGD.
DR GO; GO:1903375; P:facioacoustic ganglion development; ISO:RGD.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:0021675; P:nerve development; ISO:RGD.
DR GO; GO:0001755; P:neural crest cell migration; ISO:RGD.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR GO; GO:1902285; P:semaphorin-plexin signaling pathway involved in neuron projection guidance; ISO:RGD.
DR GO; GO:0097374; P:sensory neuron axon guidance; ISO:RGD.
DR GO; GO:0061549; P:sympathetic ganglion development; ISO:RGD.
DR GO; GO:0097490; P:sympathetic neuron projection extension; ISO:RGD.
DR GO; GO:0097491; P:sympathetic neuron projection guidance; ISO:RGD.
DR GO; GO:0061551; P:trigeminal ganglion development; ISO:RGD.
DR GO; GO:0036486; P:ventral trunk neural crest cell migration; ISO:RGD.
DR GO; GO:0021649; P:vestibulocochlear nerve structural organization; ISO:RGD.
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 2: Evidence at transcript level;
KW Calcium; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Heparin-binding; Membrane; Metal-binding; Neurogenesis;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..925
FT /note="Neuropilin-2"
FT /id="PRO_0000021865"
FT TOPO_DOM 23..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..883
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 884..925
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 297..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 820..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..849
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 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 834
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"
SQ SEQUENCE 925 AA; 103897 MW; 3BF62903F644851C CRC64;
MDMFPLTWIF LALYFSGHKV RSQQDPPCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWVVY
APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSVL
YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL
AKPRMEIILQ FLTFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSKLRS
STGILSLTFH TDMAVAKDGF SARYYLVHQE PPENFQCNAP LGMESGRIAN EQISASSTFS
DGRWTPQQSR LHGDDNGWTP NVDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQKGYYVKS
YKLEVSTNGE DWMVYRHGKN HKVFQANNDA TELVLNKLHT PLLTRFIRIR PQTWHLGIAL
RLELFGCRVT DAPCSNMLGM LSGLIADTQI SASSTREYLW SPSAARLVSS RSGWFPRNPQ
AQPGEEWLQV DLGTPKTVKG VIIQGARGGD SITAMEARAF VRKFKVSYSL NGKDWEYIQD
PRTQQPKLFE GNMHYDTPDI RRFEPVPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT
VETLGPTVKS EETTTPYPMD EDATECGENC SFEDDKDLQL PSGFNCNFDF PEETCGWMYD
RAKWLQSTWI SSANPNDRTF PDDKNFLKLQ SDGGREGQFG RLISPPVHLP RSPVCMEFQY
QAMGGHGVAL QVVREARQES KLLWVIREDQ GSEWKHGRII LPSYDMEYQI VFEGVIGKGR
SGEISIDDIR ISTDVPLENC MEPISAFAVD IPEIHGGEGY EDEIDDDYEG DWNNSSSTSG
AGSPSSGKEK SWLYTLDPIL ITIIAMSSLG VLLGATCAGL LLYCTCSYSG LSSRSCTTLE
NYNFELYDGL KHKVKINHQK CCSEA
