ID M3XMY2_MUSPF Unreviewed; 926 AA.
AC M3XMY2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN Name=NRP2 {ECO:0000313|Ensembl:ENSMPUP00000000432.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000432.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000000432.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the neuropilin family.
CC {ECO:0000256|ARBA:ARBA00006078, ECO:0000256|PIRNR:PIRNR036960}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; AEYP01060516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004764272.1; XM_004764215.2.
DR AlphaFoldDB; M3XMY2; -.
DR STRING; 9669.ENSMPUP00000000432; -.
DR Ensembl; ENSMPUT00000000440.1; ENSMPUP00000000432.1; ENSMPUG00000000435.1.
DR GeneID; 101691628; -.
DR CTD; 8828; -.
DR eggNOG; ENOG502QVB7; Eukaryota.
DR GeneTree; ENSGT00940000155270; -.
DR HOGENOM; CLU_015228_6_1_1; -.
DR InParanoid; M3XMY2; -.
DR OMA; XYDFIEI; -.
DR OrthoDB; 5293253at2759; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:1904835; P:dorsal root ganglion morphogenesis; IEA:Ensembl.
DR GO; GO:0021612; P:facial nerve structural organization; IEA:Ensembl.
DR GO; GO:1903375; P:facioacoustic ganglion development; IEA:Ensembl.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IEA:Ensembl.
DR GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IEA:Ensembl.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR GO; GO:0097374; P:sensory neuron axon guidance; IEA:Ensembl.
DR GO; GO:0061549; P:sympathetic ganglion development; IEA:Ensembl.
DR GO; GO:0097490; P:sympathetic neuron projection extension; IEA:Ensembl.
DR GO; GO:0097491; P:sympathetic neuron projection guidance; IEA:Ensembl.
DR GO; GO:0061551; P:trigeminal ganglion development; IEA:Ensembl.
DR GO; GO:0036486; P:ventral trunk neural crest cell migration; IEA:Ensembl.
DR GO; GO:0021649; P:vestibulocochlear nerve structural organization; IEA:Ensembl.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00057; FA58C; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 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; IPR022579; Neuropilin_C.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46806:SF2; NEUROPILIN-2; 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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
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 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR036960};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|PIRNR:PIRNR036960};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782,
KW ECO:0000256|PIRNR:PIRNR036960};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR036960-2};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR036960};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036960-1};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902,
KW ECO:0000256|PIRNR:PIRNR036960}; Receptor {ECO:0000256|PIRNR:PIRNR036960};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..926
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004043670"
FT TRANSMEM 860..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..142
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 149..267
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 277..427
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 434..592
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 644..802
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 297..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 28..55
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 83..105
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 149..175
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 208..230
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 277..427
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 434..592
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 926 AA; 104158 MW; 23F13D8A123BE4AD CRC64;
MDMFPLTWVF LALYFSGPEV RGQPDSPCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWIVY
APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSVL
YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL
AKPKMEIILQ FLTFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSELRS
STGILSLTFH TDMAVAKDGF SARYYLIHQD PPENFQCNVP LGMESGRIAN EQISASSTYS
DERWTPQQSR LHGEDNGWTP NLDSSKEYLQ VDLRFLTILT AIATQGAISR ETQNGYYVKS
YKLEVSTNGE DWMVYRHGKN HKVFQANNDA SEVVLNKLHM PLLTRFVRIR PQTWHSGIAL
RLELFGCRVT DAPCSNMLGM LSGLIPDSQI SASSTREYLW SPSAARLVSS RSGWFPRIPQ
AQPGEEWLQV DLGVPKTVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGRDWEYIQD
PRTQQPKLFE GNMHYDTPDI RRFDPVPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT
VETLGPTVKS EETTTPYPIE EEATECGENC SFEDDKDLQL PSGFNCNFDF PEEPCGWMYD
HAKWLRSTWP GSSSPNDRTF PDDRNFLRLQ SDGRREGQYA RLISPPVHLP RSPVCMEFQY
QATGGRGVAL QVVREASQES KLLWVIREDQ GDEWKHGRII LPSYDMEYQI VFEGVIGKGR
SGEIAIDDIR ISTDVPLENC MEPISAFAVD IPEIHGREGY EDEIDDEYEV DWSNSSSPTS
GSGAPSADKE KSWLYTLDPI LITIIAMSSL GVLLGATCAG LLLYCTCSYS GLSSRSCTTL
ENYNFELYDG LKHKVKMNHQ KCCSEA
//
