ID G3U7N0_LOXAF Unreviewed; 931 AA.
AC G3U7N0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN Name=NRP2 {ECO:0000313|Ensembl:ENSLAFP00000023838.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000023838.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000023838.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023838.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000023838.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023838.1};
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_010600644.1; XM_010602342.1.
DR AlphaFoldDB; G3U7N0; -.
DR STRING; 9785.ENSLAFP00000023838; -.
DR Ensembl; ENSLAFT00000034420.1; ENSLAFP00000023838.1; ENSLAFG00000016414.3.
DR GeneID; 100660452; -.
DR KEGG; lav:100660452; -.
DR CTD; 8828; -.
DR eggNOG; ENOG502QVB7; Eukaryota.
DR GeneTree; ENSGT00940000155270; -.
DR HOGENOM; CLU_015228_6_1_1; -.
DR InParanoid; G3U7N0; -.
DR OMA; XYDFIEI; -.
DR OrthoDB; 5293253at2759; -.
DR TreeFam; TF316506; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000007646};
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..931
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003456389"
FT TRANSMEM 865..890
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 299..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..851
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: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 931 AA; 104958 MW; 351B9F9F65B1BF8B CRC64;
MDMFSLIWVF LALYYSGQEV RGQPDPSCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWIVY
APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSVL
YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL
AKPKMEIVLQ FLTFDLEHDP LQVGEGDCKY DWLDIWDGIQ HVGPLIGKYC GTKTPSELRS
STGILSLTFH TDMAVAKDGF SARYYLVQQE PLENFQCNVP LGMESGRIAN EQISASSTYS
DRRWTPQQSR LHGDDNGWTP NLDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQNGYYVKS
YKLEVSTNGE DWMMYRHGKN HKVFQANNDA TEVVLNKLHM PLLTRFVRIR PQTWHSGIAL
RLELFGCRVT DAPCSNMLGM LSGLIADSQI SASSTREYLW NPSVARLVSS RSGWFPRIPQ
AQPGEEWLQV DLGAPKMVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGKDWEYIQD
PRILQPKLFE GNMHYDTPDI RRFDPVPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSRPT
VETLGPTMKS EETTTPYPID EEATECGENC SFEDDKELQL PSGFNCNFDF PEESCGWMYD
HAKWLRSTWT GSSSPNDRTF PDDKNFLKLQ NDGRREGQYA RLVSPPVHLP RSPVCMEFQY
QATGSQGVTL QVVREARQES KLLWVIREDQ GSEWKHGRLI LPSYDMEYQI VFEGVIGKGR
SGEIAIDDIR ISTDVPLENC MEPISAFAGE NFQVDIPEIH GRGGYDEEID DEYDMDWSNS
SSPTSGSGVS SANKEKSWLY TLDPILITII AMSSLGVLLG ATCAGLLLYC TCSYSGLSSR
SCTTLENYNF ELYDGLKHKV KMNHQKCCSE A
//
