ID G7PL91_MACFA Unreviewed; 891 AA.
AC G7PL91;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN Name=NRP2 {ECO:0000313|Ensembl:ENSMFAP00000043710.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000043710.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000043710.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000043710.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; G7PL91; -.
DR STRING; 9541.ENSMFAP00000043710; -.
DR Ensembl; ENSMFAT00000018000.2; ENSMFAP00000043710.2; ENSMFAG00000038385.2.
DR VEuPathDB; HostDB:ENSMFAG00000038385; -.
DR eggNOG; ENOG502QVB7; Eukaryota.
DR GeneTree; ENSGT00940000155270; -.
DR OrthoDB; 5293253at2759; -.
DR Proteomes; UP000233100; Chromosome 12.
DR Bgee; ENSMFAG00000038385; Expressed in lung and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
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; 1.
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; 1.
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; 1.
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; 1.
DR PROSITE; PS01180; CUB; 1.
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:UP000233100};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 825..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 115..233
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 243..393
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 400..558
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 610..768
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 115..141
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 174..196
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 243..393
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 400..558
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 891 AA; 99173 MW; 502D5835B4445681 CRC64;
MLAISPLPVT PRTTPPTRTA SGLFTPPNPT RRLSSTSTLT LKSRSMTASM TLSRFGMGTV
NPQTSWANTV GTSPRPPSSP RAPCSTSSSP PTTPGRGQAS LCATRSSRQV SSEDCSKNFT
SPNGTIESPG FPEKYPHNLD CTFTILAKPK MEIVLQFLIF DLEHDPLQVG EGDCKYDWLD
IWDGIPHVGP LIGKYCGTKT PSELRSSTGI LSLTFHTDMA VAKDGFSARY YLVHQEPLEN
FQCNVPLGME SGRIANEQIS ASSTYSDGRW TPQQSRLHGD DNGWTPNLDS NKEYLQVDLR
FLTMLTAIAT QGAISRETQN GYYVKSYKLE VSTNGEDWMV YRHGKNHKVF QANNDATEVV
LNKLHAPLLT RFVRIRPQTW HSGIALRLEL FGCRVTDAPC SNMLGMLSGL IADSQISASS
THEYLWSPSA ARLVSSRAGW FPRIPQAQPG EEWLQVDLGT PKTVKGVIIQ GARGGDSITA
VEARAFVRKF KVSYSLNGKD WEYIQDPRTQ QPKLFEGNMH YDTPDIRRFD PVPAQYVRVY
PERWSPAGIG MRLEVLGCDW TDSKPTVETL GPTVKSEETT TPYPTDEEAT ECGENCSFED
DKDLQLPSGF NCNFDFPEEP CGWMYDHAKW LRTTWASSSS PNDRTFPDDR NFLRLQSDSR
REGQYARLIS PPVHLPQSPV CMEFQYQATG GRGVALQVVR EASQESKLLW VIREDQGGEW
KHGRIILPSY DMEYQIVFEG VIGKGRSGEI AIDDIRISTD VPLENCMEPI SAFAVDIPEI
HEREGYEDEI DDEYEVDWSN SSATSGSGAP STDKEKSWLY TLDPILITII AMSSLGVLLG
ATCAGLLLYC TCSYSGLSSR SCTTLENYNF ELYDGLKHKV KMNHQKCCSE A
//
