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Database: UniProt
Entry: A0A2K5X335_MACFA
LinkDB: A0A2K5X335_MACFA
Original site: A0A2K5X335_MACFA 
ID   A0A2K5X335_MACFA        Unreviewed;       901 AA.
AC   A0A2K5X335;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN   Name=NRP2 {ECO:0000313|Ensembl:ENSMFAP00000043682.2};
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:ENSMFAP00000043682.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000043682.2, 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:ENSMFAP00000043682.2}
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   RefSeq; XP_005574088.1; XM_005574031.2.
DR   AlphaFoldDB; A0A2K5X335; -.
DR   Ensembl; ENSMFAT00000017972.2; ENSMFAP00000043682.2; ENSMFAG00000038385.2.
DR   GeneID; 102121366; -.
DR   CTD; 8828; -.
DR   VEuPathDB; HostDB:ENSMFAG00000038385; -.
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-KW.
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; 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; 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; 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|PIRNR:PIRNR036960, ECO:0000256|PIRSR:PIRSR036960-1};
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|PIRSR:PIRSR036960-1};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902,
KW   ECO:0000256|PIRNR:PIRNR036960};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR036960};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..901
FT                   /note="Neuropilin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030052546"
FT   TRANSMEM        831..854
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          298..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..620
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   901 AA;  101316 MW;  8A1199B2F1129422 CRC64;
     MDMFPLTWVF LALYFSRHQV RGQPDPPCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWIVY
     APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSML
     YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL
     AKPKMEIVLQ FLIFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSELRS
     STGILSLTFH TDMAVAKDGF SARYYLVHQE PLENFQCNVP LGMESGRIAN EQISASSTYS
     DGRWTPQQSR LHGDDNGWTP NLDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQNGYYVKS
     YKLEVSTNGE DWMVYRHGKN HKVFQANNDA TEVVLNKLHA PLLTRFVRIR PQTWHSGIAL
     RLELFGCRVT DAPCSNMLGM LSGLIADSQI SASSTHEYLW SPSAARLVSS RAGWFPRIPQ
     AQPGEEWLQV DLGTPKTVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGKDWEYIQD
     PRTQQPKLFE GNMHYDTPDI RRFDPVPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT
     VETLGPTVKS EETTTPYPTD EEATECGENC SFEDDKDLQL PSGFNCNFDF PEEPCGWMYD
     HAKWLRTTWA SSSSPNDRTF PDDRNFLRLQ SDSRREGQYA RLISPPVHLP QSPVCMEFQY
     QATGGRGVAL QVVREASQES KLLWVIREDQ GGEWKHGRII LPSYDMEYQI VFEGVIGKGR
     SGEIAIDDIR ISTDVPLENC MEPISAFAGG TLLPGTEPTV DTVPMQPIPA YWYYVMAAGG
     AVLVLVSVAL ALVLHYHRFR YAAKKTDHSI TYKTSHYTNG APLAVEPTLT IKLEQDRGSH
     C
//
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