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Database: UniProt
Entry: A0A2K6AFP7_MANLE
LinkDB: A0A2K6AFP7_MANLE
Original site: A0A2K6AFP7_MANLE 
ID   A0A2K6AFP7_MANLE        Unreviewed;       662 AA.
AC   A0A2K6AFP7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Neuropilin 1 {ECO:0000313|Ensembl:ENSMLEP00000038886.1};
GN   Name=NRP1 {ECO:0000313|Ensembl:ENSMLEP00000038886.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000038886.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000038886.1}
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   AlphaFoldDB; A0A2K6AFP7; -.
DR   Ensembl; ENSMLET00000062500.1; ENSMLEP00000038886.1; ENSMLEG00000043411.1.
DR   GeneTree; ENSGT00940000157169; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0120035; P:regulation of plasma membrane bounded cell projection organization; IEA:UniProt.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00057; FA58C; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46806:SF4; NEUROPILIN-1; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00231; FA58C; 2.
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.
PE   4: Predicted;
KW   Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00059}; Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW   Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..662
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014368997"
FT   DOMAIN          27..141
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          147..265
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          275..424
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          431..583
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DISULFID        27..54
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ   SEQUENCE   662 AA;  74174 MW;  9E32C5DF8C2A8C59 CRC64;
     MEKGLPLLCT ALALALAPAG AFRNDKCGDT IKIESPGYLT SPGYPHSYHP SEKCEWLIQA
     PDPYQRIMIN FNPHFDLEDR DCKYDYVEVF DGENENGRLW GKFCGKIAPP PVVSSGQFLF
     IKFVSDYETH GAGFSIRYEI FKRGPECSQN YTTPSGVIKS PGFPEKYPNS LECTYIVFAP
     KMSEIILEFE SFDLEPDSNP PGGMFCRYDR LEIWDGFPDV GPHIGRYCGQ KTPGRIRSSS
     GILSMVFYTD SAIAKEGFSA NYSVLQSSVS EDFKCMEAVG MESGEIHSDQ ITASSQYSTN
     WSAERSRLNY PENGWTPGED SYREWIQVDL GLLRFVTAVG TQGAISKETK KKYYVKTYKI
     DVSSNGEDWI TIKEGNKPVL FQGNTNPTDV VVAVFPKPLI TRFVRIKPAT WETGISMRFE
     VYGCKITDYP CSGMLGMVSG LISDSQITSS NQGDRNWMPE NIRLVTSRSG WALPPAPHSY
     VNEWLQIDLG EEKIVRGIII QGGKHRENKV FMRKFKIGYS NNGSDWKMIM DDSKRKAKSF
     EGNNNYDTPE LRTFPALSTR FIRIYPERAT HGGLGLRMEL LGCEVEGTIN TDQECPCART
     LAKDAKKKKG WVDSIHCRCV RSIHRETWSS GKGVCSQDAK SVAWILEGDA HLGGGVNGGL
     KR
//
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