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
//