ID A0A1U7S1M9_ALLSI Unreviewed; 935 AA.
AC A0A1U7S1M9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN Name=NRP2 {ECO:0000313|RefSeq:XP_006029609.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006029609.1};
RN [1] {ECO:0000313|RefSeq:XP_006029609.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006029609.1; XM_006029547.2.
DR AlphaFoldDB; A0A1U7S1M9; -.
DR GeneID; 102384452; -.
DR CTD; 8828; -.
DR OrthoDB; 5293253at2759; -.
DR Proteomes; UP000189705; Unplaced.
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; 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:UP000189705};
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..935
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010529360"
FT TRANSMEM 869..894
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 642..806
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 297..319
FT /note="Disordered"
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 935 AA; 104613 MW; 3461F30B44A0BDA1 CRC64;
MDTLPLVWGL LALGLCGAGV LGEAVQSCGG RLNSKDAGYI TSPGYPQDYP SHQNCEWVIY
APESNQKIIL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSSL
YIKFTSDYAR QGAGFSLRYE IYKTGSEDCS RNFTSTNGTI ESPGFPDKYP HNLDCTFTIV
AKPKMEIILQ FLTFDLEHDP LQIGEGDCKY DWLDIWDGIP QVGPLIGRYC GTKTPSEIRS
TTGILSLTFH TDLAVAKDGF SARYYLVQQE IPDNFQCNIP LGMESGRISN EQISASSTYS
DGRWTPQQSR LNSDDNGWTP NVDSNKEYLQ VDLRFLTVLT AIATQGAISR ETQNGYYVHS
YKLEVSTNGE DWMMFRHGKN HKIFQANTDA TEVVLNKIHS PVLTRFVRIR PQTWHNGIAL
RLELYGCRIT DSPCSNMLGM LSGLISDSQI SASSIRGYEW LPSIARLVSS RSGWFPRIPQ
AQPGEEWLQV DLGVPKSVKG VIIQGARGGD SITMTDARSF VKKFKVSYSL NGRDWEYILD
TKTMQPKLFE GNMHYDIPEV RRFDPVPAQY IRVHPERWSP AGIGMRLEVL GCDWTDVRPT
SETLKPTLKS EETTTPYPID EETTECGDGC GESDDSQLPA GFNCNFDLPE DLCGWSLDSA
TGDVWSFHSR NTWIDNSEPS TGSLPDGKDY LWLQSSGRRE GRHARLISPP VHLPRSAMCM
VFQYQASGGN GVMLQVWREA SQENKPLWVI TEDHGEEWRE GRIILPSYDM VYQIVFEGVI
RKGYSGAIAI DDIRIATDVS LENCMEPITA FPVDFPRFND FAIPGQGIGE NFDDDYFGLD
KNNTLFSTNS PITPKLDKDK SWLYTLDPIL VTIIAMSSLG VLLGAICAGL LLYCTCSYTG
LSSRSSTTLE NYNFELYDGI KHKVKMNHQK CCSEA
//
