ID H3CRB2_TETNG Unreviewed; 938 AA.
AC H3CRB2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN Name=NRP1 {ECO:0000313|Ensembl:ENSTNIP00000010796.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000010796.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000010796.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
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DR AlphaFoldDB; H3CRB2; -.
DR STRING; 99883.ENSTNIP00000010796; -.
DR Ensembl; ENSTNIT00000010977.1; ENSTNIP00000010796.1; ENSTNIG00000007974.1.
DR GeneTree; ENSGT00940000157169; -.
DR InParanoid; H3CRB2; -.
DR OMA; GVMIQGG; -.
DR TreeFam; TF316506; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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 GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
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:SF4; NEUROPILIN-1; 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 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 Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
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 Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
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};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Receptor {ECO:0000256|PIRNR:PIRNR036960};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..938
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003582417"
FT TRANSMEM 872..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..135
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 141..259
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 272..421
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 428..580
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 671..845
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 21..48
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 76..98
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 141..167
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 200..222
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 272..421
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 428..580
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 938 AA; 102529 MW; 35D16EE2D423001A CRC64;
WLLFLLGQVL AAASLALTDK CGGEIEIHDA DYLTSPGYPG AYPPSQQCVW VITAPEPGQK
ILINFNPHFD LEDRDCKYDY VEVYNGGDER APMLGKFCGK IAPSPIISTG GQLLIKFVSD
YETHGAGFSV RYEVFKTGPE CSTNFTAPRG VIKTPGFPEK YPNNLECTFM IFAPQMSEIL
LEFQSFDMES DPTPPSGAVC RYDWLEIWDG FPAVGPHIGR YCGLASPGRV TSYTGILSMT
ITTDNAIARE GFSASYTIRE RSLPHEDQEF ICMEPLGMES GQISAQQIKA SSQYNSNWSP
ERSRLNYHEN GWTPSDDTVR EWIQVDLGFL RFVTAIGTQG AISKETKKHY FVRSYRVDVS
STGEDWVTVK DNSKQKIFQG NHNPTDVAVA FLPKQTLARY VRIRPLTWEQ GICMRFEIYG
CRTSDYPCSG MLGMVSGQIS DAQISVSSSA DRGWVAENAR LLTGRTGWTG QQAKQPFRNE
WIQVDLGQEK MLSGVMIQGG KHRDKNVFVK KFRVGHSLDG EDWAMVREDN GTRPKIFSGN
QNHDTPELRL VAAVRTRFVR IYPDRATAEG LGLRLELTGC DLDGFLPDSD LITTAPPTTA
AASTLPVTTY GVTTAAPTAV PTTPAVTDCE DGHLGCGGET EAPYDYDATT GGAAVTEPNL
DFIPAAAYIW FACNFDFSSY CGWTAEPGKG ATWLIHPGGA SAGHRGPTFN HTGGRGNFVY
VQLSKREPPG GTGEDEDGDK VARLASVPIP APDSHLCMSF WYHMLGEHAG ALHVNLRTEA
EGTQVLWTVR GHQGSQWKEG RVLLPPAKVS YQVILEGVAD KRSPAHIAVD NIQIMDGLAD
DECTVSAAMD SLSQDTSELS GPGNMLKTLD PILITIIAMS ALGVVLGAVC GVVLYCACSQ
GSMSDRNLSA LENYNFELVD GVKLKKDKMN GQTNYSEA
//
