NRP1A_DANRE
ID NRP1A_DANRE Reviewed; 923 AA.
AC Q8QFX6; Q8AXP1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Neuropilin-1a;
DE Short=znrp1;
DE Flags: Precursor;
GN Name=nrp1a; Synonyms=np-1, nrp1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAL40862.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AB {ECO:0000269|PubMed:12142468};
RC TISSUE=Embryo {ECO:0000269|PubMed:12142468};
RX PubMed=12142468; DOI=10.1073/pnas.162366299;
RA Lee P., Goishi K., Davidson A.J., Mannix R., Zon L., Klagsbrun M.;
RT "Neuropilin-1 is required for vascular development and is a mediator of
RT VEGF-dependent angiogenesis in zebrafish.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10470-10475(2002).
RN [2] {ECO:0000312|EMBL:BAC53657.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shoji W., Tawarayama H.;
RT "The cloning and expression of neuropilin-1.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor involved in the development of the cardiovascular
CC system, in angiogenesis, in the formation of certain neuronal circuits
CC and in organogenesis outside the nervous system. It mediates the
CC chemorepulsant activity of semaphorins. Regulates angiogenesis through
CC a VEGF-dependent pathway. {ECO:0000250|UniProtKB:O14786,
CC ECO:0000269|PubMed:12142468}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Maternal transcripts are widely expressed until the early gastrula
CC stage, then become localized to the yolk syncytial layer. During
CC somatogenesis and later stages of development, expression occurs mainly
CC in neuronal and vascular tissues. {ECO:0000269|PubMed:12142468}.
CC -!- SIMILARITY: Belongs to the neuropilin family.
CC {ECO:0000255|RuleBase:RU003307, ECO:0000305}.
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DR EMBL; AY064213; AAL40862.1; -; mRNA.
DR EMBL; AB088776; BAC53657.1; -; mRNA.
DR AlphaFoldDB; Q8QFX6; -.
DR SMR; Q8QFX6; -.
DR STRING; 7955.ENSDARP00000105696; -.
DR PaxDb; Q8QFX6; -.
DR PRIDE; Q8QFX6; -.
DR ZFIN; ZDB-GENE-030519-2; nrp1a.
DR eggNOG; ENOG502QUEH; Eukaryota.
DR InParanoid; Q8QFX6; -.
DR PhylomeDB; Q8QFX6; -.
DR Reactome; R-DRE-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-DRE-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DRE-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-DRE-399956; CRMPs in Sema3A signaling.
DR PRO; PR:Q8QFX6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; IBA:GO_Central.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:ZFIN.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:InterPro.
DR GO; GO:0048675; P:axon extension; IMP:ZFIN.
DR GO; GO:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0007413; P:axonal fasciculation; IMP:ZFIN.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:0001775; P:cell activation; IMP:ZFIN.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IEA:InterPro.
DR GO; GO:0007508; P:larval heart development; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR GO; GO:0001755; P:neural crest cell migration; IMP:ZFIN.
DR GO; GO:0071678; P:olfactory bulb axon guidance; IMP:ZFIN.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IBA:GO_Central.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IGI:BHF-UCL.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; IGI:ZFIN.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IMP:ZFIN.
DR GO; GO:0001666; P:response to hypoxia; IDA:ZFIN.
DR GO; GO:0009611; P:response to wounding; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IGI:ZFIN.
DR GO; GO:0048538; P:thymus development; IMP:ZFIN.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001944; P:vasculature development; IMP:ZFIN.
DR GO; GO:0001570; P:vasculogenesis; IMP:ZFIN.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00057; FA58C; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.290; -; 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; IPR027146; NRP1.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806:SF4; PTHR46806:SF4; 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; SSF49785; SSF49785; 2.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Calcium; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Heparan sulfate; Heparin-binding; Membrane;
KW Metal-binding; Neurogenesis; Proteoglycan; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..923
FT /note="Neuropilin-1a"
FT /id="PRO_0000021857"
FT TOPO_DOM 20..856
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..923
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..139
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000305"
FT DOMAIN 145..263
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000305"
FT DOMAIN 273..422
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081,
FT ECO:0000305"
FT DOMAIN 429..581
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081,
FT ECO:0000305"
FT DOMAIN 642..811
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128,
FT ECO:0000305"
FT REGION 587..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 612
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 612
FT /note="O-linked (Xyl...) (heparan sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 25..52
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 80..102
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 145..171
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 204..226
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 273..422
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 429..581
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CONFLICT 230
FT /note="T -> S (in Ref. 2; BAC53657)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="K -> E (in Ref. 2; BAC53657)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="T -> S (in Ref. 2; BAC53657)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="L -> M (in Ref. 2; BAC53657)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="G -> D (in Ref. 2; BAC53657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 923 AA; 102493 MW; 2ED84B129AA92B2D CRC64;
MHCGLVLILF TGIFLIVSAL KNDKCGDNIR ITSANYLTSP GYPVSYYPSQ KCIWVITAPG
PNQRILINFN PHFDLEDREC KYDYVEVRDG VDENGQLVGK YCGKIAPSPV VSSGNQLFIK
FVSDYETHGA GFSIRYEIFK TGPECSRNFT SSSGVIKSPG FPEKYPNNLD CTFMIFAPKM
SEIVLEFESF ELEPDTQPPA GVFCRYDRLE IWDGFPGVGP YIGRYCGQNT PGRIISYTGT
LAMTINTDSA IAKEGFSANF TVLERTVPDD FDCTEPLGME TGEIHSDQIM ASSQYSNSWS
AERSRLNNPE NGWTPLKDTN KEWIQVDLGF LRFVSAIGTQ GAISQETKKK YYVKEYKVDV
SSNGEDWITI KDGPKQKLFQ GNTNPTDVVK AKFPKPTLTR YLRIRPINWE TGIALRFEVY
GCKISEYPCS GMLGMVSGLI TDSQITVSSH IERTWVSENA RLLTSRSGWM LLPQSQPYAD
EWLQIDLAEE KLVKGLIIQG GKHRDNKVFM KKFRLGYSNN GSDWKLVMDA TGNKPKIFEG
NLNYDTPALR TMEPVLTRFV RIYPDRGTPA GMGLRLELLG CEMEVPTVPP TTPAASTTPS
DECDDDQANC HSGTGDGYDQ TGGTTATETI REMSTIPAFL WFACDFGWAN DPSFCGWISE
DSGFRWQIQS SGTPTLNTGP NMDHTGGSGN FIYTLATGAQ ETEVARLVSP SVSGQDSDLC
LSFWYHMFGS HIGTLHIKQR RETSQGSADV LLWTVSGHQG NRWREGRVLI PHSNKPYQVI
IESVVERKSW GDIAVDDIKI LDNVNMADCK DPDVPAEPIQ PEDNFNEIMV DITDFPDIVE
NPDIGGAGNM LKTLDPILIT IIAMSALGVF LGAICGVVLY CACSHSGMSD RNLSALENYN
FELVDGVKLK KDKLNSQNSY SEA
