ID Q5XH75_XENLA Unreviewed; 953 AA.
AC Q5XH75;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN Name=nrp1.S {ECO:0000313|Xenbase:XB-GENE-17335972};
GN Synonyms=LOC397804 {ECO:0000313|EMBL:AAH84198.1}, neuropilin
GN {ECO:0000313|RefSeq:NP_001081380.1}, np-1
GN {ECO:0000313|RefSeq:NP_001081380.1}, npn-1
GN {ECO:0000313|RefSeq:NP_001081380.1}, nrp
GN {ECO:0000313|RefSeq:NP_001081380.1}, nrp-1
GN {ECO:0000313|RefSeq:NP_001081380.1}, nrp1
GN {ECO:0000313|RefSeq:NP_001081380.1}, nrp1.L
GN {ECO:0000313|RefSeq:NP_001081380.1}, pNPG152
GN {ECO:0000313|RefSeq:NP_001081380.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH84198.1};
RN [1] {ECO:0000313|RefSeq:NP_001081380.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1908252; DOI=10.1016/0896-6273(91)90268-5;
RA Takagi S., Hirata T., Agata K., Mochii M., Eguchi G., Fujisawa H.;
RT "The A5 antigen, a candidate for the neuronal recognition molecule, has
RT homologies to complement components and coagulation factors.";
RL Neuron 7:295-307(1991).
RN [2] {ECO:0000313|RefSeq:NP_001081380.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [3] {ECO:0000313|EMBL:AAH84198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000313|EMBL:AAH84198.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001081380.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23739132;
RA Kita E.M., Bertolesi G.E., Hehr C.L., Johnston J., McFarlane S.;
RT "Neuropilin-1 biases dendrite polarization in the retina.";
RL Development 140:2933-2941(2013).
RN [5] {ECO:0000313|RefSeq:NP_001081380.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27974617; DOI=10.1523/jneurosci.2400-16.2016;
RA Hornberg H., Cioni J.M., Harris W.A., Holt C.E.;
RT "Hermes Regulates Axon Sorting in the Optic Tract by Post-Transcriptional
RT Regulation of Neuropilin 1.";
RL J. Neurosci. 36:12697-12706(2016).
RN [6] {ECO:0000313|RefSeq:NP_001081380.1}
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}.
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DR EMBL; BC084198; AAH84198.1; -; mRNA.
DR RefSeq; NP_001081380.1; NM_001087911.1.
DR DNASU; 397804; -.
DR GeneID; 397804; -.
DR KEGG; xla:397804; -.
DR AGR; Xenbase:XB-GENE-17335972; -.
DR AGR; Xenbase:XB-GENE-865400; -.
DR CTD; 397804; -.
DR Xenbase; XB-GENE-17335972; nrp1.S.
DR OrthoDB; 5293253at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 397804; Expressed in spleen and 14 other cell types or tissues.
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:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
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 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 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; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 2: Evidence at transcript level;
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:UP000186698};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001081380.1};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..953
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001081380.1"
FT /id="PRO_5033206607"
FT TRANSMEM 861..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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..584
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 649..812
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 624..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 27..54
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 82..104
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 147..173
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 206..228
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 275..424
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 431..584
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 953 AA; 106384 MW; 6B94CD3007AA60C8 CRC64;
MLLRLLSCCC WLLCSLRSSW ASRNDKCGDT IKITSPSYLT SAGYPHSYPP SQRCEWLIQA
PEHYQRIMIN FNPHFDLEDR ECKYDYVEVI DGDNANGQLL GKYCGKIAPS PLVSTGPSIF
IRFVSDYETP GAGFSIRYEV FKTGPECSRN FTSSNGVIKS PKYPEKYPNA LECTYIIFAP
KMQEIVLEFE SFELEADSNA PGGQTCRYDW LGIWDGFPGV GPHIGRYCGQ NTPGRVRSFT
GILSMIFHTD SAIAKEGFFA NFSVVQSNTD EDFQCKEPLG MESGEIHFDQ ISVSSQYSMN
WSAERSRLNY VENGWTPGED TVKEWIQVDL ENLRFVSGIG TQGAISKETK KKYFVKSYKV
DISSNGEDWI TLKDGNKHLV FTGNTDATDV VYRPFSKPVI TRFVRLRPVT WENGISLRFE
LYGCKITDYP CSRMLGMVSG LISDSQITAS SQVDRNWVPE LARLVTSRSG WALPPSNTHP
YTKEWLQIDL AEEKIVRGVI IQGGKHKENK VFMRKFKIGY SNNGTEWEMI MDSSKNKPKT
FEGNTNYDTP ELRTFAHITT RFIRIIPERA SASGLALRLE LLGCEVETPT SIPTTPEVNG
GDECEGDLAN CHSGTDEGFK LTVGATGQST ETPTVEASPE EPDMTHSDLD CKFGWGSQKT
VCNWQHDISS GLKWAVLNSK TGPVQDHTGD GNFIYSEADE RHEGRAARLM SPVVSSSRSA
HCLTFWYHMD GSHVGTLSIK LKYEMEEDFD QTLWTVSGNQ GDQWKEARVV LHKTMKQYQV
IVEGTVGKGS AGGIAVDDII IANHISPSQC RAPEIDDSAN KIGEEDSEID KTGSTPNYAL
NEFNESISKK PGNVLKTLDP ILITIIAMSA LGVLLGAICG VVLYCACWHN GMSERNLSAL
ENYNFELVDG VKLKKGQIKH TELIFRSMNL EEEYGGFFAD TLKRLQSIGI EGQ
//
