NET3_HUMAN
ID NET3_HUMAN Reviewed; 580 AA.
AC O00634;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Netrin-3;
DE AltName: Full=Netrin-2-like protein;
DE Flags: Precursor;
GN Name=NTN3; Synonyms=NTN2L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8828041; DOI=10.1101/gr.6.6.525;
RA Burn T.C., Connors T.D., Van Raay T.J., Dackowski W.R., Millholland J.M.,
RA Klinger K.W., Landes G.M.;
RT "Generation of a transcriptional map for a 700-kb region surrounding the
RT polycystic kidney disease type 1 (PKD1) and tuberous sclerosis type 2
RT (TSC2) disease genes on human chromosome 16p3.3.";
RL Genome Res. 6:525-537(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9143507; DOI=10.1006/geno.1997.4659;
RA Van Raay T.J., Foskett S.M., Connors T.D., Klinger K.W., Landes G.M.,
RA Burn T.C.;
RT "The NTN2L gene encoding a novel human netrin maps to the autosomal
RT dominant polycystic kidney disease region on chromosome 16p13.3.";
RL Genomics 41:279-282(1997).
CC -!- FUNCTION: Netrins control guidance of CNS commissural axons and
CC peripheral motor axons. {ECO:0000250}.
CC -!- INTERACTION:
CC O00634; Q8NBI3: DRAXIN; NbExp=2; IntAct=EBI-10831998, EBI-10827752;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Spinal cord. {ECO:0000269|PubMed:9143507}.
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DR EMBL; U86759; AAC51247.1; -; mRNA.
DR EMBL; U86758; AAC51246.1; -; Genomic_DNA.
DR CCDS; CCDS10469.1; -.
DR RefSeq; NP_006172.1; NM_006181.2.
DR AlphaFoldDB; O00634; -.
DR SMR; O00634; -.
DR BioGRID; 110972; 4.
DR IntAct; O00634; 1.
DR STRING; 9606.ENSP00000293973; -.
DR GlyConnect; 1543; 1 N-Linked glycan (1 site).
DR GlyGen; O00634; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O00634; -.
DR PhosphoSitePlus; O00634; -.
DR BioMuta; NTN3; -.
DR jPOST; O00634; -.
DR MassIVE; O00634; -.
DR PaxDb; O00634; -.
DR PeptideAtlas; O00634; -.
DR PRIDE; O00634; -.
DR ProteomicsDB; 48004; -.
DR Antibodypedia; 66015; 89 antibodies from 20 providers.
DR DNASU; 4917; -.
DR Ensembl; ENST00000293973.2; ENSP00000293973.1; ENSG00000162068.2.
DR GeneID; 4917; -.
DR KEGG; hsa:4917; -.
DR MANE-Select; ENST00000293973.2; ENSP00000293973.1; NM_006181.3; NP_006172.1.
DR UCSC; uc002cqj.3; human.
DR CTD; 4917; -.
DR DisGeNET; 4917; -.
DR GeneCards; NTN3; -.
DR HGNC; HGNC:8030; NTN3.
DR HPA; ENSG00000162068; Tissue enriched (brain).
DR MIM; 602349; gene.
DR neXtProt; NX_O00634; -.
DR OpenTargets; ENSG00000162068; -.
DR PharmGKB; PA164724231; -.
DR VEuPathDB; HostDB:ENSG00000162068; -.
DR eggNOG; KOG3512; Eukaryota.
DR GeneTree; ENSGT00940000153882; -.
DR HOGENOM; CLU_018213_2_0_1; -.
DR InParanoid; O00634; -.
DR OMA; SHCRPAR; -.
DR OrthoDB; 858946at2759; -.
DR PhylomeDB; O00634; -.
DR TreeFam; TF352481; -.
DR PathwayCommons; O00634; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; O00634; -.
DR SIGNOR; O00634; -.
DR BioGRID-ORCS; 4917; 8 hits in 1063 CRISPR screens.
DR GenomeRNAi; 4917; -.
DR Pharos; O00634; Tbio.
DR PRO; PR:O00634; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O00634; protein.
DR Bgee; ENSG00000162068; Expressed in pancreatic ductal cell and 36 other tissues.
DR Genevisible; O00634; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; NAS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 3.
DR Gene3D; 2.40.50.120; -; 1.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF00055; Laminin_N; 1.
DR Pfam; PF01759; NTR; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS51117; LAMININ_NTER; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..580
FT /note="Netrin-3"
FT /id="PRO_0000017085"
FT DOMAIN 36..254
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 255..308
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 311..371
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 374..421
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 441..577
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 62..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 500..502
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..125
FT /evidence="ECO:0000250"
FT DISULFID 255..264
FT /evidence="ECO:0000250"
FT DISULFID 257..274
FT /evidence="ECO:0000250"
FT DISULFID 276..285
FT /evidence="ECO:0000250"
FT DISULFID 288..308
FT /evidence="ECO:0000250"
FT DISULFID 311..320
FT /evidence="ECO:0000250"
FT DISULFID 313..338
FT /evidence="ECO:0000250"
FT DISULFID 341..350
FT /evidence="ECO:0000250"
FT DISULFID 353..371
FT /evidence="ECO:0000250"
FT DISULFID 374..386
FT /evidence="ECO:0000250"
FT DISULFID 376..393
FT /evidence="ECO:0000250"
FT DISULFID 395..404
FT /evidence="ECO:0000250"
FT DISULFID 407..421
FT /evidence="ECO:0000250"
FT DISULFID 441..514
FT /evidence="ECO:0000250"
FT DISULFID 460..577
FT /evidence="ECO:0000250"
FT VARIANT 425
FT /note="P -> S (in dbSNP:rs34818219)"
FT /id="VAR_050086"
SQ SEQUENCE 580 AA; 61466 MW; 15F99643E74C644C CRC64;
MPGWPWGLLL TAGTLFAALS PGPPAPADPC HDEGGAPRGC VPGLVNAALG REVLASSTCG
RPATRACDAS DPRRAHSPAL LTSPGGTASP LCWRSESLPR APLNVTLTVP LGKAFELVFV
SLRFCSAPPA SVALLKSQDH GRSWAPLGFF SSHCDLDYGR LPAPANGPAG PGPEALCFPA
PLAQPDGSGL LAFSMQDSSP PGLDLDSSPV LQDWVTATDV RVVLTRPSTA GDPRDMEAVV
PYSYAATDLQ VGGRCKCNGH ASRCLLDTQG HLICDCRHGT EGPDCGRCKP FYCDRPWQRA
TARESHACLA CSCNGHARRC RFNMELYRLS GRRSGGVCLN CRHNTAGRHC HYCREGFYRD
PGRALSDRRA CRACDCHPVG AAGKTCNQTT GQCPCKDGVT GLTCNRCAPG FQQSRSPVAP
CVKTPIPGPT EDSSPVQPQD CDSHCKPARG SYRISLKKFC KKDYAVQVAV GARGEARGAW
TRFPVAVLAV FRSGEERARR GSSALWVPAG DAACGCPRLL PGRRYLLLGG GPGAAAGGAG
GRGPGLIAAR GSLVLPWRDA WTRRLRRLQR RERRGRCSAA
