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Database: UniProt
Entry: O09118
LinkDB: O09118
Original site: O09118 
ID   NET1_MOUSE              Reviewed;         604 AA.
AC   O09118; B1ARR0; Q60832; Q9QY50;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   10-APR-2019, entry version 164.
DE   RecName: Full=Netrin-1;
DE   Flags: Precursor;
GN   Name=Ntn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Embryonic brain;
RX   PubMed=8978605; DOI=10.1016/S0092-8674(00)81795-X;
RA   Serafini T., Colamarino S.A., Leonardo E.D., Wang H., Beddington R.,
RA   Skarnes W.C., Tessier-Lavigne M.;
RT   "Netrin-1 is required for commissural axon guidance in the developing
RT   vertebrate nervous system.";
RL   Cell 87:1001-1014(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10381568; DOI=10.1016/S0925-4773(99)00035-0;
RA   Pueschel A.W.;
RT   "Divergent properties of mouse netrins.";
RL   Mech. Dev. 83:65-75(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 352-398, AND SUBCELLULAR LOCATION.
RX   PubMed=7604039; DOI=10.1073/pnas.92.14.6592;
RA   Skarnes W.C., Moss J.E., Hurtley S.M., Beddington R.S.;
RT   "Capturing genes encoding membrane and secreted proteins important for
RT   mouse development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6592-6596(1995).
RN   [7]
RP   INTERACTION WITH DSCAM.
RX   PubMed=18585357; DOI=10.1016/j.cell.2008.05.030;
RA   Ly A., Nikolaev A., Suresh G., Zheng Y., Tessier-Lavigne M., Stein E.;
RT   "DSCAM is a netrin receptor that collaborates with DCC in mediating
RT   turning responses to netrin-1.";
RL   Cell 133:1241-1254(2008).
RN   [8]
RP   INTERACTION WITH APP.
RX   PubMed=27068745; DOI=10.1074/jbc.M115.698092;
RA   Hashimoto Y., Toyama Y., Kusakari S., Nawa M., Matsuoka M.;
RT   "An Alzheimer Disease-linked Rare Mutation Potentiates Netrin Receptor
RT   Uncoordinated-5C-induced Signaling That Merges with Amyloid beta
RT   Precursor Protein Signaling.";
RL   J. Biol. Chem. 291:12282-12293(2016).
RN   [9]
RP   FUNCTION.
RX   PubMed=28483977; DOI=10.1523/JNEUROSCI.2617-16.2017;
RA   Shao Q., Yang T., Huang H., Alarmanazi F., Liu G.;
RT   "Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates
RT   Netrin-1 Repulsion.";
RL   J. Neurosci. 37:5620-5633(2017).
CC   -!- FUNCTION: Netrins control guidance of CNS commissural axons and
CC       peripheral motor axons. Its association with either DCC or some
CC       UNC5 receptors will lead to axon attraction or repulsion,
CC       respectively. Binding to UNC5C might cause dissociation of UNC5C
CC       from polymerized TUBB3 in microtubules and thereby lead to
CC       increased microtubule dynamics and axon repulsion
CC       (PubMed:28483977). Involved in dorsal root ganglion axon
CC       projection towards the spinal cord (PubMed:28483977). It also
CC       serves as a survival factor via its association with its receptors
CC       which prevent the initiation of apoptosis. Involved in colorectal
CC       tumorigenesis by regulating apoptosis (By similarity).
CC       {ECO:0000250|UniProtKB:O95631, ECO:0000269|PubMed:10381568,
CC       ECO:0000269|PubMed:28483977, ECO:0000269|PubMed:8978605}.
CC   -!- SUBUNIT: Binds to its receptors; DCC, UNC5A, UNC5B, UNC5C and
CC       probably UNC5D (By similarity). Binds to its receptor; DSCAM
CC       (PubMed:18585357). Interacts with APP (PubMed:27068745).
CC       {ECO:0000250|UniProtKB:O95631, ECO:0000269|PubMed:18585357,
CC       ECO:0000269|PubMed:27068745}.
CC   -!- INTERACTION:
CC       Q8K1S3-1:Unc5b; NbExp=4; IntAct=EBI-1798844, EBI-11658250;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:7604039}.
CC   -!- TISSUE SPECIFICITY: In the embryo, widely expressed in the
CC       developing nervous system and in mesodermal tissues.
CC       {ECO:0000269|PubMed:10381568}.
DR   EMBL; U65418; AAC52971.1; -; mRNA.
DR   EMBL; AF128865; AAD28602.1; -; mRNA.
DR   EMBL; AL669842; CAI24775.1; -; Genomic_DNA.
DR   EMBL; AL606831; CAI24775.1; JOINED; Genomic_DNA.
DR   EMBL; AL662894; CAI24775.1; JOINED; Genomic_DNA.
DR   EMBL; AL606831; CAI25691.1; -; Genomic_DNA.
DR   EMBL; AL662894; CAI25691.1; JOINED; Genomic_DNA.
DR   EMBL; AL669842; CAI25691.1; JOINED; Genomic_DNA.
DR   EMBL; AL662894; CAI25793.1; -; Genomic_DNA.
DR   EMBL; AL606831; CAI25793.1; JOINED; Genomic_DNA.
DR   EMBL; AL669842; CAI25793.1; JOINED; Genomic_DNA.
DR   EMBL; CH466601; EDL10446.1; -; Genomic_DNA.
DR   EMBL; BC141294; AAI41295.1; -; mRNA.
DR   EMBL; U23505; AAA87938.1; -; mRNA.
DR   CCDS; CCDS24864.1; -.
DR   RefSeq; NP_032770.2; NM_008744.2.
DR   UniGene; Mm.39095; -.
DR   PDB; 4OVE; X-ray; 2.64 A; A=23-457.
DR   PDBsum; 4OVE; -.
DR   ProteinModelPortal; O09118; -.
DR   SMR; O09118; -.
DR   IntAct; O09118; 4.
DR   STRING; 10090.ENSMUSP00000104314; -.
DR   PhosphoSitePlus; O09118; -.
DR   MaxQB; O09118; -.
DR   PaxDb; O09118; -.
DR   PeptideAtlas; O09118; -.
DR   PRIDE; O09118; -.
DR   Ensembl; ENSMUST00000021284; ENSMUSP00000021284; ENSMUSG00000020902.
DR   Ensembl; ENSMUST00000108674; ENSMUSP00000104314; ENSMUSG00000020902.
DR   GeneID; 18208; -.
DR   KEGG; mmu:18208; -.
DR   UCSC; uc007jnm.1; mouse.
DR   CTD; 9423; -.
DR   MGI; MGI:105088; Ntn1.
DR   eggNOG; KOG3512; Eukaryota.
DR   eggNOG; ENOG410XS7U; LUCA.
DR   GeneTree; ENSGT00940000153882; -.
DR   HOGENOM; HOG000286017; -.
DR   HOVERGEN; HBG006464; -.
DR   InParanoid; O09118; -.
DR   KO; K06843; -.
DR   OMA; DQFLWVR; -.
DR   OrthoDB; 858946at2759; -.
DR   TreeFam; TF352481; -.
DR   Reactome; R-MMU-373752; Netrin-1 signaling.
DR   Reactome; R-MMU-418885; DCC mediated attractive signaling.
DR   PRO; PR:O09118; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020902; Expressed in 281 organ(s), highest expression level in aorta.
DR   ExpressionAtlas; O09118; baseline and differential.
DR   Genevisible; O09118; MM.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0071944; C:cell periphery; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0033564; P:anterior/posterior axon guidance; IMP:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; IGI:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR   GO; GO:0060603; P:mammary gland duct morphogenesis; IGI:MGI.
DR   GO; GO:0030517; P:negative regulation of axon extension; IDA:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0007097; P:nuclear migration; IDA:MGI.
DR   GO; GO:0045773; P:positive regulation of axon extension; IDA:MGI.
DR   GO; GO:2000147; P:positive regulation of cell motility; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR   GO; GO:0051963; P:regulation of synapse assembly; IDA:SynGO.
DR   GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:UniProtKB.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
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; SSF49785; SSF49785; 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   3D-structure; Apoptosis; Complete proteome; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    604       Netrin-1.
FT                                /FTId=PRO_0000017083.
FT   DOMAIN       47    284       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      285    340       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      341    403       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      404    453       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      472    601       NTR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00295}.
FT   MOTIF       530    532       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD     95     95       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    116    116       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    131    131       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    119    152       {ECO:0000250}.
FT   DISULFID    285    294       {ECO:0000250}.
FT   DISULFID    287    304       {ECO:0000250}.
FT   DISULFID    306    315       {ECO:0000250}.
FT   DISULFID    318    338       {ECO:0000250}.
FT   DISULFID    341    350       {ECO:0000250}.
FT   DISULFID    343    368       {ECO:0000250}.
FT   DISULFID    371    380       {ECO:0000250}.
FT   DISULFID    383    401       {ECO:0000250}.
FT   DISULFID    404    416       {ECO:0000250}.
FT   DISULFID    406    423       {ECO:0000250}.
FT   DISULFID    425    434       {ECO:0000250}.
FT   DISULFID    437    451       {ECO:0000250}.
FT   DISULFID    472    544       {ECO:0000250}.
FT   DISULFID    491    601       {ECO:0000250}.
FT   CONFLICT     24     24       Missing (in Ref. 1; AAC52971).
FT                                {ECO:0000305}.
FT   CONFLICT     88     88       L -> V (in Ref. 1; AAC52971 and 2;
FT                                AAD28602). {ECO:0000305}.
FT   CONFLICT    466    466       V -> A (in Ref. 2; AAD28602).
FT                                {ECO:0000305}.
FT   STRAND       40     42       {ECO:0000244|PDB:4OVE}.
FT   TURN         58     61       {ECO:0000244|PDB:4OVE}.
FT   STRAND       65     67       {ECO:0000244|PDB:4OVE}.
FT   STRAND       75     81       {ECO:0000244|PDB:4OVE}.
FT   STRAND       83     85       {ECO:0000244|PDB:4OVE}.
FT   STRAND       88     94       {ECO:0000244|PDB:4OVE}.
FT   TURN         99    101       {ECO:0000244|PDB:4OVE}.
FT   HELIX       105    108       {ECO:0000244|PDB:4OVE}.
FT   STRAND      132    153       {ECO:0000244|PDB:4OVE}.
FT   STRAND      157    166       {ECO:0000244|PDB:4OVE}.
FT   STRAND      172    177       {ECO:0000244|PDB:4OVE}.
FT   HELIX       181    185       {ECO:0000244|PDB:4OVE}.
FT   STRAND      197    199       {ECO:0000244|PDB:4OVE}.
FT   HELIX       206    208       {ECO:0000244|PDB:4OVE}.
FT   STRAND      213    215       {ECO:0000244|PDB:4OVE}.
FT   STRAND      217    221       {ECO:0000244|PDB:4OVE}.
FT   TURN        222    225       {ECO:0000244|PDB:4OVE}.
FT   HELIX       227    234       {ECO:0000244|PDB:4OVE}.
FT   HELIX       236    241       {ECO:0000244|PDB:4OVE}.
FT   STRAND      243    253       {ECO:0000244|PDB:4OVE}.
FT   STRAND      275    285       {ECO:0000244|PDB:4OVE}.
FT   STRAND      294    296       {ECO:0000244|PDB:4OVE}.
FT   STRAND      302    304       {ECO:0000244|PDB:4OVE}.
FT   TURN        312    315       {ECO:0000244|PDB:4OVE}.
FT   STRAND      348    352       {ECO:0000244|PDB:4OVE}.
FT   HELIX       354    359       {ECO:0000244|PDB:4OVE}.
FT   STRAND      366    370       {ECO:0000244|PDB:4OVE}.
FT   STRAND      373    376       {ECO:0000244|PDB:4OVE}.
FT   TURN        377    380       {ECO:0000244|PDB:4OVE}.
FT   STRAND      387    389       {ECO:0000244|PDB:4OVE}.
FT   STRAND      401    403       {ECO:0000244|PDB:4OVE}.
FT   TURN        408    410       {ECO:0000244|PDB:4OVE}.
FT   TURN        418    420       {ECO:0000244|PDB:4OVE}.
FT   TURN        431    434       {ECO:0000244|PDB:4OVE}.
FT   STRAND      441    443       {ECO:0000244|PDB:4OVE}.
FT   STRAND      451    453       {ECO:0000244|PDB:4OVE}.
SQ   SEQUENCE   604 AA;  67810 MW;  135120DB6F0482F3 CRC64;
     MMRAVWEALA ALAAVACLVG AVRGGPGLSM FAGQAAQPDP CSDENGHPRR CIPDFVNAAF
     GKDVRVSSTC GRPPARYCVV SERGEERLRS CHLCNSSDPK KAHPPAFLTD LNNPHNLTCW
     QSENYLQFPH NVTLTLSLGK KFEVTYVSLQ FCSPRPESMA IYKSMDYGRT WVPFQFYSTQ
     CRKMYNRPHR APITKQNEQE AVCTDSHTDM RPLSGGLIAF STLDGRPSAH DFDNSPVLQD
     WVTATDIRVA FSRLHTFGDE NEDDSELARD SYYYAVSDLQ VGGRCKCNGH AARCVRDRDD
     SLVCDCRHNT AGPECDRCKP FHYDRPWQRA TAREANECVA CNCNLHARRC RFNMELYKLS
     GRKSGGVCLN CRHNTAGRHC HYCKEGFYRD MGKPITHRKA CKACDCHPVG AAGKTCNQTT
     GQCPCKDGVT GITCNRCAKG YQQSRSPIAP CIKIPVAPPT TAASSVEEPE DCDSYCKASK
     GKLKMNMKKY CRKDYAVQIH ILKADKAGDW WKFTVNIISV YKQGTSRIRR GDQSLWIRSR
     DIACKCPKIK PLKKYLLLGN AEDSPDQSGI VADKSSLVIQ WRDTWARRLR KFQQREKKGK
     CKKA
//
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