NET3_MOUSE
ID NET3_MOUSE Reviewed; 580 AA.
AC Q9R1A3; Q9QY49; Q9WVA6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Netrin-3;
DE AltName: Full=Netrin-2-like protein;
DE Flags: Precursor;
GN Name=Ntn3; Synonyms=Ntn2l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10366627; DOI=10.1523/jneurosci.19-12-04938.1999;
RA Wang H., Copeland N.G., Gilbert D.J., Jenkins N.A., Tessier-Lavigne M.;
RT "Netrin-3, a mouse homolog of human NTN2L, is highly expressed in sensory
RT ganglia and shows differential binding to netrin receptors.";
RL J. Neurosci. 19:4938-4947(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seaman C., Lackmann M., Kravets L., Anderson R.B., Cooper H.M.;
RT "Netrin-3, a novel netrin-related axon guidance cue is associated with
RT motor neurons within the developing vertebrate nervous system.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11231084; DOI=10.1016/s0925-4773(00)00563-3;
RA Seaman C., Cooper H.M.;
RT "Netrin-3 protein is localized to the axons of motor, sensory, and
RT sympathetic neurons.";
RL Mech. Dev. 101:245-248(2001).
CC -!- FUNCTION: Netrins control guidance of CNS commissural axons and
CC peripheral motor axons. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:11231084}.
CC -!- TISSUE SPECIFICITY: Very low levels at 10.5 to 12.5 dpc in dorsal root
CC ganglia. High levels in motor neurons at 13.5, 14.5 and 15.5 dpc. At
CC 11.5 dpc also expressed in the developing limb buds.
CC {ECO:0000269|PubMed:10381568, ECO:0000269|PubMed:11231084}.
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DR EMBL; AF152418; AAD40063.1; -; mRNA.
DR EMBL; AK031199; BAC27297.1; -; mRNA.
DR EMBL; AF149094; AAD42078.1; -; mRNA.
DR EMBL; AF128866; AAD28603.1; -; mRNA.
DR CCDS; CCDS28478.1; -.
DR RefSeq; NP_035077.1; NM_010947.3.
DR AlphaFoldDB; Q9R1A3; -.
DR SMR; Q9R1A3; -.
DR BioGRID; 201867; 1.
DR STRING; 10090.ENSMUSP00000024931; -.
DR GlyGen; Q9R1A3; 2 sites.
DR PhosphoSitePlus; Q9R1A3; -.
DR MaxQB; Q9R1A3; -.
DR PaxDb; Q9R1A3; -.
DR PRIDE; Q9R1A3; -.
DR ProteomicsDB; 252811; -.
DR Antibodypedia; 66015; 89 antibodies from 20 providers.
DR DNASU; 18209; -.
DR Ensembl; ENSMUST00000024931; ENSMUSP00000024931; ENSMUSG00000117406.
DR GeneID; 18209; -.
DR KEGG; mmu:18209; -.
DR UCSC; uc008auy.2; mouse.
DR CTD; 4917; -.
DR MGI; MGI:1341188; Ntn3.
DR VEuPathDB; HostDB:ENSMUSG00000117406; -.
DR eggNOG; KOG3512; Eukaryota.
DR GeneTree; ENSGT00940000153882; -.
DR HOGENOM; CLU_018213_2_0_1; -.
DR InParanoid; Q9R1A3; -.
DR OMA; SHCRPAR; -.
DR OrthoDB; 858946at2759; -.
DR PhylomeDB; Q9R1A3; -.
DR TreeFam; TF352481; -.
DR BioGRID-ORCS; 18209; 7 hits in 42 CRISPR screens.
DR PRO; PR:Q9R1A3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9R1A3; protein.
DR Bgee; ENSMUSG00000117406; Expressed in humerus cartilage element and 68 other tissues.
DR ExpressionAtlas; Q9R1A3; baseline and differential.
DR Genevisible; Q9R1A3; MM.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; TAS:MGI.
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:0007520; P:myoblast fusion; ISA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISA:MGI.
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 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..580
FT /note="Netrin-3"
FT /id="PRO_0000017086"
FT DOMAIN 36..254
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 255..310
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 311..373
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 374..423
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 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 CONFLICT 23
FT /note="L -> P (in Ref. 2; AAD42078)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="V -> M (in Ref. 2; AAD42078)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="A -> G (in Ref. 3; AAD28603)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="A -> P (in Ref. 3; AAD28603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 62023 MW; E1D7BFBADD10629D CRC64;
MPTWLWGLLL TAGTLSAALS PGLPASADPC YDEAREPRSC IPGLVNAALG REVLASSTCG
RSANRVCDSS DPQRAHSADL LTSAPGTASP LCWRSDLLQQ APFNVTLTVP LGKAFELVFV
SLRFCSAPPT SVALLKSQDH GRSWVPLGFF SSSCTLDYGR LPAPADGPSG PGPEALCFPA
PQAQPDGGGL LAFSVQDGSP QGLDLDNSPV LQDWVTATDI RIVLTRPAIQ GDTRDGGVTV
PYSYSATELQ VGGRCKCNGH ASRCLLDTHG HLVCDCQHGT EGPDCSRCKP FYCDRPWQRA
TGQEAHACLA CSCNGHARRC RFNMELYRLS GRRSGGVCLN CRHNTAGRHC HYCREGFYRD
PGRVLSDRRA CRACDCHPVG AAGKTCNQTT GQCPCKDGVT GLTCNRCAPG FQQSRSPVAP
CVKTPVPGPT EESSPVEPQD CESHCRPARG SYRISLKKFC RKDYAVQVAV GARGEARGSW
TRFPVAVLAV FRSGEERARR GSSALWVPTL DAACGCPRLL PGRRYLLLGG GPGAAAGSTA
GRGQGLSAAR GSLVLPWRDA WTRRLRRLQR RERRGRCGTA
