NET3_CHICK
ID NET3_CHICK Reviewed; 581 AA.
AC Q90923;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Netrin-3;
DE AltName: Full=Netrin-2;
DE Flags: Precursor; Fragment;
GN Name=NTN3; Synonyms=NTN2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Embryonic brain;
RX PubMed=8062384; DOI=10.1016/0092-8674(94)90420-0;
RA Serafini T., Kennedy T.E., Galko M.J., Mirzayan C., Jessell T.M.,
RA Tessier-Lavigne M.;
RT "The netrins define a family of axon outgrowth-promoting proteins
RT homologous to C. elegans UNC-6.";
RL Cell 78:409-424(1994).
CC -!- FUNCTION: Netrins control guidance of CNS commissural axons and
CC peripheral motor axons.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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DR EMBL; L34550; AAA61743.1; -; mRNA.
DR PIR; B54665; B54665.
DR RefSeq; NP_001264534.1; NM_001277605.1.
DR AlphaFoldDB; Q90923; -.
DR SMR; Q90923; -.
DR STRING; 9031.ENSGALP00000043056; -.
DR PaxDb; Q90923; -.
DR GeneID; 396387; -.
DR KEGG; gga:396387; -.
DR CTD; 4917; -.
DR VEuPathDB; HostDB:geneid_396387; -.
DR eggNOG; KOG3512; Eukaryota.
DR InParanoid; Q90923; -.
DR OrthoDB; 858946at2759; -.
DR PhylomeDB; Q90923; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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: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; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..581
FT /note="Netrin-3"
FT /id="PRO_0000017087"
FT DOMAIN 35..261
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 262..317
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 318..380
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 381..430
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 449..578
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT MOTIF 507..509
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..124
FT /evidence="ECO:0000250"
FT DISULFID 262..271
FT /evidence="ECO:0000250"
FT DISULFID 264..281
FT /evidence="ECO:0000250"
FT DISULFID 283..292
FT /evidence="ECO:0000250"
FT DISULFID 295..315
FT /evidence="ECO:0000250"
FT DISULFID 318..327
FT /evidence="ECO:0000250"
FT DISULFID 320..345
FT /evidence="ECO:0000250"
FT DISULFID 348..357
FT /evidence="ECO:0000250"
FT DISULFID 360..378
FT /evidence="ECO:0000250"
FT DISULFID 381..393
FT /evidence="ECO:0000250"
FT DISULFID 383..400
FT /evidence="ECO:0000250"
FT DISULFID 402..411
FT /evidence="ECO:0000250"
FT DISULFID 414..428
FT /evidence="ECO:0000250"
FT DISULFID 449..521
FT /evidence="ECO:0000250"
FT DISULFID 468..578
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 581 AA; 65107 MW; 4AE59387A5F44659 CRC64;
LRLLLTTSVL RLARAANPFV AQQTPPDPCY DESGAPRRCI PEFVNAAFGK EVQASSTCGK
PPTRHCDASD PRRAHPPAYL TDLNTAANMT CWRSETLHHL PHNVTLTLSL GKKFEVVYVS
LQFCSPRPES TAIFKSMDYG KTWVPYQYYS SQCRKIYGKP SKATVTKQNE QEALCTDGLT
DLYPLTGGLI AFSTLDGRPS AQDFDSSPVL QDWVTATDIR VVFSRPHLFR ELGGREAGEE
DGGAGATPYY YSVGELQVGG RCKCNGHASR CVKDKEQKLV CDCKHNTEGP ECDRCKPFHY
DRPWQRASAR EANECLACNC NLHARRCRFN MELYKLSGRK SGGVCLNCRH NTAGRHCHYC
KEGFYRDLSK SITDRKACKA CDCHPVGAAG KTCNQTTGQC PCKDGVTGLT CNRCAKGFQQ
SRSPVAPCIK IPAINPTSLV TSTEAPADCD SYCKPAKGNY KINMKKYCKK DYVVQVNILE
METVANWAKF TINILSVYKC RDERVKRGDN FLWIHLKDLS CKCPKIQISK KYLVMGISEN
STDRPGLMAD KNSLVIQWRD AWTRRLRKLQ RREKKGKCVK P
