NET1_CHICK
ID NET1_CHICK Reviewed; 606 AA.
AC Q90922;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Netrin-1;
DE Flags: Precursor;
GN Name=NTN1;
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. Promotes neurite outgrowth from commissural
CC axons but acts as a chemorepellent for trochlear motor axons. These
CC effects are mediated by distinct receptors.
CC -!- INTERACTION:
CC Q90922; Q9ERC8: Dscam; Xeno; NbExp=7; IntAct=EBI-1798593, EBI-1798601;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O95631}.
CC Cytoplasm {ECO:0000250|UniProtKB:O95631}. Note=Mainly secreted.
CC {ECO:0000250|UniProtKB:O95631}.
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DR EMBL; L34549; AAA60369.1; -; mRNA.
DR PIR; A54665; A54665.
DR RefSeq; NP_990750.1; NM_205419.1.
DR PDB; 4PLM; X-ray; 2.80 A; A=26-457.
DR PDB; 4PLN; X-ray; 3.20 A; A/B=26-457.
DR PDB; 4PLO; X-ray; 2.90 A; A=26-457.
DR PDB; 7LER; X-ray; 5.99 A; A/B/C/D/E/F/G/H=26-458.
DR PDB; 7LRF; X-ray; 3.21 A; A/B=26-458.
DR PDBsum; 4PLM; -.
DR PDBsum; 4PLN; -.
DR PDBsum; 4PLO; -.
DR PDBsum; 7LER; -.
DR PDBsum; 7LRF; -.
DR AlphaFoldDB; Q90922; -.
DR SMR; Q90922; -.
DR IntAct; Q90922; 3.
DR STRING; 9031.ENSGALP00000038541; -.
DR PaxDb; Q90922; -.
DR GeneID; 396389; -.
DR KEGG; gga:396389; -.
DR CTD; 9423; -.
DR VEuPathDB; HostDB:geneid_396389; -.
DR eggNOG; KOG3512; Eukaryota.
DR HOGENOM; CLU_018213_2_0_1; -.
DR InParanoid; Q90922; -.
DR OrthoDB; 858946at2759; -.
DR PhylomeDB; Q90922; -.
DR PRO; PR:Q90922; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IEA:Ensembl.
DR GO; GO:0019724; P:B cell mediated immunity; ISS:UniProtKB.
DR GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0061643; P:chemorepulsion of axon; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0097475; P:motor neuron migration; IEA:Ensembl.
DR GO; GO:0030517; P:negative regulation of axon extension; IEA:Ensembl.
DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:1903975; P:regulation of glial cell migration; IEA:Ensembl.
DR GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:UniProtKB.
DR GO; GO:0002456; P:T cell mediated immunity; ISS:UniProtKB.
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; IPR008979; Galactose-bd-like_sf.
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; 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; Cytoplasm; Disulfide bond; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..606
FT /note="Netrin-1"
FT /id="PRO_0000017084"
FT DOMAIN 49..286
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 287..342
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 343..405
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 406..455
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 474..603
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT MOTIF 532..534
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..154
FT /evidence="ECO:0000250"
FT DISULFID 287..296
FT /evidence="ECO:0000250"
FT DISULFID 289..306
FT /evidence="ECO:0000250"
FT DISULFID 308..317
FT /evidence="ECO:0000250"
FT DISULFID 320..340
FT /evidence="ECO:0000250"
FT DISULFID 343..352
FT /evidence="ECO:0000250"
FT DISULFID 345..370
FT /evidence="ECO:0000250"
FT DISULFID 373..382
FT /evidence="ECO:0000250"
FT DISULFID 385..403
FT /evidence="ECO:0000250"
FT DISULFID 406..418
FT /evidence="ECO:0000250"
FT DISULFID 408..425
FT /evidence="ECO:0000250"
FT DISULFID 427..436
FT /evidence="ECO:0000250"
FT DISULFID 439..453
FT /evidence="ECO:0000250"
FT DISULFID 474..546
FT /evidence="ECO:0000250"
FT DISULFID 493..603
FT /evidence="ECO:0000250"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4PLN"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4PLO"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4PLM"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 134..155
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 159..171
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:4PLM"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:4PLM"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:4PLM"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:4PLM"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:4PLM"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 277..287
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:4PLM"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:4PLM"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:4PLO"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4PLM"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4PLM"
SQ SEQUENCE 606 AA; 68127 MW; 9BFF0E3B07A71AE1 CRC64;
MPRRGAEGPL ALLLAAAWLA QPLRGGYPGL NMFAVQTAQP DPCYDEHGLP RRCIPDFVNS
AFGKEVKVSS TCGKPPSRYC VVTEKGEEQV RSCHLCNASD PKRAHPPSFL TDLNNPHNLT
CWQSDSYVQY PHNVTLTLSL GKKFEVTYVS LQFCSPRPES MAIYKSMDYG KTWVPFQFYS
TQCRKMYNKP SRAAITKQNE QEAICTDSHT DVRPLSGGLI AFSTLDGRPT AHDFDNSPVL
QDWVTATDIK VTFSRLHTFG DENEDDSELA RDSYFYAVSD LQVGGRCKCN GHASRCVRDR
DDNLVCDCKH NTAGPECDRC KPFHYDRPWQ RATAREANEC VACNCNLHAR RCRFNMELYK
LSGRKSGGVC LNCRHNTAGR HCHYCKEGFY RDLSKPISHR KACKECDCHP VGAAGQTCNQ
TTGQCPCKDG VTGITCNRCA KGYQQSRSPI APCIKIPAAP PPTAASSTEE PADCDSYCKA
SKGKLKINMK KYCKKDYAVQ IHILKAEKNA DWWKFTVNII SVYKQGSNRL RRGDQTLWVH
AKDIACKCPK VKPMKKYLLL GSTEDSPDQS GIIADKSSLV IQWRDTWARR LRKFQQREKK
GKCRKA
