NET1_RAT
ID NET1_RAT Reviewed; 604 AA.
AC Q924Z9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 23-FEB-2022, entry version 121.
DE RecName: Full=Netrin-1;
DE Flags: Precursor;
GN Name=Ntn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11356879; DOI=10.1523/jneurosci.21-11-03911.2001;
RA Manitt C., Colicos M.A., Thompson K.M., Rousselle E., Peterson A.C.,
RA Kennedy T.E.;
RT "Widespread expression of netrin-1 by neurons and oligodendrocytes in the
RT adult mammalian spinal cord.";
RL J. Neurosci. 21:3911-3922(2001).
RN [2]
RP FUNCTION, AND INTERACTION WITH DCC.
RX PubMed=8861902; DOI=10.1016/s0092-8674(00)81336-7;
RA Keino-Masu K., Masu M., Hinck L., Leonardo E.D., Chan S.S.-Y.,
RA Culotti J.G., Tessier-Lavigne M.;
RT "Deleted in colorectal cancer (DCC) encodes a netrin receptor.";
RL Cell 87:175-185(1996).
CC -!- FUNCTION: Netrins control guidance of CNS commissural axons and
CC peripheral motor axons. Its association with either DCC or some UNC5
CC receptors will lead to axon attraction or repulsion, respectively.
CC Binding to UNC5C might cause dissociation of UNC5C from polymerized
CC TUBB3 in microtubules and thereby lead to increased microtubule
CC dynamics and axon repulsion (By similarity). Involved in dorsal root
CC ganglion axon projection towards the spinal cord (By similarity). It
CC also 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:O09118, ECO:0000250|UniProtKB:O95631,
CC ECO:0000269|PubMed:8861902}.
CC -!- SUBUNIT: Binds to its receptors; DCC, UNC5A, UNC5B, UNC5C and probably
CC UNC5D. Binds to its receptor; DSCAM (By similarity). Interacts with APP
CC (By similarity). {ECO:0000250|UniProtKB:O09118,
CC ECO:0000250|UniProtKB:O95631}.
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; AY028417; AAK17014.1; -; mRNA.
DR IntAct; Q924Z9; 1.
DR STRING; 10116.ENSRNOP00000005255; -.
DR GlyGen; Q924Z9; 4 sites.
DR PaxDb; Q924Z9; -.
DR PRIDE; Q924Z9; -.
DR UCSC; RGD:619809; rat.
DR RGD; 619809; Ntn1.
DR eggNOG; KOG3512; Eukaryota.
DR InParanoid; Q924Z9; -.
DR PhylomeDB; Q924Z9; -.
DR Reactome; R-RNO-373752; Netrin-1 signaling.
DR Reactome; R-RNO-418885; DCC mediated attractive signaling.
DR PRO; PR:Q924Z9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0061643; P:chemorepulsion of axon; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0030879; P:mammary gland development; ISO:RGD.
DR GO; GO:0060603; P:mammary gland duct morphogenesis; ISO:RGD.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0007097; P:nuclear migration; ISO:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:RGD.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IDA: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 Apoptosis; Cytoplasm; Disulfide bond; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..604
FT /note="Netrin-1"
FT /id="PRO_0000320574"
FT DOMAIN 47..284
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 285..340
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 341..403
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 404..453
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 472..601
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT MOTIF 530..532
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..152
FT /evidence="ECO:0000250"
FT DISULFID 285..294
FT /evidence="ECO:0000250"
FT DISULFID 287..304
FT /evidence="ECO:0000250"
FT DISULFID 306..315
FT /evidence="ECO:0000250"
FT DISULFID 318..338
FT /evidence="ECO:0000250"
FT DISULFID 341..350
FT /evidence="ECO:0000250"
FT DISULFID 343..368
FT /evidence="ECO:0000250"
FT DISULFID 371..380
FT /evidence="ECO:0000250"
FT DISULFID 383..401
FT /evidence="ECO:0000250"
FT DISULFID 404..416
FT /evidence="ECO:0000250"
FT DISULFID 406..423
FT /evidence="ECO:0000250"
FT DISULFID 425..434
FT /evidence="ECO:0000250"
FT DISULFID 437..451
FT /evidence="ECO:0000250"
FT DISULFID 472..544
FT /evidence="ECO:0000250"
FT DISULFID 491..601
FT /evidence="ECO:0000250"
SQ SEQUENCE 604 AA; 67873 MW; 7CC03C6D721839F9 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 TAASSMEEPE DCDSYCKASK
GKLKMNMKKY CRKDYAVQIH ILKADKAGDW WKFTVNIISV YKQGTSRIRR GDQSLWIRSR
DIAXKCPKIK PLKKYLLLGN AEDSPDQSGI VADKSXLVIQ WRDTWARRXR KFQQREKKGK
CKKA
