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Database: UniProt
Entry: Q924Z9
LinkDB: Q924Z9
Original site: Q924Z9 
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   10-APR-2019, entry version 110.
DE   RecName: Full=Netrin-1;
DE   Flags: Precursor;
GN   Name=Ntn1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11356879;
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
RT   the 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
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 (By similarity).
CC       Involved in dorsal root ganglion axon projection towards the
CC       spinal cord (By similarity). It also serves as a survival factor
CC       via its association with its receptors which prevent the
CC       initiation of apoptosis. Involved in colorectal tumorigenesis by
CC       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
CC       probably UNC5D. Binds to its receptor; DSCAM (By similarity).
CC       Interacts with APP (By similarity). {ECO:0000250|UniProtKB:O09118,
CC       ECO:0000250|UniProtKB:O95631}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:O09118}.
DR   EMBL; AY028417; AAK17014.1; -; mRNA.
DR   UniGene; Rn.17851; -.
DR   ProteinModelPortal; Q924Z9; -.
DR   IntAct; Q924Z9; 1.
DR   STRING; 10116.ENSRNOP00000005255; -.
DR   PaxDb; Q924Z9; -.
DR   PRIDE; Q924Z9; -.
DR   UCSC; RGD:619809; rat.
DR   RGD; 619809; Ntn1.
DR   eggNOG; KOG3512; Eukaryota.
DR   eggNOG; ENOG410XS7U; LUCA.
DR   HOGENOM; HOG000286017; -.
DR   HOVERGEN; HBG006464; -.
DR   InParanoid; Q924Z9; -.
DR   PhylomeDB; Q924Z9; -.
DR   PRO; PR:Q924Z9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; NAS:RGD.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; IDA:UniProtKB.
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:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IDA: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   Apoptosis; Complete proteome; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    604       Netrin-1.
FT                                /FTId=PRO_0000320574.
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}.
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
//
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