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Database: UniProt
Entry: Q2HXW4
LinkDB: Q2HXW4
Original site: Q2HXW4 
ID   NET1_PIG                Reviewed;         600 AA.
AC   Q2HXW4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   10-APR-2019, entry version 78.
DE   RecName: Full=Netrin-1;
DE   Flags: Precursor;
GN   Name=NTN1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Maeda A., Matsuda F., Goto Y., Cheng Y., Manabe N.;
RT   "Molecular cloning of porcine (Sus scrofa) p53-regulated receptor for
RT   death and life (p53RDL1) and netrin-1.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; DQ368597; ABC86678.1; -; mRNA.
DR   RefSeq; NP_001038013.1; NM_001044548.1.
DR   UniGene; Ssc.22870; -.
DR   ProteinModelPortal; Q2HXW4; -.
DR   SMR; Q2HXW4; -.
DR   STRING; 9823.ENSSSCP00000019063; -.
DR   PaxDb; Q2HXW4; -.
DR   PRIDE; Q2HXW4; -.
DR   GeneID; 733599; -.
DR   KEGG; ssc:733599; -.
DR   CTD; 9423; -.
DR   eggNOG; KOG3512; Eukaryota.
DR   eggNOG; ENOG410XS7U; LUCA.
DR   HOGENOM; HOG000286017; -.
DR   HOVERGEN; HBG006464; -.
DR   InParanoid; Q2HXW4; -.
DR   KO; K06843; -.
DR   OrthoDB; 858946at2759; -.
DR   ChiTaRS; UNC-6; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; ISS:UniProtKB.
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:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS: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   2: Evidence at transcript 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    600       Netrin-1.
FT                                /FTId=PRO_0000320573.
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    600       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}.
SQ   SEQUENCE   600 AA;  67372 MW;  73985DA23CC87960 CRC64;
     MMRAMWEALA ALAAVSCLVG AVRGGPGLSM FAGQAAQPDP CSDENGHPRR CIPDFVNAAF
     GKDVRVSSTC GRPPARYCVV SERGEERLRS CHLCNASDPK KAHPPAFLTD LNNPHNLTCW
     QSENYLQFPH NVTLTLSLGK KFEVTYVSLQ FCSPRPESMA IYKSMDYGRT WVPFQFYSTQ
     CRKMYNRPHR APITKQNEQE AVCTDSHTDM RPLSGGLIAF STLDGRPSAH DFDNSPVLQD
     WVTATDIRVA FSRLHTFGDE NEDDSELARD SYFYAVSDLQ VGGRCKCNGH AARCVRDRDD
     SLVCDCRHNT AGPECDRCKP FHYDRPWQRA TAREANECVA CNCNLHARRC RFNMELYKLS
     GRKSGGVCLN CRHNTAGRHC HYCKEGYFRD LGKPITHRKA CKACDCHPVG AAGKTCNQTT
     GQCPCKDGVT GVTCNRCAKG YQQSRSPIAP CIKIPVAPPT TAASSVEEPE DCDSYCKASK
     GKLKINMKKY CKKDYAVQIH ILKADKAGDW WKFTVNIISV YKQGASRIRR GDQNLWIRSR
     DIACKCPKIK PLKKYLLLGN AEDSPDQSGI VADKSSLVIQ WRDTWARRLR KFQQREKKEL
//
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