NET1_PIG
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 25-MAY-2022, entry version 91.
DE RecName: Full=Netrin-1;
DE Flags: Precursor;
GN Name=NTN1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; 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 death
RT 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 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 -!- 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; DQ368597; ABC86678.1; -; mRNA.
DR RefSeq; NP_001038013.1; NM_001044548.1.
DR AlphaFoldDB; 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 InParanoid; Q2HXW4; -.
DR OrthoDB; 858946at2759; -.
DR ChiTaRS; UNC-6; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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:0061643; P:chemorepulsion of axon; ISS:UniProtKB.
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: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 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 2: Evidence at transcript 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..600
FT /note="Netrin-1"
FT /id="PRO_0000320573"
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..600
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"
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
