NET4_MOUSE
ID NET4_MOUSE Reviewed; 628 AA.
AC Q9JI33; E9QMT3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Netrin-4;
DE AltName: Full=Beta-netrin;
DE Flags: Precursor;
GN Name=Ntn4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=ICR;
RX PubMed=10940631; DOI=10.1016/s0925-4773(00)00369-5;
RA Yin Y., Sanes J.R., Miner J.H.;
RT "Identification and expression of mouse netrin-4.";
RL Mech. Dev. 96:115-119(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=11038171; DOI=10.1083/jcb.151.2.221;
RA Koch M., Murrell J.R., Hunter D.D., Olson P.F., Jin W., Keene D.R.,
RA Brunken W.J., Burgeson R.E.;
RT "A novel member of the netrin family, beta-netrin, shares homology with the
RT beta chain of laminin. Identification, expression, and functional
RT characterization.";
RL J. Cell Biol. 151:221-234(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May play an important role in neural, kidney and vascular
CC development. Promotes neurite elongation from olfactory bulb explants.
CC {ECO:0000269|PubMed:11038171}.
CC -!- SUBUNIT: May form a homodimer.
CC -!- INTERACTION:
CC Q9JI33; P02468: Lamc1; NbExp=2; IntAct=EBI-15755373, EBI-7059830;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, heart, ovary, testis,
CC retina, brain, olfactory bulb, and widely expressed in embryo.
CC {ECO:0000269|PubMed:10940631, ECO:0000269|PubMed:11038171}.
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DR EMBL; AF268066; AAF91404.1; -; mRNA.
DR EMBL; AF281278; AAG30823.1; -; mRNA.
DR EMBL; AC124585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24128.1; -.
DR RefSeq; NP_067295.2; NM_021320.3.
DR PDB; 4WNX; X-ray; 2.72 A; A=30-462.
DR PDBsum; 4WNX; -.
DR AlphaFoldDB; Q9JI33; -.
DR SMR; Q9JI33; -.
DR BioGRID; 208320; 3.
DR DIP; DIP-60741N; -.
DR IntAct; Q9JI33; 4.
DR STRING; 10090.ENSMUSP00000020204; -.
DR GlyGen; Q9JI33; 4 sites.
DR PhosphoSitePlus; Q9JI33; -.
DR MaxQB; Q9JI33; -.
DR PaxDb; Q9JI33; -.
DR PRIDE; Q9JI33; -.
DR ProteomicsDB; 287379; -.
DR Antibodypedia; 30131; 206 antibodies from 27 providers.
DR DNASU; 57764; -.
DR Ensembl; ENSMUST00000020204; ENSMUSP00000020204; ENSMUSG00000020019.
DR GeneID; 57764; -.
DR KEGG; mmu:57764; -.
DR UCSC; uc007gux.2; mouse.
DR CTD; 59277; -.
DR MGI; MGI:1888978; Ntn4.
DR VEuPathDB; HostDB:ENSMUSG00000020019; -.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000156615; -.
DR HOGENOM; CLU_016961_2_1_1; -.
DR InParanoid; Q9JI33; -.
DR OMA; PKAFCGM; -.
DR OrthoDB; 236390at2759; -.
DR PhylomeDB; Q9JI33; -.
DR TreeFam; TF352481; -.
DR Reactome; R-MMU-373752; Netrin-1 signaling.
DR BioGRID-ORCS; 57764; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ntn4; mouse.
DR PRO; PR:Q9JI33; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JI33; protein.
DR Bgee; ENSMUSG00000020019; Expressed in pigmented layer of retina and 197 other tissues.
DR ExpressionAtlas; Q9JI33; baseline and differential.
DR Genevisible; Q9JI33; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043237; F:laminin-1 binding; IDA:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0016322; P:neuron remodeling; IDA:MGI.
DR GO; GO:0060668; P:regulation of branching involved in salivary gland morphogenesis by extracellular matrix-epithelial cell signaling; IDA:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 3.
DR CDD; cd03578; NTR_netrin-4_like; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR035811; Netrin-4_NTR.
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; SSF50242; SSF50242; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01248; EGF_LAM_1; 2.
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; Basement membrane; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..628
FT /note="Netrin-4"
FT /id="PRO_0000042117"
FT DOMAIN 30..261
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 262..331
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 332..394
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 395..448
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 506..627
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 262..271
FT /evidence="ECO:0000250"
FT DISULFID 264..293
FT /evidence="ECO:0000250"
FT DISULFID 295..304
FT /evidence="ECO:0000250"
FT DISULFID 307..329
FT /evidence="ECO:0000250"
FT DISULFID 332..341
FT /evidence="ECO:0000250"
FT DISULFID 334..359
FT /evidence="ECO:0000250"
FT DISULFID 362..371
FT /evidence="ECO:0000250"
FT DISULFID 374..392
FT /evidence="ECO:0000250"
FT DISULFID 395..413
FT /evidence="ECO:0000250"
FT DISULFID 397..420
FT /evidence="ECO:0000250"
FT DISULFID 422..431
FT /evidence="ECO:0000250"
FT DISULFID 434..446
FT /evidence="ECO:0000250"
FT DISULFID 506..576
FT /evidence="ECO:0000250"
FT DISULFID 520..627
FT /evidence="ECO:0000250"
FT CONFLICT 477
FT /note="A -> T (in Ref. 1; AAF91404 and 2; AAG30823)"
FT /evidence="ECO:0000305"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4WNX"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:4WNX"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 115..136
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:4WNX"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4WNX"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:4WNX"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:4WNX"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 220..230
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 252..262
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4WNX"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:4WNX"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:4WNX"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:4WNX"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:4WNX"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:4WNX"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:4WNX"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:4WNX"
SQ SEQUENCE 628 AA; 69867 MW; 30C5553175E6678D CRC64;
MGSCARLLLL WGCSAVAAGL NGVAGANSRC EKACNPRMGN LALGRKLRAD TMCGQNATEL
FCFYSENADL TCRQPKCDKC NAAHSHLAHP PSAMADSSFR FPRTWWQSAE DVHREKIQLD
LEAEFYFTHL IMVFKSPRPA AMVLDRSQDF GKTWKPYKYF ATNCSATFGL EDDVVKKGAI
CTSRYSNPFP CTGGEVIFRA LSPPYDIENP YSAKVQEQLK ITNLRVRLLK RQSCPCQIND
LNAKPHHFMH YAVYDFIVKG SCFCNGHADQ CLPVEGFRPI KAPGAFHVVH GRCMCKHNTA
GSHCQHCAPL YNDRPWEAAD GRTGAPNECR TCKCNGHADT CHFDVNVWEA SGNRSGGVCN
NCQHNTEGQH CQRCKPGFYR DLRRPFSAPD ACKACSCHPV GSAILPFSSV TFCDPSNGDC
PCKPGVAGPH CDRCMVGYWG FGDYGCRPCD CAGSCDPLTG DCISSNADVD WYHEVPAFHS
MHNKSEPSWE WEDEQGFSAL RHSGKCECKE QVLGNPKAFC GMKYSYVLKI KILSAHDKGS
HAEVNVKIKK VLKSTKLKIL RGKRTLYPES WTNRGCTCPI LNPGLEYLVA GHEDVRTGKL
IVNMKSFVQH WKPALGRRVM HILKRDCV
