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   04-FEB-2015, entry version 99.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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/c;
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
RT   with the beta chain of laminin. Identification, expression, and
RT   functional 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: May play an important role in neural, kidney and
CC       vascular development. Promotes neurite elongation from olfactory
CC       bulb explants. {ECO:0000269|PubMed:11038171}.
CC   -!- SUBUNIT: May form a homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, liver, heart, ovary,
CC       testis, retina, brain, olfactory bulb, and widely expressed in
CC       embryo. {ECO:0000269|PubMed:10940631,
CC       ECO:0000269|PubMed:11038171}.
CC   -!- SIMILARITY: Contains 3 laminin EGF-like domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00460}.
CC   -!- SIMILARITY: Contains 1 laminin N-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00466}.
CC   -!- SIMILARITY: Contains 1 NTR domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00295}.
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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   UniGene; Mm.483868; -.
DR   ProteinModelPortal; Q9JI33; -.
DR   SMR; Q9JI33; 31-462.
DR   BioGrid; 208320; 3.
DR   DIP; DIP-60741N; -.
DR   PhosphoSite; Q9JI33; -.
DR   MaxQB; Q9JI33; -.
DR   PaxDb; Q9JI33; -.
DR   PRIDE; Q9JI33; -.
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   eggNOG; NOG329215; -.
DR   GeneTree; ENSGT00780000121873; -.
DR   HOGENOM; HOG000060085; -.
DR   HOVERGEN; HBG082019; -.
DR   InParanoid; Q9JI33; -.
DR   KO; K06845; -.
DR   OMA; KGAICTS; -.
DR   OrthoDB; EOG7BKCT6; -.
DR   TreeFam; TF352481; -.
DR   Reactome; REACT_196607; Non-integrin membrane-ECM interactions.
DR   Reactome; REACT_229826; Netrin-1 signaling.
DR   NextBio; 313932; -.
DR   PRO; PR:Q9JI33; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; Q9JI33; -.
DR   CleanEx; MM_NTN4; -.
DR   ExpressionAtlas; Q9JI33; baseline and differential.
DR   Genevestigator; Q9JI33; -.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043237; F:laminin-1 binding; IDA:MGI.
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   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR008211; Laminin_N.
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   2: Evidence at transcript level;
KW   Basement membrane; Complete proteome; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    628       Netrin-4.
FT                                /FTId=PRO_0000042117.
FT   DOMAIN       30    261       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      262    331       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      332    394       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      395    448       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      506    627       NTR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00295}.
FT   CARBOHYD     56     56       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    163    163       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    353    353       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    483    483       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    262    271       {ECO:0000250}.
FT   DISULFID    264    293       {ECO:0000250}.
FT   DISULFID    295    304       {ECO:0000250}.
FT   DISULFID    307    329       {ECO:0000250}.
FT   DISULFID    332    341       {ECO:0000250}.
FT   DISULFID    334    359       {ECO:0000250}.
FT   DISULFID    362    371       {ECO:0000250}.
FT   DISULFID    374    392       {ECO:0000250}.
FT   DISULFID    395    413       {ECO:0000250}.
FT   DISULFID    397    420       {ECO:0000250}.
FT   DISULFID    422    431       {ECO:0000250}.
FT   DISULFID    434    446       {ECO:0000250}.
FT   DISULFID    506    576       {ECO:0000250}.
FT   DISULFID    520    627       {ECO:0000250}.
FT   CONFLICT    477    477       A -> T (in Ref. 1; AAF91404 and 2;
FT                                AAG30823). {ECO:0000305}.
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
//