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Database: UniProt
Entry: Q8R4F1
LinkDB: Q8R4F1
Original site: Q8R4F1 
ID   NTNG2_MOUSE             Reviewed;         589 AA.
AC   Q8R4F1; A2AKX0; Q8R4F2; Q8VIP6; Q8VIP7; Q8VIP8;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   13-FEB-2019, entry version 141.
DE   RecName: Full=Netrin-G2;
DE   AltName: Full=Laminet-2;
DE   Flags: Precursor;
GN   Name=Ntng2; Synonyms=Lmnt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2A; 2B AND 2C), FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB71994.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:BAB71994.1};
RX   PubMed=11804778; DOI=10.1016/S0925-4773(01)00600-1;
RA   Nakashiba T., Nishimura S., Ikeda T., Itohara S.;
RT   "Complementary expression and neurite outgrowth activity of netrin-G
RT   subfamily members.";
RL   Mech. Dev. 111:47-60(2002).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2A AND 2B), TISSUE SPECIFICITY,
RP   AND GLYCOSYLATION.
RC   TISSUE=Brain {ECO:0000269|PubMed:11906208};
RX   PubMed=11906208; DOI=10.1006/mcne.2001.1089;
RA   Yin Y., Miner J.H., Sanes J.R.;
RT   "Laminets: laminin- and netrin-related genes expressed in distinct
RT   neuronal subsets.";
RL   Mol. Cell. Neurosci. 19:344-358(2002).
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH LRRC4.
RX   PubMed=16980967; DOI=10.1038/nn1763;
RA   Kim S., Burette A., Chung H.S., Kwon S.-K., Woo J., Lee H.W., Kim K.,
RA   Kim H., Weinberg R.J., Kim E.;
RT   "NGL family PSD-95-interacting adhesion molecules regulate excitatory
RT   synapse formation.";
RL   Nat. Neurosci. 9:1294-1301(2006).
RN   [6]
RP   INTERACTION WITH LRRC4.
RX   PubMed=17973922; DOI=10.1111/j.1601-183X.2007.00361.x;
RA   Zhang W., Rajan I., Savelieva K.V., Wang C.Y., Vogel P., Kelly M.,
RA   Xu N., Hasson B., Jarman W., Lanthorn T.H.;
RT   "Netrin-G2 and netrin-G2 ligand are both required for normal auditory
RT   responsiveness.";
RL   Genes Brain Behav. 7:385-392(2008).
CC   -!- FUNCTION: Involved in controlling patterning and neuronal circuit
CC       formation at the laminar, cellular, subcellular and synaptic
CC       levels. Promotes neurite outgrowth of both axons and dendrites.
CC       {ECO:0000269|PubMed:11804778}.
CC   -!- SUBUNIT: Interacts with LRRC4. {ECO:0000269|PubMed:16980967,
CC       ECO:0000269|PubMed:17973922}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11804778};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11804778};
CC       Extracellular side {ECO:0000269|PubMed:11804778}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2B {ECO:0000269|PubMed:11906208}; Synonyms=G2b
CC       {ECO:0000269|PubMed:11804778};
CC         IsoId=Q8R4F1-1; Sequence=Displayed;
CC       Name=2A {ECO:0000269|PubMed:11906208}; Synonyms=G2a
CC       {ECO:0000269|PubMed:11804778};
CC         IsoId=Q8R4F1-2; Sequence=VSP_050562, VSP_050563;
CC       Name=2C {ECO:0000305}; Synonyms=G2c {ECO:0000269|PubMed:11804778};
CC         IsoId=Q8R4F1-3; Sequence=VSP_050564, VSP_050565;
CC   -!- TISSUE SPECIFICITY: Expression is restricted primarily to neurons
CC       of the CNS, particularly in the cerebral cortex, habenular nucleus
CC       and superior colliculus. Low levels in lung, kidney, heart and
CC       spleen. {ECO:0000269|PubMed:11804778,
CC       ECO:0000269|PubMed:11906208}.
CC   -!- DEVELOPMENTAL STAGE: Expression is detected from embryonic day 9.
CC       Strong expression is maintained from embryonic day 14 well into
CC       adulthood. {ECO:0000269|PubMed:11804778}.
CC   -!- DOMAIN: The laminin N-terminal domain mediates 1:1 binding to NGL
CC       ligand with sub-micromolar affinity. Three NGL-binding loops
CC       mediate discrimination for LRRC4/NGL2 among other NGLs by binding
CC       specifically to its LRR repeats. This specificity drives the
CC       sorting of a mixed population of molecules into discrete cell
CC       surface subdomains (By similarity). {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11906208}.
DR   EMBL; AB052336; BAB71994.1; -; mRNA.
DR   EMBL; AB052337; BAB71995.1; -; mRNA.
DR   EMBL; AB052338; BAB71996.1; -; mRNA.
DR   EMBL; AF475079; AAL84788.1; -; mRNA.
DR   EMBL; AF475080; AAL84789.1; -; mRNA.
DR   EMBL; AL772379; CAM16243.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08409.1; -; Genomic_DNA.
DR   CCDS; CCDS15851.1; -. [Q8R4F1-2]
DR   CCDS; CCDS15852.1; -. [Q8R4F1-1]
DR   CCDS; CCDS84499.1; -. [Q8R4F1-3]
DR   RefSeq; NP_001292734.1; NM_001305805.1. [Q8R4F1-3]
DR   RefSeq; NP_598007.1; NM_133500.2. [Q8R4F1-2]
DR   RefSeq; NP_598008.1; NM_133501.2. [Q8R4F1-1]
DR   UniGene; Mm.442448; -.
DR   ProteinModelPortal; Q8R4F1; -.
DR   SMR; Q8R4F1; -.
DR   IntAct; Q8R4F1; 1.
DR   STRING; 10090.ENSMUSP00000035468; -.
DR   PhosphoSitePlus; Q8R4F1; -.
DR   PaxDb; Q8R4F1; -.
DR   PRIDE; Q8R4F1; -.
DR   Ensembl; ENSMUST00000048455; ENSMUSP00000035468; ENSMUSG00000035513. [Q8R4F1-1]
DR   Ensembl; ENSMUST00000091153; ENSMUSP00000088688; ENSMUSG00000035513. [Q8R4F1-3]
DR   Ensembl; ENSMUST00000102873; ENSMUSP00000099937; ENSMUSG00000035513. [Q8R4F1-2]
DR   GeneID; 171171; -.
DR   KEGG; mmu:171171; -.
DR   UCSC; uc008izo.2; mouse. [Q8R4F1-1]
DR   UCSC; uc012btf.2; mouse. [Q8R4F1-3]
DR   CTD; 84628; -.
DR   MGI; MGI:2159341; Ntng2.
DR   eggNOG; KOG3512; Eukaryota.
DR   eggNOG; ENOG410XS7U; LUCA.
DR   GeneTree; ENSGT00940000153601; -.
DR   HOGENOM; HOG000231614; -.
DR   HOVERGEN; HBG052676; -.
DR   InParanoid; Q8R4F1; -.
DR   KO; K16359; -.
DR   OMA; TWHPYQY; -.
DR   OrthoDB; 117497at2759; -.
DR   TreeFam; TF333945; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   ChiTaRS; Ntng2; mouse.
DR   PRO; PR:Q8R4F1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000035513; Expressed in 55 organ(s), highest expression level in medulla oblongata.
DR   ExpressionAtlas; Q8R4F1; baseline and differential.
DR   Genevisible; Q8R4F1; MM.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0099029; C:anchored component of presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0090543; C:Flemming body; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR   GO; GO:0098698; P:postsynaptic specialization assembly; IDA:SynGO.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Laminin EGF-like domain; Lipoprotein; Membrane;
KW   Neurogenesis; Reference proteome; Repeat; Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    566       Netrin-G2.
FT                                /FTId=PRO_0000017097.
FT   PROPEP      567    589       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000017098.
FT   DOMAIN       35    286       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      287    346       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      413    468       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      469    513       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   REGION       69     88       NGL discriminant loop I. {ECO:0000250}.
FT   REGION      201    203       NGL discriminant loop II. {ECO:0000250}.
FT   REGION      264    267       NGL discriminant loop III. {ECO:0000250}.
FT   LIPID       566    566       GPI-anchor amidated glycine.
FT                                {ECO:0000255}.
FT   CARBOHYD    122    122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    128    128       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    310    310       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    482    482       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     22     39       {ECO:0000250}.
FT   DISULFID     61     81       {ECO:0000250}.
FT   DISULFID     69     77       {ECO:0000250}.
FT   DISULFID    171    195       {ECO:0000250}.
FT   DISULFID    287    296       {ECO:0000250}.
FT   DISULFID    289    305       {ECO:0000250}.
FT   DISULFID    307    316       {ECO:0000250}.
FT   DISULFID    319    344       {ECO:0000250}.
FT   DISULFID    413    422       {ECO:0000255}.
FT   DISULFID    415    433       {ECO:0000255}.
FT   DISULFID    436    445       {ECO:0000255}.
FT   DISULFID    448    466       {ECO:0000255}.
FT   DISULFID    469    481       {ECO:0000255}.
FT   DISULFID    471    487       {ECO:0000255}.
FT   DISULFID    489    498       {ECO:0000255}.
FT   DISULFID    501    511       {ECO:0000255}.
FT   DISULFID    516    529       {ECO:0000250}.
FT   DISULFID    523    535       {ECO:0000250}.
FT   DISULFID    537    546       {ECO:0000250}.
FT   VAR_SEQ     353    411       Missing (in isoform 2A).
FT                                {ECO:0000303|PubMed:11804778,
FT                                ECO:0000303|PubMed:11906208}.
FT                                /FTId=VSP_050562.
FT   VAR_SEQ     353    377       Missing (in isoform 2C).
FT                                {ECO:0000303|PubMed:11804778,
FT                                ECO:0000303|PubMed:11906208}.
FT                                /FTId=VSP_050564.
FT   VAR_SEQ     378    378       A -> T (in isoform 2C).
FT                                {ECO:0000303|PubMed:11804778,
FT                                ECO:0000303|PubMed:11906208}.
FT                                /FTId=VSP_050565.
FT   VAR_SEQ     412    412       D -> N (in isoform 2A).
FT                                {ECO:0000303|PubMed:11804778,
FT                                ECO:0000303|PubMed:11906208}.
FT                                /FTId=VSP_050563.
FT   CONFLICT     41     41       P -> S (in Ref. 2; AAL84788/AAL84789).
FT                                {ECO:0000305}.
FT   CONFLICT    392    392       S -> F (in Ref. 2; AAL84789).
FT                                {ECO:0000305}.
SQ   SEQUENCE   589 AA;  66166 MW;  F2AB419F0EE074F7 CRC64;
     MLRLLALFLH CLPLVSGDYD ICKSWVTTDE GPTWEFYACQ PKVMRLKDYV KVKVEPSGIT
     CGDPPERFCS HENPYLCSNE CDASNPDLAH PPRLMFDRED EGLATYWQSV TWSRYPSPLE
     ANITLSWNKS VELTDDVVVT FEYGRPTVMV LEKSLDNGRT WQPYQFYAED CMEAFGMSAR
     RARDMSPSSA HRVLCTEEYS RWAGSKKEKH VRFEVRDRFA IFAGPDLRNM DNLYTRMESA
     KGLKEFFTFT DLRMRLLRPA LGGTYVQREN LYKYFYAISN IEVIGRCKCN LHANLCTVRE
     GSLQCECEHN TTGPDCGRCK KNFRTRAWRA GSYLPLPHGS PNACAAAGSA FGSQTKPPTM
     APLGDSSFWP QVSSSAEAVA ISVAVPSQAK DSTLFELKPR SPQVIPIEEF QDCECYGHSN
     RCSYIDFLNV VTCVSCKHNT RGQHCQHCRL GYYRNGSAEL DDENVCIECN CNQIGSVHDR
     CNETGFCECR EGAVGPKCDD CLPTHYWRQG CYPNVCDDDQ LLCQNGGTCQ QNQRCACPPG
     YTGIRCEQPR CDLADDAGPD CDRAPGIVPR PDTLLGCLLL LGLAARLAC
//
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