位置:首页 > 蛋白库 > NTNG2_MOUSE
NTNG2_MOUSE
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   03-AUG-2022, entry version 161.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2A; 2B AND 2C), FUNCTION, SUBCELLULAR
RP   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, AND
RP   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 neuronal
RT   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., 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).
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., Xu N.,
RA   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).
RN   [7]
RP   FUNCTION.
RX   PubMed=31668703; DOI=10.1016/j.ajhg.2019.09.025;
RA   Dias C.M., Punetha J., Zheng C., Mazaheri N., Rad A., Efthymiou S.,
RA   Petersen A., Dehghani M., Pehlivan D., Partlow J.N., Posey J.E.,
RA   Salpietro V., Gezdirici A., Malamiri R.A., Al Menabawy N.M., Selim L.A.,
RA   Vahidi Mehrjardi M.Y., Banu S., Polla D.L., Yang E.,
RA   Rezazadeh Varaghchi J., Mitani T., van Beusekom E., Najafi M., Sedaghat A.,
RA   Keller-Ramey J., Durham L., Coban-Akdemir Z., Karaca E., Orlova V.,
RA   Schaeken L.L.M., Sherafat A., Jhangiani S.N., Stanley V., Shariati G.,
RA   Galehdari H., Gleeson J.G., Walsh C.A., Lupski J.R., Seiradake E.,
RA   Houlden H., van Bokhoven H., Maroofian R.;
RT   "Homozygous Missense Variants in NTNG2, Encoding a Presynaptic Netrin-G2
RT   Adhesion Protein, Lead to a Distinct Neurodevelopmental Disorder.";
RL   Am. J. Hum. Genet. 105:1048-1056(2019).
RN   [8]
RP   FUNCTION.
RX   PubMed=31692205; DOI=10.1002/humu.23945;
RA   Heimer G., van Woerden G.M., Barel O., Marek-Yagel D., Kol N.,
RA   Munting J.B., Borghei M., Atawneh O.M., Nissenkorn A., Rechavi G.,
RA   Anikster Y., Elgersma Y., Kushner S.A., Ben Zeev B.;
RT   "Netrin-G2 dysfunction causes a Rett-like phenotype with areflexia.";
RL   Hum. Mutat. 41:476-486(2020).
CC   -!- FUNCTION: Involved in controlling patterning and neuronal circuit
CC       formation at the laminar, cellular, subcellular and synaptic levels.
CC       Promotes neurite outgrowth of both axons and dendrites.
CC       {ECO:0000269|PubMed:11804778, ECO:0000269|PubMed:31668703,
CC       ECO:0000269|PubMed:31692205}.
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}; Extracellular
CC       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 of
CC       the CNS, particularly in the cerebral cortex, habenular nucleus and
CC       superior colliculus. Low levels in lung, kidney, heart and spleen.
CC       {ECO:0000269|PubMed:11804778, 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 mediate
CC       discrimination for LRRC4/NGL2 among other NGLs by binding specifically
CC       to its LRR repeats. This specificity drives the sorting of a mixed
CC       population of molecules into discrete cell surface subdomains (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11906208}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; -; NOT_ANNOTATED_CDS; 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   AlphaFoldDB; Q8R4F1; -.
DR   SMR; Q8R4F1; -.
DR   BioGRID; 228486; 1.
DR   IntAct; Q8R4F1; 1.
DR   STRING; 10090.ENSMUSP00000035468; -.
DR   GlyConnect; 2533; 2 N-Linked glycans (1 site).
DR   GlyGen; Q8R4F1; 5 sites, 2 N-linked glycans (1 site).
DR   PhosphoSitePlus; Q8R4F1; -.
DR   PaxDb; Q8R4F1; -.
DR   PRIDE; Q8R4F1; -.
DR   ProteomicsDB; 293768; -. [Q8R4F1-1]
DR   ProteomicsDB; 293769; -. [Q8R4F1-2]
DR   ProteomicsDB; 293770; -. [Q8R4F1-3]
DR   Antibodypedia; 31663; 112 antibodies from 26 providers.
DR   DNASU; 171171; -.
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   VEuPathDB; HostDB:ENSMUSG00000035513; -.
DR   eggNOG; KOG3512; Eukaryota.
DR   GeneTree; ENSGT00940000153601; -.
DR   HOGENOM; CLU_039838_1_0_1; -.
DR   InParanoid; Q8R4F1; -.
DR   OMA; FPNVCDE; -.
DR   PhylomeDB; Q8R4F1; -.
DR   TreeFam; TF333945; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 171171; 2 hits in 58 CRISPR screens.
DR   ChiTaRS; Ntng2; mouse.
DR   PRO; PR:Q8R4F1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8R4F1; protein.
DR   Bgee; ENSMUSG00000035513; Expressed in granulocyte and 80 other tissues.
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:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
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:2001222; P:regulation of neuron migration; IMP:UniProtKB.
DR   GO; GO:0150011; P:regulation of neuron projection arborization; IMP:UniProtKB.
DR   GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   CDD; cd00055; EGF_Lam; 3.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
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; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Laminin EGF-like domain; Lipoprotein; Membrane; Neurogenesis;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..566
FT                   /note="Netrin-G2"
FT                   /id="PRO_0000017097"
FT   PROPEP          567..589
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000017098"
FT   DOMAIN          35..286
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          287..346
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          413..468
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          469..513
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          69..88
FT                   /note="NGL discriminant loop I"
FT                   /evidence="ECO:0000250"
FT   REGION          201..203
FT                   /note="NGL discriminant loop II"
FT                   /evidence="ECO:0000250"
FT   REGION          264..267
FT                   /note="NGL discriminant loop III"
FT                   /evidence="ECO:0000250"
FT   LIPID           566
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..39
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        171..195
FT                   /evidence="ECO:0000250"
FT   DISULFID        287..296
FT                   /evidence="ECO:0000250"
FT   DISULFID        289..305
FT                   /evidence="ECO:0000250"
FT   DISULFID        307..316
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        413..422
FT                   /evidence="ECO:0000255"
FT   DISULFID        415..433
FT                   /evidence="ECO:0000255"
FT   DISULFID        436..445
FT                   /evidence="ECO:0000255"
FT   DISULFID        448..466
FT                   /evidence="ECO:0000255"
FT   DISULFID        469..481
FT                   /evidence="ECO:0000255"
FT   DISULFID        471..487
FT                   /evidence="ECO:0000255"
FT   DISULFID        489..498
FT                   /evidence="ECO:0000255"
FT   DISULFID        501..511
FT                   /evidence="ECO:0000255"
FT   DISULFID        516..529
FT                   /evidence="ECO:0000250"
FT   DISULFID        523..535
FT                   /evidence="ECO:0000250"
FT   DISULFID        537..546
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         353..411
FT                   /note="Missing (in isoform 2A)"
FT                   /evidence="ECO:0000303|PubMed:11804778,
FT                   ECO:0000303|PubMed:11906208"
FT                   /id="VSP_050562"
FT   VAR_SEQ         353..377
FT                   /note="Missing (in isoform 2C)"
FT                   /evidence="ECO:0000303|PubMed:11804778,
FT                   ECO:0000303|PubMed:11906208"
FT                   /id="VSP_050564"
FT   VAR_SEQ         378
FT                   /note="A -> T (in isoform 2C)"
FT                   /evidence="ECO:0000303|PubMed:11804778,
FT                   ECO:0000303|PubMed:11906208"
FT                   /id="VSP_050565"
FT   VAR_SEQ         412
FT                   /note="D -> N (in isoform 2A)"
FT                   /evidence="ECO:0000303|PubMed:11804778,
FT                   ECO:0000303|PubMed:11906208"
FT                   /id="VSP_050563"
FT   CONFLICT        41
FT                   /note="P -> S (in Ref. 2; AAL84788/AAL84789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="S -> F (in Ref. 2; AAL84789)"
FT                   /evidence="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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024