LRRT2_RAT
ID LRRT2_RAT Reviewed; 515 AA.
AC D4A7P2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Leucine-rich repeat transmembrane neuronal protein 2;
DE AltName: Full=Leucine-rich repeat neuronal 2 protein;
DE Flags: Precursor;
GN Name=Lrrtm2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [2]
RP FUNCTION, INTERACTION WITH DLG4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF 512-GLU--VAL-515.
RX PubMed=19285470; DOI=10.1016/j.neuron.2009.01.017;
RA Linhoff M.W., Lauren J., Cassidy R.M., Dobie F.A., Takahashi H.,
RA Nygaard H.B., Airaksinen M.S., Strittmatter S.M., Craig A.M.;
RT "An unbiased expression screen for synaptogenic proteins identifies the
RT LRRTM protein family as synaptic organizers.";
RL Neuron 61:734-749(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DLG4 AND NRXN1.
RX PubMed=20064388; DOI=10.1016/j.neuron.2009.12.019;
RA de Wit J., Sylwestrak E., O'Sullivan M.L., Otto S., Tiglio K., Savas J.N.,
RA Yates J.R. III, Comoletti D., Taylor P., Ghosh A.;
RT "LRRTM2 interacts with Neurexin1 and regulates excitatory synapse
RT formation.";
RL Neuron 64:799-806(2009).
CC -!- FUNCTION: Involved in the development and maintenance of excitatory
CC synapse in the nervous system. Regulates surface expression of AMPA
CC receptors and instructs the development of functional glutamate release
CC sites. Acts as a ligand for the presynaptic receptors NRXN1-A and
CC NRXN1-B. {ECO:0000269|PubMed:19285470, ECO:0000269|PubMed:20064388}.
CC -!- SUBUNIT: Interacts with DLG4 and NRXN1. {ECO:0000269|PubMed:19285470,
CC ECO:0000269|PubMed:20064388}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Postsynaptic cell membrane; Single-pass type I membrane
CC protein. Note=Localized to excitatory synapses.
CC -!- TISSUE SPECIFICITY: Expressed in neuronal tissues. Widely distributed
CC in neuropil regions in discrete puncta throughout the brain (at protein
CC level). Detected in cortex, thalamus, striatum, olfactory bulb,
CC cerebellum and all hippocampal subfields (at protein level). More
CC abundant in deep than in superficial layers of neocortex (at protein
CC level). {ECO:0000269|PubMed:19285470}.
CC -!- DOMAIN: Synaptogenic effects are mediated by the extracellular LRR
CC region.
CC -!- SIMILARITY: Belongs to the LRRTM family. {ECO:0000305}.
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DR EMBL; CH473974; EDL76254.1; -; Genomic_DNA.
DR RefSeq; NP_001102939.1; NM_001109469.1.
DR AlphaFoldDB; D4A7P2; -.
DR SMR; D4A7P2; -.
DR STRING; 10116.ENSRNOP00000067172; -.
DR GlyGen; D4A7P2; 4 sites.
DR iPTMnet; D4A7P2; -.
DR PhosphoSitePlus; D4A7P2; -.
DR PaxDb; D4A7P2; -.
DR PRIDE; D4A7P2; -.
DR ABCD; D4A7P2; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000075420; ENSRNOP00000067172; ENSRNOG00000047085.
DR GeneID; 685472; -.
DR KEGG; rno:685472; -.
DR UCSC; RGD:1593785; rat.
DR CTD; 26045; -.
DR RGD; 1593785; Lrrtm2.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160581; -.
DR HOGENOM; CLU_032965_0_0_1; -.
DR InParanoid; D4A7P2; -.
DR OMA; ECSPKIC; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; D4A7P2; -.
DR TreeFam; TF332659; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:D4A7P2; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Proteomes; UP000234681; Chromosome 18.
DR Bgee; ENSRNOG00000047085; Expressed in brain and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0042043; F:neurexin family protein binding; IPI:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0002091; P:negative regulation of receptor internalization; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:0050808; P:synapse organization; IDA:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 9.
DR PROSITE; PS51450; LRR; 10.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..515
FT /note="Leucine-rich repeat transmembrane neuronal protein
FT 2"
FT /id="PRO_0000405434"
FT TOPO_DOM 34..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 61..83
FT /note="LRR 1"
FT REPEAT 84..107
FT /note="LRR 2"
FT REPEAT 109..131
FT /note="LRR 3"
FT REPEAT 132..155
FT /note="LRR 4"
FT REPEAT 156..179
FT /note="LRR 5"
FT REPEAT 181..203
FT /note="LRR 6"
FT REPEAT 205..227
FT /note="LRR 7"
FT REPEAT 229..251
FT /note="LRR 8"
FT REPEAT 252..275
FT /note="LRR 9"
FT REPEAT 276..299
FT /note="LRR 10"
FT MOTIF 512..515
FT /note="Involved in DLG4-binding"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 512..515
FT /note="Missing: Loss of DLG4-binding."
FT /evidence="ECO:0000269|PubMed:19285470"
SQ SEQUENCE 515 AA; 58804 MW; DA8E14ACE61F7714 CRC64;
MGLHFKWPLG APMLAAIYAM SVVLKMLPAL GMACPPKCRC EKLLFYCDSQ GFHSVPNATD
KGSLGLSLRH NHITALERDQ FASFSQLTWL HLDHNQISTV KEDAFQGLYK LKELILSSNK
IFYLPNTTFT QLINLQNLDL SFNQLSSLHP ELFYGLRKLQ TLHLRSNSLR TIPVRLFWDC
RSLEFLDLST NRLRSLARNG FAGLIKLREL HLEHNQLTKI NFAHFLRLSS LHTLFLQWNK
ISNLTCGMEW TWSTLEKLDL TGNEIKAIDL TVFETMPNLK ILLMDNNKLN SLDSKILSSL
RSLTTVGLSG NLWECSPRVC ALASWLGSFQ GRWEHSILCH SPDHTQGEDI LDAVHGFQLC
WNLSTTVTAM ATTYRDPTTE YTKISSSSYH VGDKEIPTTA GIAVTTEEHF PEPDNAIFTQ
RVITGTMALL FSFFFIIFIV FISRKCCPPT LRRIRQCSMI QNHRQLRSQT RLHMSNMSDQ
GPYSEYEPTH EGPFIIINGY GQCKCQQLPY KECEV
