ID   LRRT2_MOUSE             Reviewed;         515 AA.
AC   Q8BGA3; Q80U08;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Leucine-rich repeat transmembrane neuronal protein 2;
DE   Flags: Precursor;
GN   Name=Lrrtm2; Synonyms=Kiaa0416;
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=C57BL/6J;
RX   PubMed=12676565; DOI=10.1016/s0888-7543(03)00030-2;
RA   Lauren J., Airaksinen M.S., Saarma M., Timmusk T.T.;
RT   "A novel gene family encoding leucine-rich repeat transmembrane proteins
RT   differentially expressed in the nervous system.";
RL   Genomics 81:411-421(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Cerebellum, Hippocampus, Medulla oblongata, and
RC   Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Involved in the development and maintenance of excitatory
CC       synapses in the vertebrate nervous system. Regulates surface expression
CC       of AMPA receptors and instructs the development of functional glutamate
CC       release sites. Acts as a ligand for the presynaptic receptors NRXN1-A
CC       and NRXN1-B (By similarity). {ECO:0000250|UniProtKB:D4A7P2}.
CC   -!- SUBUNIT: Interacts with DLG4. Interacts with neurexin NRXN1;
CC       interaction is mediated by heparan sulfate glycan modification on
CC       neurexin. {ECO:0000250|UniProtKB:D4A7P2}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Postsynaptic cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Note=Localized to excitatory synapses.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in neuronal tissues.
CC       {ECO:0000269|PubMed:12676565}.
CC   -!- DOMAIN: Synaptogenic effects are mediated by the extracellular LRR
CC       region. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LRRTM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65560.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AY182027; AAO67548.1; -; mRNA.
DR   EMBL; AK043173; BAC31484.1; -; mRNA.
DR   EMBL; AK043784; BAC31653.1; -; mRNA.
DR   EMBL; AK044705; BAC32042.1; -; mRNA.
DR   EMBL; AK046818; BAC32883.1; -; mRNA.
DR   EMBL; AK049920; BAC33985.1; -; mRNA.
DR   EMBL; AK122278; BAC65560.1; ALT_INIT; mRNA.
DR   CCDS; CCDS50251.1; -.
DR   RefSeq; NP_821072.1; NM_178005.4.
DR   AlphaFoldDB; Q8BGA3; -.
DR   SASBDB; Q8BGA3; -.
DR   SMR; Q8BGA3; -.
DR   BioGRID; 223196; 1.
DR   STRING; 10090.ENSMUSP00000089225; -.
DR   GlyCosmos; Q8BGA3; 4 sites, No reported glycans.
DR   GlyGen; Q8BGA3; 5 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BGA3; -.
DR   PhosphoSitePlus; Q8BGA3; -.
DR   SwissPalm; Q8BGA3; -.
DR   PaxDb; 10090-ENSMUSP00000089225; -.
DR   PeptideAtlas; Q8BGA3; -.
DR   ProteomicsDB; 290176; -.
DR   ABCD; Q8BGA3; 1 sequenced antibody.
DR   Antibodypedia; 57042; 168 antibodies from 29 providers.
DR   DNASU; 107065; -.
DR   Ensembl; ENSMUST00000091636.5; ENSMUSP00000089225.4; ENSMUSG00000071862.4.
DR   GeneID; 107065; -.
DR   KEGG; mmu:107065; -.
DR   UCSC; uc008ema.2; mouse.
DR   AGR; MGI:2389174; -.
DR   CTD; 26045; -.
DR   MGI; MGI:2389174; Lrrtm2.
DR   VEuPathDB; HostDB:ENSMUSG00000071862; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000160581; -.
DR   HOGENOM; CLU_032965_0_0_1; -.
DR   InParanoid; Q8BGA3; -.
DR   OMA; DMWQSLG; -.
DR   OrthoDB; 2875365at2759; -.
DR   PhylomeDB; Q8BGA3; -.
DR   TreeFam; TF332659; -.
DR   Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR   BioGRID-ORCS; 107065; 2 hits in 75 CRISPR screens.
DR   PRO; PR:Q8BGA3; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q8BGA3; Protein.
DR   Bgee; ENSMUSG00000071862; Expressed in lateral geniculate body and 112 other cell types or tissues.
DR   ExpressionAtlas; Q8BGA3; baseline and differential.
DR   GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISS:MGI.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; ISO:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR   GO; GO:0042043; F:neurexin family protein binding; ISO:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IGI:MGI.
DR   GO; GO:0002091; P:negative regulation of receptor internalization; IGI:MGI.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR   GO; GO:0050808; P:synapse organization; IGI:MGI.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR24373:SF268; LEUCINE RICH REPEAT TRANSMEMBRANE NEURONAL 2; 1.
DR   PANTHER; PTHR24373; SLIT RELATED LEUCINE-RICH REPEAT NEURONAL PROTEIN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 10.
DR   Genevisible; Q8BGA3; MM.
PE   2: Evidence at transcript 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_0000018354"
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   DOMAIN          34..61
FT                   /note="LRRNT"
FT   REPEAT          63..83
FT                   /note="LRR 1"
FT   REPEAT          86..107
FT                   /note="LRR 2"
FT   REPEAT          110..131
FT                   /note="LRR 3"
FT   REPEAT          134..155
FT                   /note="LRR 4"
FT   REPEAT          158..179
FT                   /note="LRR 5"
FT   REPEAT          182..203
FT                   /note="LRR 6"
FT   REPEAT          206..227
FT                   /note="LRR 7"
FT   REPEAT          230..251
FT                   /note="LRR 8"
FT   REPEAT          254..275
FT                   /note="LRR 9"
FT   REPEAT          278..299
FT                   /note="LRR 10"
FT   DOMAIN          311..362
FT                   /note="LRRCT"
FT   MOTIF           512..515
FT                   /note="Involved in DLG4-binding"
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   515 AA;  58816 MW;  B0EE6888A99F31C9 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
     ISNLTCGMDW TWSTLEKLDL TGNEIKAIDL TVFETMPNLK ILLMDNNKLN SLDSKILNSL
     KSLTTVGLSG NLWECSPRVC ALASWLGSFQ GRWEHSILCH SPDHTQGEDI LDAVHGFQLC
     WNLSTTVTAM ATTYRDPTTE YTKISSSSYH VGDKEIPTTA GIAVTTEEHF PEPDNAIFTQ
     RVITGTMALL FSFFFIIFIV FISRKCCPPT LRRIRQCSMI QNHRQLRSQT RLHMSNMSDQ
     GPYNEYEPTH EGPFIIINGY GQCKCQQLPY KECEV
//