ID   LRRT1_MOUSE             Reviewed;         522 AA.
AC   Q8K377; Q3UVX1;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Leucine-rich repeat transmembrane neuronal protein 1;
DE   Flags: Precursor;
GN   Name=Lrrtm1;
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; TISSUE=Diencephalon, and Eye;
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   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16860615; DOI=10.1016/j.modgep.2006.05.004;
RA   Haines B.P., Rigby P.W.J.;
RT   "Developmentally regulated expression of the LRRTM gene family during mid-
RT   gestation mouse embryogenesis.";
RL   Gene Expr. Patterns 7:23-29(2007).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   DOI=10.1038/sj.mp.4002116;
RA   Francks C., Maegawa S., Lauren J., Abrahams B.S., Velayos-Baeza A.,
RA   Medland S.E., Colella S., Groszer M., McAuley E.Z., Caffrey T.M.,
RA   Timmusk T., Pruunsild P., Koppel I., Lind P.A., Matsumoto-Itaba N.,
RA   Nicod J., Xiong L., Joober R., Enard W., Krinsky B., Nanba E.,
RA   Richardson A.J., Riley B.P., Martin N.G., Strittmatter S.M., Moeller H.J.,
RA   Rujescu D., St Clair D., Muglia P., Roos J.L., Fisher S.E.,
RA   Wade-Martins R., Rouleau G.A., Stein J.F., Karayiorgou M., Geschwind D.H.,
RA   Ragoussis J., Kendler K.S., Airaksinen M.S., Oshimura M., DeLisi L.E.,
RA   Monaco A.P.;
RT   "LRRTM1 protein is located in the endoplasmic reticulum (ER) in mammalian
RT   cells.";
RL   Mol. Psychiatry 12:1057-1057(2007).
RN   [6]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=17667961; DOI=10.1038/sj.mp.4002053;
RA   Francks C., Maegawa S., Lauren J., Abrahams B.S., Velayos-Baeza A.,
RA   Medland S.E., Colella S., Groszer M., McAuley E.Z., Caffrey T.M.,
RA   Timmusk T., Pruunsild P., Koppel I., Lind P.A., Matsumoto-Itaba N.,
RA   Nicod J., Xiong L., Joober R., Enard W., Krinsky B., Nanba E.,
RA   Richardson A.J., Riley B.P., Martin N.G., Strittmatter S.M., Moeller H.J.,
RA   Rujescu D., St Clair D., Muglia P., Roos J.L., Fisher S.E.,
RA   Wade-Martins R., Rouleau G.A., Stein J.F., Karayiorgou M., Geschwind D.H.,
RA   Ragoussis J., Kendler K.S., Airaksinen M.S., Oshimura M., DeLisi L.E.,
RA   Monaco A.P.;
RT   "LRRTM1 on chromosome 2p12 is a maternally suppressed gene that is
RT   associated paternally with handedness and schizophrenia.";
RL   Mol. Psychiatry 12:1129-1139(2007).
RN   [7]
RP   DISRUPTION PHENOTYPE.
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).
CC   -!- FUNCTION: Exhibits strong synaptogenic activity, restricted to
CC       excitatory presynaptic differentiation, acting at both pre- and
CC       postsynaptic level. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Postsynaptic cell membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Note=Accumulates extensively in the endoplasmic reticulum of
CC       transfected nonneuronal cells. {ECO:0000269|PubMed:17667961,
CC       ECO:0000269|Ref.5}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the nervous system by
CC       postmitotic neurons, but also in some non-neuronal tissues. In adult
CC       brain expression is most prominent in the forebraain, particularly in
CC       the thalamus and in the cortical areas including hippocampus, piriform
CC       and posterior cingulate. {ECO:0000269|PubMed:12676565,
CC       ECO:0000269|PubMed:17667961}.
CC   -!- DEVELOPMENTAL STAGE: Initially detected at 9 dpc with expression
CC       present in the overlying ectoderm of the limb bud in the presumptive
CC       apical ectodermal ridge. Expression is also seen in the dorsal otic
CC       vesicle in the presumptive endolymphatic appendage. Neural expression
CC       is present in the forebrain and midbrain with a sharp boundary across
CC       the central midbrain. Expression is also seen in the hindbrain. A
CC       stripe of expression can be detected in the neural tube. At 10 and 11
CC       dpc expression is restricted to the apical ectodermal ridge. Expression
CC       persists in the endolymphatic diverticular appendage of the otic
CC       vesicle the forebrain/midbrain and the ventricular layer of the central
CC       neural tube through these stages. {ECO:0000269|PubMed:16860615}.
CC   -!- DISRUPTION PHENOTYPE: Mutant animals survive in the expected Mendelian
CC       ratios, are fertile and display no overt phenotype. Brain morphology
CC       appears grossly normal, except for rare cases of anomalous
CC       ventroculomegaly. Increase in the presynaptic area occupied by
CC       SLC17A7/VGLUT1 in some strata of the hippocampal neuropil of the CA1
CC       region. {ECO:0000269|PubMed:19285470}.
CC   -!- SIMILARITY: Belongs to the LRRTM family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The hands to say it - Issue
CC       91 of February 2008;
CC       URL="https://web.expasy.org/spotlight/back_issues/091";
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DR   EMBL; AY182025; AAO67546.1; -; mRNA.
DR   EMBL; AK053345; BAC35354.1; -; mRNA.
DR   EMBL; AK053364; BAC35363.1; -; mRNA.
DR   EMBL; AK136857; BAE23148.1; -; mRNA.
DR   EMBL; BC027803; AAH27803.1; -; mRNA.
DR   CCDS; CCDS39522.1; -.
DR   RefSeq; NP_083156.2; NM_028880.3.
DR   RefSeq; XP_006506775.1; XM_006506712.1.
DR   AlphaFoldDB; Q8K377; -.
DR   SMR; Q8K377; -.
DR   BioGRID; 216677; 1.
DR   IntAct; Q8K377; 3.
DR   MINT; Q8K377; -.
DR   STRING; 10090.ENSMUSP00000125207; -.
DR   GlyCosmos; Q8K377; 4 sites, No reported glycans.
DR   GlyGen; Q8K377; 5 sites, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; Q8K377; -.
DR   SwissPalm; Q8K377; -.
DR   MaxQB; Q8K377; -.
DR   PaxDb; 10090-ENSMUSP00000125207; -.
DR   PeptideAtlas; Q8K377; -.
DR   ProteomicsDB; 252530; -.
DR   Antibodypedia; 47487; 280 antibodies from 28 providers.
DR   DNASU; 74342; -.
DR   Ensembl; ENSMUST00000020400.5; ENSMUSP00000020400.5; ENSMUSG00000060780.3.
DR   Ensembl; ENSMUST00000159616.2; ENSMUSP00000125207.2; ENSMUSG00000060780.3.
DR   Ensembl; ENSMUST00000161677.2; ENSMUSP00000124373.2; ENSMUSG00000060780.3.
DR   GeneID; 74342; -.
DR   KEGG; mmu:74342; -.
DR   UCSC; uc009cjt.1; mouse.
DR   AGR; MGI:2389173; -.
DR   CTD; 347730; -.
DR   MGI; MGI:2389173; Lrrtm1.
DR   VEuPathDB; HostDB:ENSMUSG00000060780; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000161705; -.
DR   HOGENOM; CLU_032965_0_0_1; -.
DR   InParanoid; Q8K377; -.
DR   OMA; FHLCEDA; -.
DR   OrthoDB; 5344967at2759; -.
DR   PhylomeDB; Q8K377; -.
DR   TreeFam; TF332659; -.
DR   Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR   BioGRID-ORCS; 74342; 1 hit in 75 CRISPR screens.
DR   ChiTaRS; Lrrtm1; mouse.
DR   PRO; PR:Q8K377; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8K377; Protein.
DR   Bgee; ENSMUSG00000060780; Expressed in lateral geniculate body and 208 other cell types or tissues.
DR   ExpressionAtlas; Q8K377; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISS:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; ISO:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR   GO; GO:0035640; P:exploration behavior; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP: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:0035418; P:protein localization to synapse; IMP:MGI.
DR   GO; GO:0031623; P:receptor internalization; IGI:MGI.
DR   GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR   GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP: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:SF290; LEUCINE-RICH REPEAT TRANSMEMBRANE NEURONAL PROTEIN 1; 1.
DR   PANTHER; PTHR24373; SLIT RELATED LEUCINE-RICH REPEAT NEURONAL PROTEIN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 9.
DR   Genevisible; Q8K377; 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..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..522
FT                   /note="Leucine-rich repeat transmembrane neuronal protein
FT                   1"
FT                   /id="PRO_0000018351"
FT   TOPO_DOM        35..427
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        449..522
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..63
FT                   /note="LRRNT"
FT   REPEAT          64..87
FT                   /note="LRR 1"
FT   REPEAT          89..111
FT                   /note="LRR 2"
FT   REPEAT          112..135
FT                   /note="LRR 3"
FT   REPEAT          136..159
FT                   /note="LRR 4"
FT   REPEAT          161..183
FT                   /note="LRR 5"
FT   REPEAT          184..207
FT                   /note="LRR 6"
FT   REPEAT          209..231
FT                   /note="LRR 7"
FT   REPEAT          233..255
FT                   /note="LRR 8"
FT   REPEAT          256..278
FT                   /note="LRR 9"
FT   REPEAT          280..302
FT                   /note="LRR 10"
FT   DOMAIN          314..365
FT                   /note="LRRCT"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   522 AA;  58718 MW;  6EBBA18034539DCC CRC64;
     MDFLLLGLCL HWLLRRPSGV VLCLLGACFQ MLPAAPSGCP GQCRCEGRLL YCEALNLTEA
     PHNLSGLLGL SLRYNSLSEL RAGQFTGLMQ LTWLYLDHNH ICSVQGDAFQ KLRRVKELTL
     SSNQITELAN TTFRPMPNLR SVDLSYNKLQ ALAPDLFHGL RKLTTLHMRA NAIQFVPVRI
     FQDCRSLKFL DIGYNQLKSL ARNSFAGLFK LTELHLEHND LIKVNFAHFP RLISLHSLCL
     RRNKVAIVVS SLDWVWNLEK MDLSGNEIEY MEPHVFETVP YLQTLQLDSN RLTYIEPRIL
     NSWKSLTSIT LAGNLWDCGR NVCALASWLS NFQGRYDANL QCASPEYAQG EDVLDAVYAF
     HLCEDGAEPT SGHLLSVAVT NRSDLTPPES SATTLVDGGE GHDGTFEPIT VALPGGEHAE
     NAVQIHKVVT GTMALIFSFL IVVLVLYVSW KCFPASLRQL RQCFVTQRRK QKQKQTMHQM
     AAMSAQEYYV DYKPNHIEGA LVIINEYGSC TCHQQPAREC EV
//