LRRT1_MOUSE
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 03-AUG-2022, entry version 168.
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";
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; 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 GlyGen; Q8K377; 4 sites.
DR PhosphoSitePlus; Q8K377; -.
DR SwissPalm; Q8K377; -.
DR MaxQB; Q8K377; -.
DR PaxDb; Q8K377; -.
DR PeptideAtlas; Q8K377; -.
DR PRIDE; Q8K377; -.
DR ProteomicsDB; 252530; -.
DR Antibodypedia; 47487; 244 antibodies from 28 providers.
DR DNASU; 74342; -.
DR Ensembl; ENSMUST00000020400; ENSMUSP00000020400; ENSMUSG00000060780.
DR Ensembl; ENSMUST00000159616; ENSMUSP00000125207; ENSMUSG00000060780.
DR Ensembl; ENSMUST00000161677; ENSMUSP00000124373; ENSMUSG00000060780.
DR GeneID; 74342; -.
DR KEGG; mmu:74342; -.
DR UCSC; uc009cjt.1; mouse.
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; LEWTWHF; -.
DR OrthoDB; 412279at2759; -.
DR PhylomeDB; Q8K377; -.
DR TreeFam; TF332659; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 74342; 1 hit in 70 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 206 other tissues.
DR ExpressionAtlas; Q8K377; baseline and differential.
DR Genevisible; Q8K377; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099060; C:integral component of 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; -; 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; 9.
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
