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Database: UniProt
Entry: O43300
LinkDB: O43300
Original site: O43300 
ID   LRRT2_HUMAN             Reviewed;         516 AA.
AC   O43300; A0AVL3; A8K4U9; B7ZLN8; Q7L770;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 3.
DT   07-APR-2021, entry version 159.
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; Synonyms=KIAA0416, LRRN2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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   TISSUE=Brain;
RX   PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA   Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT   new cDNA clones from brain which code for large proteins in vitro.";
RL   DNA Res. 4:307-313(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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).
CC   -!- FUNCTION: Involved in the development and maintenance of excitatory
CC       synapse 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}.
CC   -!- SUBUNIT: Interacts with DLG4 and NRXN1. {ECO:0000250}.
CC   -!- INTERACTION:
CC       O43300; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-18096461, EBI-10171534;
CC       O43300; P01375: TNF; NbExp=3; IntAct=EBI-18096461, EBI-359977;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell junction, synapse, postsynaptic cell membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Note=Localized to excitatory synapses. {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=BAA24846.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY182026; AAO67547.1; -; mRNA.
DR   EMBL; AB007876; BAA24846.2; ALT_INIT; mRNA.
DR   EMBL; AK291064; BAF83753.1; -; mRNA.
DR   EMBL; BC126408; AAI26409.1; -; mRNA.
DR   EMBL; BC126410; AAI26411.1; -; mRNA.
DR   EMBL; BC143926; AAI43927.1; -; mRNA.
DR   CCDS; CCDS47272.1; -.
DR   RefSeq; NP_056379.1; NM_015564.2.
DR   PDB; 5Z8X; X-ray; 3.15 A; A/B/C/D=34-373.
DR   PDB; 5Z8Y; X-ray; 3.40 A; A/C/E/G=34-371.
DR   PDBsum; 5Z8X; -.
DR   PDBsum; 5Z8Y; -.
DR   SMR; O43300; -.
DR   BioGRID; 117508; 16.
DR   IntAct; O43300; 10.
DR   MINT; O43300; -.
DR   STRING; 9606.ENSP00000274711; -.
DR   GlyGen; O43300; 4 sites.
DR   iPTMnet; O43300; -.
DR   PhosphoSitePlus; O43300; -.
DR   BioMuta; LRRTM2; -.
DR   MassIVE; O43300; -.
DR   PaxDb; O43300; -.
DR   PeptideAtlas; O43300; -.
DR   PRIDE; O43300; -.
DR   ProteomicsDB; 48875; -.
DR   ABCD; O43300; 1 sequenced antibody.
DR   Antibodypedia; 57042; 151 antibodies.
DR   DNASU; 26045; -.
DR   Ensembl; ENST00000274711; ENSP00000274711; ENSG00000146006.
DR   GeneID; 26045; -.
DR   KEGG; hsa:26045; -.
DR   UCSC; uc011cyz.2; human.
DR   CTD; 26045; -.
DR   DisGeNET; 26045; -.
DR   GeneCards; LRRTM2; -.
DR   HGNC; HGNC:19409; LRRTM2.
DR   HPA; ENSG00000146006; Tissue enriched (brain).
DR   MIM; 610868; gene.
DR   neXtProt; NX_O43300; -.
DR   OpenTargets; ENSG00000146006; -.
DR   PharmGKB; PA134993038; -.
DR   VEuPathDB; HostDB:ENSG00000146006.7; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000160581; -.
DR   HOGENOM; CLU_032965_0_0_1; -.
DR   InParanoid; O43300; -.
DR   OMA; VYGFQLC; -.
DR   PhylomeDB; O43300; -.
DR   TreeFam; TF332659; -.
DR   PathwayCommons; O43300; -.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   BioGRID-ORCS; 26045; 8 hits in 980 CRISPR screens.
DR   ChiTaRS; LRRTM2; human.
DR   GenomeRNAi; 26045; -.
DR   Pharos; O43300; Tbio.
DR   PRO; PR:O43300; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; O43300; protein.
DR   Bgee; ENSG00000146006; Expressed in frontal cortex and 156 other tissues.
DR   ExpressionAtlas; O43300; baseline and differential.
DR   Genevisible; O43300; HS.
DR   GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0042043; F:neurexin family protein binding; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0002091; P:negative regulation of receptor internalization; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0099151; P:regulation of postsynaptic density assembly; IEA:Ensembl.
DR   GO; GO:0050808; P:synapse organization; IEA:Ensembl.
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   3D-structure; Cell junction; Cell membrane; Glycoprotein;
KW   Leucine-rich repeat; Membrane; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..516
FT                   /note="Leucine-rich repeat transmembrane neuronal protein
FT                   2"
FT                   /id="PRO_0000018353"
FT   TOPO_DOM        34..422
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        444..516
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           513..516
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"
FT   CONFLICT        334
FT                   /note="E -> G (in Ref. 3; BAF83753)"
FT                   /evidence="ECO:0000305"
FT   STRAND          41..46
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          64..67
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   TURN            78..81
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          88..91
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   TURN            102..107
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          113..115
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   TURN            126..131
FT                   /evidence="ECO:0007744|PDB:5Z8Y"
FT   STRAND          137..139
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   TURN            150..155
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          161..163
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   TURN            174..179
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          185..187
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   TURN            198..203
FT                   /evidence="ECO:0007744|PDB:5Z8Y"
FT   STRAND          209..211
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          219..221
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   HELIX           222..225
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          233..235
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          243..245
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          257..259
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   TURN            270..275
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          281..283
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   HELIX           294..297
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          304..307
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   HELIX           317..319
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   HELIX           320..328
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   STRAND          331..335
FT                   /evidence="ECO:0007744|PDB:5Z8Y"
FT   TURN            343..347
FT                   /evidence="ECO:0007744|PDB:5Z8X"
FT   HELIX           350..356
FT                   /evidence="ECO:0007744|PDB:5Z8X"
SQ   SEQUENCE   516 AA;  59076 MW;  F2EDD45C854BC3A6 CRC64;
     MGLHFKWPLG APMLAAIYAM SMVLKMLPAL GMACPPKCRC EKLLFYCDSQ GFHSVPNATD
     KGSLGLSLRH NHITELERDQ FASFSQLTWL HLDHNQISTV KEDAFQGLYK LKELILSSNK
     IFYLPNTTFT QLINLQNLDL SFNQLSSLHP ELFYGLRKLQ TLHLRSNSLR TIPVRLFWDC
     RSLEFLDLST NRLRSLARNG FAGLIKLREL HLEHNQLTKI NFAHFLRLSS LHTLFLQWNK
     ISNLTCGMEW TWGTLEKLDL TGNEIKAIDL TVFETMPNLK ILLMDNNKLN SLDSKILNSL
     RSLTTVGLSG NLWECSARIC ALASWLGSFQ GRWEHSILCH SPDHTQGEDI LDAVHGFQLC
     WNLSTTVTVM ATTYRDPTTE YTKRISSSSY HVGDKEIPTT AGIAVTTEEH FPEPDNAIFT
     QRVITGTMAL LFSFFFIIFI VFISRKCCPP TLRRIRQCSM VQNHRQLRSQ TRLHMSNMSD
     QGPYNEYEPT HEGPFIIING YGQCKCQQLP YKECEV
//
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