LRRT2_HUMAN
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 03-AUG-2022, entry version 164.
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. 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=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 AlphaFoldDB; O43300; -.
DR SMR; O43300; -.
DR BioGRID; 117508; 21.
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; 158 antibodies from 28 providers.
DR DNASU; 26045; -.
DR Ensembl; ENST00000274711.7; ENSP00000274711.5; ENSG00000146006.8.
DR GeneID; 26045; -.
DR KEGG; hsa:26045; -.
DR MANE-Select; ENST00000274711.7; ENSP00000274711.5; NM_015564.3; NP_056379.1.
DR UCSC; uc011cyz.2; human.
DR CTD; 26045; -.
DR DisGeNET; 26045; -.
DR GeneCards; LRRTM2; -.
DR HGNC; HGNC:19409; LRRTM2.
DR HPA; ENSG00000146006; Group enriched (brain, retina).
DR MIM; 610868; gene.
DR neXtProt; NX_O43300; -.
DR OpenTargets; ENSG00000146006; -.
DR PharmGKB; PA134993038; -.
DR VEuPathDB; HostDB:ENSG00000146006; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160581; -.
DR HOGENOM; CLU_032965_0_0_1; -.
DR InParanoid; O43300; -.
DR OMA; ECSPKIC; -.
DR PhylomeDB; O43300; -.
DR TreeFam; TF332659; -.
DR PathwayCommons; O43300; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; O43300; -.
DR BioGRID-ORCS; 26045; 11 hits in 1062 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 lateral nuclear group of thalamus and 149 other tissues.
DR ExpressionAtlas; O43300; baseline and differential.
DR Genevisible; O43300; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 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..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:0007829|PDB:5Z8X"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5Z8X"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:5Z8X"
FT TURN 102..107
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5Z8X"
FT TURN 126..131
FT /evidence="ECO:0007829|PDB:5Z8Y"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5Z8X"
FT TURN 150..155
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5Z8X"
FT TURN 174..179
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5Z8X"
FT TURN 198..203
FT /evidence="ECO:0007829|PDB:5Z8Y"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5Z8X"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5Z8X"
FT TURN 270..275
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:5Z8X"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:5Z8X"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5Z8X"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:5Z8X"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5Z8Y"
FT TURN 343..347
FT /evidence="ECO:0007829|PDB:5Z8X"
FT HELIX 350..356
FT /evidence="ECO:0007829|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
