LRRT3_HUMAN
ID LRRT3_HUMAN Reviewed; 581 AA.
AC Q86VH5; A8K2A3; Q2NKX7; Q6N0A3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Leucine-rich repeat transmembrane neuronal protein 3;
DE Flags: Precursor;
GN Name=LRRTM3; ORFNames=UNQ803/PRO1693;
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] (ISOFORM 2), 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] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thalamus;
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] (ISOFORM 1).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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: Exhibits a limited synaptogenic activity in vitro, restricted
CC to excitatory presynaptic differentiation (By similarity). May play a
CC role in the development and maintenance of the vertebrate nervous
CC system. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86VH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VH5-2; Sequence=VSP_014189, VSP_014190;
CC -!- TISSUE SPECIFICITY: Expressed in neuronal tissues.
CC {ECO:0000269|PubMed:12676565}.
CC -!- SIMILARITY: Belongs to the LRRTM family. {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; AY182028; AAO67549.1; -; mRNA.
DR EMBL; AY358315; AAQ88681.1; -; mRNA.
DR EMBL; AK290168; BAF82857.1; -; mRNA.
DR EMBL; BX640611; CAE45717.1; -; mRNA.
DR EMBL; BC111492; AAI11493.1; -; mRNA.
DR EMBL; BC113715; AAI13716.1; -; mRNA.
DR EMBL; BC113717; AAI13718.1; -; mRNA.
DR CCDS; CCDS7270.1; -. [Q86VH5-1]
DR RefSeq; NP_821079.3; NM_178011.4. [Q86VH5-1]
DR AlphaFoldDB; Q86VH5; -.
DR SMR; Q86VH5; -.
DR BioGRID; 131481; 19.
DR STRING; 9606.ENSP00000355187; -.
DR GlyGen; Q86VH5; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q86VH5; -.
DR PhosphoSitePlus; Q86VH5; -.
DR BioMuta; LRRTM3; -.
DR DMDM; 68052341; -.
DR MassIVE; Q86VH5; -.
DR MaxQB; Q86VH5; -.
DR PaxDb; Q86VH5; -.
DR PeptideAtlas; Q86VH5; -.
DR PRIDE; Q86VH5; -.
DR ProteomicsDB; 70020; -. [Q86VH5-1]
DR ProteomicsDB; 70021; -. [Q86VH5-2]
DR Antibodypedia; 14490; 80 antibodies from 24 providers.
DR DNASU; 347731; -.
DR Ensembl; ENST00000361320.5; ENSP00000355187.3; ENSG00000198739.11. [Q86VH5-1]
DR GeneID; 347731; -.
DR KEGG; hsa:347731; -.
DR MANE-Select; ENST00000361320.5; ENSP00000355187.3; NM_178011.5; NP_821079.3.
DR UCSC; uc001jmz.2; human. [Q86VH5-1]
DR CTD; 347731; -.
DR DisGeNET; 347731; -.
DR GeneCards; LRRTM3; -.
DR HGNC; HGNC:19410; LRRTM3.
DR HPA; ENSG00000198739; Tissue enhanced (adrenal gland, brain, ovary, pituitary gland).
DR MIM; 610869; gene.
DR neXtProt; NX_Q86VH5; -.
DR OpenTargets; ENSG00000198739; -.
DR PharmGKB; PA134962991; -.
DR VEuPathDB; HostDB:ENSG00000198739; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160543; -.
DR HOGENOM; CLU_032965_0_0_1; -.
DR InParanoid; Q86VH5; -.
DR OMA; EDTMESH; -.
DR OrthoDB; 650731at2759; -.
DR PhylomeDB; Q86VH5; -.
DR TreeFam; TF332659; -.
DR PathwayCommons; Q86VH5; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 347731; 16 hits in 1010 CRISPR screens.
DR ChiTaRS; LRRTM3; human.
DR GenomeRNAi; 347731; -.
DR Pharos; Q86VH5; Tbio.
DR PRO; PR:Q86VH5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86VH5; protein.
DR Bgee; ENSG00000198739; Expressed in corpus callosum and 83 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IMP:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
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 InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 9.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Glycoprotein; Leucine-rich repeat;
KW Membrane; Postsynaptic cell membrane; Reference proteome; Repeat; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..581
FT /note="Leucine-rich repeat transmembrane neuronal protein
FT 3"
FT /id="PRO_0000018355"
FT TOPO_DOM 31..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..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..226
FT /note="LRR 7"
FT REPEAT 230..251
FT /note="LRR 8"
FT REPEAT 254..275
FT /note="LRR 9"
FT REPEAT 279..300
FT /note="LRR 10"
FT DOMAIN 312..363
FT /note="LRRCT"
FT REGION 377..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 513
FT /note="I -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12676565,
FT ECO:0000303|PubMed:12975309"
FT /id="VSP_014189"
FT VAR_SEQ 514..581
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12676565,
FT ECO:0000303|PubMed:12975309"
FT /id="VSP_014190"
FT CONFLICT 266
FT /note="E -> G (in Ref. 4; CAE45717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 65896 MW; A025CF13AA663730 CRC64;
MGFNVIRLLS GSAVALVIAP TVLLTMLSSA ERGCPKGCRC EGKMVYCESQ KLQEIPSSIS
AGCLGLSLRY NSLQKLKYNQ FKGLNQLTWL YLDHNHISNI DENAFNGIRR LKELILSSNR
ISYFLNNTFR PVTNLRNLDL SYNQLHSLGS EQFRGLRKLL SLHLRSNSLR TIPVRIFQDC
RNLELLDLGY NRIRSLARNV FAGMIRLKEL HLEHNQFSKL NLALFPRLVS LQNLYLQWNK
ISVIGQTMSW TWSSLQRLDL SGNEIEAFSG PSVFQCVPNL QRLNLDSNKL TFIGQEILDS
WISLNDISLA GNIWECSRNI CSLVNWLKSF KGLRENTIIC ASPKELQGVN VIDAVKNYSI
CGKSTTERFD LARALPKPTF KPKLPRPKHE SKPPLPPTVG ATEPGPETDA DAEHISFHKI
IAGSVALFLS VLVILLVIYV SWKRYPASMK QLQQRSLMRR HRKKKRQSLK QMTPSTQEFY
VDYKPTNTET SEMLLNGTGP CTYNKSGSRE CEIPLSMNVS TFLAYDQPTI SYCGVHHELL
SHKSFETNAQ EDTMETHLET ELDLSTITTA GRISDHKQQL A