LRIT3_MOUSE
ID LRIT3_MOUSE Reviewed; 681 AA.
AC W8DXL4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 3 {ECO:0000305};
DE Flags: Precursor;
GN Name=Lrit3 {ECO:0000312|MGI:MGI:2685267};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6JRj {ECO:0000312|EMBL:AHI87499.1};
RX PubMed=24598786; DOI=10.1371/journal.pone.0090342;
RA Neuille M., El Shamieh S., Orhan E., Michiels C., Antonio A.,
RA Lancelot M.E., Condroyer C., Bujakowska K., Poch O., Sahel J.A., Audo I.,
RA Zeitz C.;
RT "Lrit3 deficient mouse (nob6): a novel model of complete congenital
RT stationary night blindness (cCSNB).";
RL PLoS ONE 9:E90342-E90342(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25997951; DOI=10.1111/ejn.12959;
RA Neuille M., Morgans C.W., Cao Y., Orhan E., Michiels C., Sahel J.A.,
RA Audo I., Duvoisin R.M., Martemyanov K.A., Zeitz C.;
RT "LRIT3 is essential to localize TRPM1 to the dendritic tips of depolarizing
RT bipolar cells and may play a role in cone synapse formation.";
RL Eur. J. Neurosci. 42:1966-1975(2015).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF LEU-134.
RX PubMed=26427409; DOI=10.1007/978-3-319-17121-0_24;
RA Charette J.R., Samuels I.S., Yu M., Stone L., Hicks W., Shi L.Y.,
RA Krebs M.P., Naggert J.K., Nishina P.M., Peachey N.S.;
RT "A Chemical Mutagenesis Screen Identifies Mouse Models with ERG Defects.";
RL Adv. Exp. Med. Biol. 854:177-183(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28334377; DOI=10.1167/iovs.16-20745;
RA Neuille M., Cao Y., Caplette R., Guerrero-Given D., Thomas C., Kamasawa N.,
RA Sahel J.A., Hamel C.P., Audo I., Picaud S., Martemyanov K.A., Zeitz C.;
RT "LRIT3 Differentially Affects Connectivity and Synaptic Transmission of
RT Cones to ON- and OFF-Bipolar Cells.";
RL Invest. Ophthalmol. Vis. Sci. 58:1768-1778(2017).
CC -!- FUNCTION: Plays a role in the synapse formation and synaptic
CC transmission between cone photoreceptor cells and retinal bipolar cells
CC (PubMed:25997951, PubMed:26427409, PubMed:28334377). Required for
CC normal transmission of a light-evoked stimulus from the cone
CC photoreceptor cells to the ON-bipolar cells and ON-ganglion cells in
CC the inner retina (PubMed:26427409, PubMed:28334377). Required in
CC retinal ON-bipolar cells for normal localization of the cation channel
CC TRPM1 at dendrite tips (PubMed:25997951). Seems to play a specific role
CC in synaptic contacts made by ON-bipolar cells with cone photoreceptor
CC pedicles (PubMed:28334377). May also have a role in cone synapse
CC formation (PubMed:25997951, PubMed:28334377). Might facilitate FGFR1
CC exit from the endoplasmic reticulum to the Golgi (By similarity). Could
CC be a regulator of the FGFRs (By similarity).
CC {ECO:0000250|UniProtKB:Q3SXY7, ECO:0000269|PubMed:25997951,
CC ECO:0000269|PubMed:26427409, ECO:0000269|PubMed:28334377}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000269|PubMed:25997951}. Perikaryon
CC {ECO:0000269|PubMed:25997951}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q3SXY7}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Punctate expression at dendrite tips.
CC {ECO:0000269|PubMed:25997951}.
CC -!- TISSUE SPECIFICITY: Detected in the outer plexiform layer (OPL) of the
CC retina, where it localizes to rod and cone ON-bipolar cells (at protein
CC level). Also detected in bipolar cell bodies in the inner retinal layer
CC (INL) (at protein level). {ECO:0000269|PubMed:25997951}.
CC -!- DISRUPTION PHENOTYPE: Viable. Retinal anatomy is grossly normal,
CC although thickness of the INL is reduced. In addition thickness of the
CC innermost region consisting of the inner plexiform layer, ganglion cell
CC layer and optic nerve fiber layer (IPL, GCL, NFL), is reduced.
CC Optomotor responses in dim conditions are impaired. Electroretinography
CC shows completely absent b-wave response under dim conditions, and
CC milder abnormalities under bright conditions (PubMed:24598786).
CC Abolishes ON-responses and delays OFF-responses in retinal ganglion
CC cells (PubMed:28334377). Rod photoreceptors show normal morphology
CC (PubMed:28334377). Cone photoreceptor synapses show morphological
CC abnormalities including a decrease in the number of triad processes in
CC cone pedicles in favor of diad processes, the number of flat contacts
CC at the base of pedicle synapses are increased, deep invaginating
CC contacts made by cone ON-bipolar cells are lost, and vacuole-like
CC structures are present at cone synaptic terminals (PubMed:28334377).
CC {ECO:0000269|PubMed:24598786, ECO:0000269|PubMed:28334377}.
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DR EMBL; KF954709; AHI87499.1; -; mRNA.
DR EMBL; AC111097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS57256.2; -.
DR RefSeq; NP_001274153.1; NM_001287224.1.
DR AlphaFoldDB; W8DXL4; -.
DR SMR; W8DXL4; -.
DR STRING; 10090.ENSMUSP00000140184; -.
DR GlyGen; W8DXL4; 4 sites.
DR PhosphoSitePlus; W8DXL4; -.
DR PRIDE; W8DXL4; -.
DR ProteomicsDB; 287273; -.
DR Antibodypedia; 2679; 78 antibodies from 18 providers.
DR Ensembl; ENSMUST00000185462; ENSMUSP00000140184; ENSMUSG00000093865.
DR GeneID; 242235; -.
DR KEGG; mmu:242235; -.
DR UCSC; uc033hzp.1; mouse.
DR CTD; 345193; -.
DR MGI; MGI:2685267; Lrit3.
DR VEuPathDB; HostDB:ENSMUSG00000093865; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000156627; -.
DR OMA; AELDNCV; -.
DR OrthoDB; 317712at2759; -.
DR PhylomeDB; W8DXL4; -.
DR BioGRID-ORCS; 242235; 2 hits in 71 CRISPR screens.
DR PRO; PR:W8DXL4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; W8DXL4; protein.
DR Bgee; ENSMUSG00000093865; Expressed in retinal neural layer and 15 other tissues.
DR ExpressionAtlas; W8DXL4; baseline and differential.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Cell projection; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Reference proteome;
KW Repeat; Sensory transduction; Signal; Transmembrane; Transmembrane helix;
KW Vision.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..681
FT /note="Leucine-rich repeat, immunoglobulin-like domain and
FT transmembrane domain-containing protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5007218087"
FT TOPO_DOM 20..584
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 56..79
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 80..103
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 104..128
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 129..151
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 152..175
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 254..344
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 350..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 275..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 134
FT /note="L->P: Defects in depolarization of photoreceptors in
FT the inner retina, and defects in cone photoreceptor light
FT response. Gross morphology is normal."
FT /evidence="ECO:0000269|PubMed:26427409"
SQ SEQUENCE 681 AA; 74827 MW; 02B8795BA4F3A176 CRC64;
MWLSACLCLV LSFLGGVNGT CPSQCSCEYH GRHDGSGSRL VLCNDLDMNE VPANFPVDTS
KLRIEKTVVR RLPAEAFYYL VELQYLWLAY NSVASIETSS FYNLRQLHEL RLDGNSLTAF
PWVSLLDMPH LRTLDLHNNR IASVPNEAVR YLRNLTCLDL SSNRLTTLPP DFLDSWSHLA
VTPSRSPDFP PRRIILGLQD NPWFCDCHIS KVIELSKVTD HAVVLLDPLM VCSEPERFQG
ILFQRVELEK CLKPSVMMSA TKITSALGSN VLLRCDAKGH PTPQLTWTRS DGSTVNYTVI
QESPGEGIRW SIISLTSISH KDAGDYRCKA KNLAGISEAV VTVTVVGGVT TTLSPDSSER
SPGEPPEQHP QPGLGGSTPP SKSWLSPGLT SAPSYPTPSA ALYTSTWSPP PSSLPPIFSA
ASATTSVQTS ISGRTARTSH QPPLLHPGGK SNAKIEKNGR KFPPLSASKK EELALLDQAA
PMETNVTIKD LRVARETGVS VTLMWNSSSS TQESSVTVLY SKYGEKDLLL VNADDYGKNQ
ATINGLEPGS QYVACVCPKG VGPREDLCIT FSTNRVEGRG SQWSLLLVVT STACVIVVPL
ICFLLYKVCK LQCTSDPFWE EDLSKETYIQ FETLSPRSQS IGELWTRRHR DDGERLLLCS
QSSVDSQMNL KSDGCRTEYY G
