LRRT4_RAT
ID LRRT4_RAT Reviewed; 590 AA.
AC B4F7C5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Leucine-rich repeat transmembrane neuronal protein 4;
DE Flags: Precursor;
GN Name=Lrrtm4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [2]
RP FUNCTION.
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).
RN [3]
RP IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
CC -!- FUNCTION: May play a role in the development and maintenance of the
CC nervous system (By similarity). Exhibits strong synaptogenic activity,
CC restricted to excitatory presynaptic differentiation. {ECO:0000250,
CC ECO:0000269|PubMed:19285470}.
CC -!- SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents, including LRRTM4. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing. {ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Postsynaptic cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:22632720}.
CC -!- SIMILARITY: Belongs to the LRRTM family. {ECO:0000305}.
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DR EMBL; BC168219; AAI68219.1; -; mRNA.
DR RefSeq; NP_001128218.1; NM_001134746.1.
DR RefSeq; XP_008761247.2; XM_008763025.2.
DR RefSeq; XP_008761248.2; XM_008763026.2.
DR AlphaFoldDB; B4F7C5; -.
DR SMR; B4F7C5; -.
DR BioGRID; 271527; 2.
DR CORUM; B4F7C5; -.
DR STRING; 10116.ENSRNOP00000034217; -.
DR GlyGen; B4F7C5; 3 sites.
DR iPTMnet; B4F7C5; -.
DR PhosphoSitePlus; B4F7C5; -.
DR PaxDb; B4F7C5; -.
DR PRIDE; B4F7C5; -.
DR ABCD; B4F7C5; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000092261; ENSRNOP00000075874; ENSRNOG00000021938.
DR GeneID; 500219; -.
DR KEGG; rno:500219; -.
DR CTD; 80059; -.
DR RGD; 1560707; Lrrtm4.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154909; -.
DR InParanoid; B4F7C5; -.
DR OMA; PMRVFLD; -.
DR OrthoDB; 427408at2759; -.
DR PhylomeDB; B4F7C5; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:B4F7C5; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000021938; Expressed in frontal cortex and 5 other tissues.
DR ExpressionAtlas; B4F7C5; baseline.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISO:RGD.
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; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:RGD.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; ISO:RGD.
DR GO; GO:0072578; P:neurotransmitter-gated ion channel clustering; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:1901629; P:regulation of presynaptic membrane organization; ISO:RGD.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; IDA: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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 9.
DR PROSITE; PS51450; LRR; 9.
PE 1: Evidence at protein 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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..590
FT /note="Leucine-rich repeat transmembrane neuronal protein
FT 4"
FT /id="PRO_0000420526"
FT TOPO_DOM 31..424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..59
FT /note="LRRNT"
FT REPEAT 60..83
FT /note="LRR 1"
FT REPEAT 84..107
FT /note="LRR 2"
FT REPEAT 108..131
FT /note="LRR 3"
FT REPEAT 132..155
FT /note="LRR 4"
FT REPEAT 157..179
FT /note="LRR 5"
FT REPEAT 180..203
FT /note="LRR 6"
FT REPEAT 205..227
FT /note="LRR 7"
FT REPEAT 228..251
FT /note="LRR 8"
FT REPEAT 252..275
FT /note="LRR 9"
FT REPEAT 276..299
FT /note="LRR 10"
FT DOMAIN 311..362
FT /note="LRRCT"
FT CARBOHYD 58
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 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 590 AA; 67170 MW; 24EE346E08598482 CRC64;
MGFRLITQLK GMSVLLVLFP TLLLVMLTGA QRACPKNCRC DGKIVYCESH AFADIPENIS
GGSQGLSLRF NSIQKLKSNQ FAGLNQLIWL YLDHNYISSV DEDAFQGIRR LKELILSSNK
ITYLHNKTFH PVPNLRNLDL SYNKLQTLQS EQFKGLRKLI ILHLRSNSLK TVPIRVFQDC
RNLDFLDLGY NRLRSLSRNA FAGLLKLKEL HLEHNQFSKI NFAHFPRLFN LRSIYLQWNR
IRSVSQGLTW TWSSLHTLDL SGNDIQAIEP GTFKCLPNLQ KLNLDSNKLT NVSQETVNAW
ISLISITLSG NMWECSRSIC PLFYWLKNFK GNKESTMICA GPKHIQGEKV SDAVETYNIC
SDVQVVNTER SHLAPQTPQK PPFFPKPTIF KSDAIPATLE AVSPSPGFQI PGTDHEYEHV
SFHKIIAGSV ALFLSVAMIL LVIYVSWKRY PASMKQLQQH SLMKRRRKKA RESERQMNSP
LQEYYVDYKP TNSETMDISV NGSGPCTYTI SGSRECEMPH HVKPLPYYSY DQPVIGYCQA
HQPLHINKAY EAVSIEQDDS PSLELGRDHS FIATIARSAA PAIYLERITN
