LRFN2_MOUSE
ID LRFN2_MOUSE Reviewed; 788 AA.
AC Q80TG9; B9EIF8; Q9CYK3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 2;
DE Flags: Precursor;
GN Name=Lrfn2; Synonyms=Kiaa1246, Salm1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, INTERACTION WITH DLG4, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP GLYCOSYLATION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
RP 787-THR-VAL-788.
RX PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA Morimura N., Inoue T., Katayama K., Aruga J.;
RT "Comparative analysis of structure, expression and PSD95-binding capacity
RT of Lrfn, a novel family of neuronal transmembrane proteins.";
RL Gene 380:72-83(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Enhances
CC the cell surface expression of 2 NMDA receptor subunits GRIN1 and
CC GRIN2A (By similarity). May play a role in redistributing DLG4 to the
CC cell periphery. {ECO:0000250, ECO:0000269|PubMed:16828986}.
CC -!- SUBUNIT: Forms heteromeric complexes with LRFN1, LRFN3, LRFN4 and
CC LRFN5. Can form homomeric complexes, but not across cell junctions (By
CC similarity). Interacts with DLG4. Directly interacts with DLG1, DLG2
CC and DLG3 (By similarity). Directly interacts with 2 NMDA receptor
CC subunits GRIN1 and GRIN2A (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q80TG9; Q811D0: Dlg1; NbExp=3; IntAct=EBI-877092, EBI-514290;
CC Q80TG9; Q62108: Dlg4; NbExp=3; IntAct=EBI-877092, EBI-300895;
CC Q80TG9; P35439: Grin1; Xeno; NbExp=2; IntAct=EBI-877092, EBI-877897;
CC Q80TG9; P35439-1: Grin1; Xeno; NbExp=2; IntAct=EBI-877092, EBI-877923;
CC Q80TG9; P35439-4: Grin1; Xeno; NbExp=2; IntAct=EBI-877092, EBI-877935;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16828986}. Synapse
CC {ECO:0000269|PubMed:16828986}. Postsynaptic cell membrane
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with a weak,
CC but broad expression in the cerebral cortex and diencephalic nuclei.
CC Strongly expressed in both the pyramidal layer and the dentate gyrus of
CC the hippocampus. Also detected in other parts of the central nervous
CC system, including the olfactory bulb, pons, cerebellum, and medulla
CC oblongata, as well as in the peripheral nervous system, such as the
CC ganglia of cranial nerves and the dorsal root ganglion during
CC gestation. {ECO:0000269|PubMed:16828986}.
CC -!- DEVELOPMENTAL STAGE: Expression starts around 11.5-12.5 dpc. At 11.5
CC dpc, detected in the outer layer of the telencephalic vesicles. This
CC pattern of expression continues until 17.5 dpc with expression in the
CC cortical plate, but not in the inner layer of the cerebral cortex,
CC including subplate, ventricular zone, and subventricular zone. As also
CC detected in the hippocampus, amygdala and widely in diencephalic
CC nuclei. {ECO:0000269|PubMed:16828986}.
CC -!- DOMAIN: The PDZ-binding motif is required for cell surface expression,
CC neurite outgrowth promotion and interaction with DLG1, DLG3 and DLG4.
CC {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16828986}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65758.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK017594; BAB30828.1; -; mRNA.
DR EMBL; AK044375; BAC31891.1; -; mRNA.
DR EMBL; AK122476; BAC65758.1; ALT_INIT; mRNA.
DR EMBL; CH466559; EDL23629.1; -; Genomic_DNA.
DR EMBL; BC139418; AAI39419.1; -; mRNA.
DR CCDS; CCDS28871.1; -.
DR RefSeq; NP_081728.2; NM_027452.3.
DR AlphaFoldDB; Q80TG9; -.
DR SMR; Q80TG9; -.
DR BioGRID; 214114; 1.
DR IntAct; Q80TG9; 6.
DR MINT; Q80TG9; -.
DR STRING; 10090.ENSMUSP00000047573; -.
DR GlyGen; Q80TG9; 4 sites.
DR iPTMnet; Q80TG9; -.
DR PhosphoSitePlus; Q80TG9; -.
DR MaxQB; Q80TG9; -.
DR PaxDb; Q80TG9; -.
DR PRIDE; Q80TG9; -.
DR ProteomicsDB; 252522; -.
DR Antibodypedia; 2525; 110 antibodies from 23 providers.
DR DNASU; 70530; -.
DR Ensembl; ENSMUST00000046254; ENSMUSP00000047573; ENSMUSG00000040490.
DR GeneID; 70530; -.
DR KEGG; mmu:70530; -.
DR UCSC; uc008cyd.2; mouse.
DR CTD; 57497; -.
DR MGI; MGI:1917780; Lrfn2.
DR VEuPathDB; HostDB:ENSMUSG00000040490; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000156417; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; Q80TG9; -.
DR OMA; EFNCQSA; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; Q80TG9; -.
DR TreeFam; TF350185; -.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 70530; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Lrfn2; mouse.
DR PRO; PR:Q80TG9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80TG9; protein.
DR Bgee; ENSMUSG00000040490; Expressed in dentate gyrus of hippocampal formation granule cell and 51 other tissues.
DR Genevisible; Q80TG9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR013098; Ig_I-set.
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; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..788
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 2"
FT /id="PRO_0000014840"
FT TOPO_DOM 21..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..52
FT /note="LRRNT"
FT REPEAT 53..74
FT /note="LRR 1"
FT REPEAT 77..98
FT /note="LRR 2"
FT REPEAT 101..122
FT /note="LRR 3"
FT REPEAT 125..146
FT /note="LRR 4"
FT REPEAT 150..171
FT /note="LRR 5"
FT REPEAT 174..195
FT /note="LRR 6"
FT REPEAT 198..219
FT /note="LRR 7"
FT DOMAIN 242..288
FT /note="LRRCT"
FT DOMAIN 289..375
FT /note="Ig-like"
FT DOMAIN 422..518
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 383..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 785..788
FT /note="PDZ-binding"
FT COMPBIAS 383..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 787..788
FT /note="Missing: Loss of DLG4-binding."
FT /evidence="ECO:0000269|PubMed:16828986"
FT CONFLICT 42
FT /note="G -> R (in Ref. 1; BAB30828)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="L -> K (in Ref. 1; BAB30828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 788 AA; 84963 MW; 65B70CA475E99D6B CRC64;
METLLGGLLA FGMAFAVVDA CPKYCVCQNL SESLGTLCPS KGLLFVPPDI DRRTVELRLG
GNFIIHIGRQ DFANMTGLVD LTLSRNTISH IQPFSFLDLE SLRSLHLDSN RLPSLGEDTL
RGLVNLQHLI VNNNQLGGIA DDAFEDFLLT LEDLDLSYNN LHGLPWDSVR RMVNLHQLSL
DHNLLDHIAE GTFADLQKLA RLDLTSNRLQ KLPPDPIFAR SQASLLTATP FAPPLSFSFG
GNPLHCNCEL LWLRRLERDD DLETCGSPGS LKGRYFWHIR EEEFVCEPPL ITQHTHKLLV
LEGQAATLKC KAIGDPSPLI HWVAPDDRLV GNSSRTAVYD NGTLDILITT SQDSGPFTCI
AANAAGEATA TVEVSIVQLP HLSNSTSRMA PPKSRLSDIT GSSKTSRGGG GSGAGEPPKS
TPERAVLVSD VTTTSALVKW SVSKSAPRVK MYQLQYNCSD DEVLIYRMIP ASNKAFVVNN
LVSGTGYDLC VLAMWDDTAT TLTATNIVGC AQFFTKADYP QCQSMHSQIL GGTMILVIGG
IIVATLLVFI VILMVRYKVC NHDTPGKMAA ATVSNVYSQT NGSQPPPLGG IPVGQLPQAP
PKVVVRNELM DFSTSLARAC DSSSSSSLGS GEAAGLGRGP WRLPPPAPRP KPSLDRLMGA
FASLDLKSQR KEELLDSRTP AGRGAGTSSR GHHSDREPLL GPPATRARSL LPLPLEGKAK
RSHSFDMGDF AAAAAAVPGG YSPPRRVSNI WTKRSLSVNG MLLPFEESDL VGARGTFGSS
EWVMESTV
