LRFN3_MOUSE
ID LRFN3_MOUSE Reviewed; 626 AA.
AC Q8BLY3; Q505E2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 3;
DE AltName: Full=Synaptic adhesion-like molecule 4;
DE Flags: Precursor;
GN Name=Lrfn3; Synonyms=Salm4;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=16495444; DOI=10.1523/jneurosci.3799-05.2006;
RA Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.;
RT "A novel family of adhesion-like molecules that interacts with the NMDA
RT receptor.";
RL J. Neurosci. 26:2174-2183(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [5]
RP SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND GLYCOSYLATION.
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 FUNCTION, AND INTERACTION WITH LRFN1; LRFN2; LRFN3; LRFN4 AND LRFN5.
RX PubMed=18227064; DOI=10.1074/jbc.m709456200;
RA Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X., Petralia R.S.,
RA Wenthold R.J.;
RT "The SALM family of adhesion-like molecules forms heteromeric and homomeric
RT complexes.";
RL J. Biol. Chem. 283:8395-8405(2008).
RN [7]
RP FUNCTION.
RX PubMed=18585462; DOI=10.1016/j.mcn.2008.05.019;
RA Wang P.Y., Seabold G.K., Wenthold R.J.;
RT "Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.";
RL Mol. Cell. Neurosci. 39:83-94(2008).
CC -!- FUNCTION: Cell adhesion molecule that mediates homophilic cell-cell
CC adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in
CC hippocampal neurons. {ECO:0000269|PubMed:18227064,
CC ECO:0000269|PubMed:18585462}.
CC -!- SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN4 and
CC LRFN5. Able to form homomeric complexes across cell junctions, between
CC adjacent cells. Does not interact with DLG4.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16828986};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16828986}. Cell
CC projection, axon {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane
CC {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis, stomach, small
CC intestine and kidney. Residually expressed in heart, lung, liver,
CC skeletal muscle and uterus. In the brain, weak, but broad expression in
CC the cerebral cortex and diencephalic nuclei. Also detected in other
CC parts of the central nervous system, including the olfactory bulb,
CC pons, cerebellum, and medulla oblongata, as well as in the peripheral
CC nervous system, such as the ganglia of cranial nerves and the dorsal
CC root ganglion during gestation. {ECO:0000269|PubMed:16828986}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 4.5 to 18.5 dpc. Initial levels are
CC low until 6.5 dpc and residual from 7.5 to 9.5 dpc. Expression
CC increases from 10.5 to 15.5 dpc before falling again to a level
CC slightly higher than the one seen on 4.5 to 6.5 dpc. At 11.5 dpc,
CC broadly expressed in the telencephalic and diencephalic vesicles. At
CC 17.5 dpc, expressed in cerebral cortex, hippocampus, dorsal thalamus
CC and amygdala. {ECO:0000269|PubMed:16828986}.
CC -!- DOMAIN: Lacks a cytoplasmic PDZ-binding domain, which has been
CC implicated in function of related Lrfn proteins.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16828986}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; DQ078787; AAZ23616.1; -; mRNA.
DR EMBL; AK040916; BAC30743.1; -; mRNA.
DR EMBL; CH466593; EDL24028.1; -; Genomic_DNA.
DR EMBL; BC066999; AAH66999.1; -; mRNA.
DR EMBL; BC094593; AAH94593.1; -; mRNA.
DR CCDS; CCDS21088.1; -.
DR RefSeq; NP_780687.1; NM_175478.2.
DR AlphaFoldDB; Q8BLY3; -.
DR SMR; Q8BLY3; -.
DR STRING; 10090.ENSMUSP00000037616; -.
DR GlyGen; Q8BLY3; 5 sites.
DR iPTMnet; Q8BLY3; -.
DR PhosphoSitePlus; Q8BLY3; -.
DR MaxQB; Q8BLY3; -.
DR PaxDb; Q8BLY3; -.
DR PRIDE; Q8BLY3; -.
DR ProteomicsDB; 290165; -.
DR Antibodypedia; 29620; 83 antibodies from 25 providers.
DR DNASU; 233067; -.
DR Ensembl; ENSMUST00000046351; ENSMUSP00000037616; ENSMUSG00000036957.
DR GeneID; 233067; -.
DR KEGG; mmu:233067; -.
DR UCSC; uc009gee.1; mouse.
DR CTD; 79414; -.
DR MGI; MGI:2442512; Lrfn3.
DR VEuPathDB; HostDB:ENSMUSG00000036957; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161203; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; Q8BLY3; -.
DR OMA; EPALQPC; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; Q8BLY3; -.
DR TreeFam; TF350185; -.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 233067; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q8BLY3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BLY3; protein.
DR Bgee; ENSMUSG00000036957; Expressed in islet of Langerhans and 65 other tissues.
DR Genevisible; Q8BLY3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; ISO:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
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.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..626
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 3"
FT /id="PRO_0000014842"
FT TOPO_DOM 17..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..59
FT /note="LRRNT"
FT REPEAT 84..105
FT /note="LRR 1"
FT REPEAT 108..129
FT /note="LRR 2"
FT REPEAT 132..153
FT /note="LRR 3"
FT REPEAT 157..178
FT /note="LRR 4"
FT REPEAT 181..202
FT /note="LRR 5"
FT REPEAT 205..226
FT /note="LRR 6"
FT DOMAIN 249..295
FT /note="LRRCT"
FT DOMAIN 295..382
FT /note="Ig-like"
FT DOMAIN 425..523
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 382..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 317..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 626 AA; 66056 MW; 95321B8D058E0079 CRC64;
MAVLPLLLCL LPLAPASSPP QPAISSPCPR RCRCQTQSMP LSVLCPGAGL LFVPPSLDRR
AAELRLADNF IAAVRRRDLA NMTGLLHLSL SRNTIRHVAA GAFADLRALR ALHLDGNRLT
SLGEGQLRGL VNLRHLILSN NQLAALAAGA LDDCAETLED LDLSYNNLEQ LPWEALGRLG
NVNTLGLDHN LLASVPAGAF SRLHKLARLD MTSNRLTTIP PDPLFSRLPL LARPRGSPAS
ALVLAFGGNP LHCNCELVWL RRLAREDDLE ACASPPALGG RYFWAVGEEE FVCEPPVVTH
RSPPLAVPAG RPAALRCRAV GDPEPRVRWV SPQGRLLGNS SRARAFPNGT LELLVTEPED
GGTFTCIAAN AAGEATAAVE LTVGPPPPPQ LANSTSCDPP RDGEPDALTP PSAASASAKV
ADTVAPTDRG VQVTEHGATA ALVQWPDQRP VPGIRMYQIQ YNSSADDILV YRMIPADSRS
FLLTDLASGR TYDLCVLAVY EDSATGLTAT RPVGCARFST EPALRPCAAP HAPFLGGTMI
IALGGVIVAS VLVFIFVLLL RYKVHGGQPP GKAKATAPVS SVCSQTNGAL GPVPSAPAPE
PAAPRAHTVV QLDCEPWGPS HEPAGP
