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Q8BLY3 (LRFN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich repeat and fibronectin type-III domain-containing protein 3
Alternative name(s):
Synaptic adhesion-like molecule 4
Gene names
Name:Lrfn3
Synonyms:Salm4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Promotes neurite outgrowth in hippocampal neurons. Ref.6 Ref.7

Subunit structure

Can form heteromeric complexes with LRFN1, LRFN2, LRFN4 and LRFN5. Able to form homomeric complexes across cell junctions, between adjacent cells. Does not interact with DLG4.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell projection › axon By similarity. Cell projection › dendrite By similarity. Cell junction › synapse By similarity. Cell junction › synapse › presynaptic cell membrane By similarity. Cell junction › synapse › postsynaptic cell membrane By similarity Ref.5.

Tissue specificity

Expressed in brain, testis, stomach, small intestine and kidney. Residually expressed in heart, lung, liver, skeletal muscle and uterus. In the brain, weak, but broad expression in the cerebral cortex and diencephalic nuclei. Also detected in other parts of the central nervous system, including the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as in the peripheral nervous system, such as the ganglia of cranial nerves and the dorsal root ganglion during gestation. Ref.5

Developmental stage

Expressed from 4.5 to 18.5 dpc. Initial levels are low until 6.5 dpc and residual from 7.5 to 9.5 dpc. Expression increases from 10.5 to 15.5 dpc before falling again to a level slightly higher than the one seen on 4.5 to 6.5 dpc. At 11.5 dpc, broadly expressed in the telencephalic and diencephalic vesicles. At 17.5 dpc, expressed in cerebral cortex, hippocampus, dorsal thalamus and amygdala. Ref.5

Domain

Lacks a cytoplasmic PDZ-binding domain, which has been implicated in function of related Lrfn proteins.

Post-translational modification

N-glycosylated. Ref.5

Sequence similarities

Belongs to the LRFN family.

Contains 1 fibronectin type-III domain.

Contains 1 Ig-like (immunoglobulin-like) domain.

Contains 6 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 626610Leucine-rich repeat and fibronectin type-III domain-containing protein 3
PRO_0000014842

Regions

Topological domain17 – 539523Extracellular Potential
Transmembrane540 – 56021Helical; Potential
Topological domain561 – 62666Cytoplasmic Potential
Domain19 – 5941LRRNT
Repeat84 – 10522LRR 1
Repeat108 – 12922LRR 2
Repeat132 – 15322LRR 3
Repeat157 – 17822LRR 4
Repeat181 – 20222LRR 5
Repeat205 – 22622LRR 6
Domain249 – 29547LRRCT
Domain295 – 38288Ig-like
Domain426 – 51590Fibronectin type-III

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential
Disulfide bond317 ↔ 366 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BLY3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 95321B8D058E0079

FASTA62666,056
        10         20         30         40         50         60 
MAVLPLLLCL LPLAPASSPP QPAISSPCPR RCRCQTQSMP LSVLCPGAGL LFVPPSLDRR 

        70         80         90        100        110        120 
AAELRLADNF IAAVRRRDLA NMTGLLHLSL SRNTIRHVAA GAFADLRALR ALHLDGNRLT 

       130        140        150        160        170        180 
SLGEGQLRGL VNLRHLILSN NQLAALAAGA LDDCAETLED LDLSYNNLEQ LPWEALGRLG 

       190        200        210        220        230        240 
NVNTLGLDHN LLASVPAGAF SRLHKLARLD MTSNRLTTIP PDPLFSRLPL LARPRGSPAS 

       250        260        270        280        290        300 
ALVLAFGGNP LHCNCELVWL RRLAREDDLE ACASPPALGG RYFWAVGEEE FVCEPPVVTH 

       310        320        330        340        350        360 
RSPPLAVPAG RPAALRCRAV GDPEPRVRWV SPQGRLLGNS SRARAFPNGT LELLVTEPED 

       370        380        390        400        410        420 
GGTFTCIAAN AAGEATAAVE LTVGPPPPPQ LANSTSCDPP RDGEPDALTP PSAASASAKV 

       430        440        450        460        470        480 
ADTVAPTDRG VQVTEHGATA ALVQWPDQRP VPGIRMYQIQ YNSSADDILV YRMIPADSRS 

       490        500        510        520        530        540 
FLLTDLASGR TYDLCVLAVY EDSATGLTAT RPVGCARFST EPALRPCAAP HAPFLGGTMI 

       550        560        570        580        590        600 
IALGGVIVAS VLVFIFVLLL RYKVHGGQPP GKAKATAPVS SVCSQTNGAL GPVPSAPAPE 

       610        620 
PAAPRAHTVV QLDCEPWGPS HEPAGP

« Hide

References

« Hide 'large scale' references
[1]"A novel family of adhesion-like molecules that interacts with the NMDA receptor."
Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.
J. Neurosci. 26:2174-2183(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Aorta and Vein.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]"Comparative analysis of structure, expression and PSD95-binding capacity of Lrfn, a novel family of neuronal transmembrane proteins."
Morimura N., Inoue T., Katayama K., Aruga J.
Gene 380:72-83(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
[6]"The SALM family of adhesion-like molecules forms heteromeric and homomeric complexes."
Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X., Petralia R.S., Wenthold R.J.
J. Biol. Chem. 283:8395-8405(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LRFN1; LRFN2; LRFN3; LRFN4 AND LRFN5.
[7]"Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth."
Wang P.Y., Seabold G.K., Wenthold R.J.
Mol. Cell. Neurosci. 39:83-94(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ078787 mRNA. Translation: AAZ23616.1.
AK040916 mRNA. Translation: BAC30743.1.
CH466593 Genomic DNA. Translation: EDL24028.1.
BC066999 mRNA. Translation: AAH66999.1.
BC094593 mRNA. Translation: AAH94593.1.
IPIIPI00222949.
RefSeqNP_780687.1. NM_175478.2.
UniGeneMm.23157.

3D structure databases

ProteinModelPortalQ8BLY3.
SMRQ8BLY3. Positions 27-387.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000037616.

PTM databases

PhosphoSiteQ8BLY3.

Proteomic databases

PaxDbQ8BLY3.
PRIDEQ8BLY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046351; ENSMUSP00000037616; ENSMUSG00000036957.
GeneID233067.
KEGGmmu:233067.
UCSCuc009gee.1. mouse.

Organism-specific databases

CTD79414.
MGIMGI:2442512. Lrfn3.

Phylogenomic databases

eggNOGNOG239228.
GeneTreeENSGT00660000095307.
HOGENOMHOG000237343.
HOVERGENHBG052352.
InParanoidQ505E2.
KOK16356.
OMAWAVGEEE.
OrthoDBEOG43TZV6.

Gene expression databases

ArrayExpressQ8BLY3.
BgeeQ8BLY3.
GenevestigatorQ8BLY3.
GermOnlineENSMUSG00000036957. Mus musculus.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 1 hit.
PROSITEPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio381527.
SOURCESearch...

Entry information

Entry nameLRFN3_MOUSE
AccessionPrimary (citable) accession number: Q8BLY3
Secondary accession number(s): Q505E2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents