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Protein

Leucine-rich repeat and fibronectin type-III domain-containing protein 3

Gene

Lrfn3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Promotes neurite outgrowth in hippocampal neurons.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-8849932. SALM protein interactions at the synapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat and fibronectin type-III domain-containing protein 3
Alternative name(s):
Synaptic adhesion-like molecule 4
Gene namesi
Name:Lrfn3
Synonyms:Salm4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2442512. Lrfn3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 539523ExtracellularSequence analysisAdd
BLAST
Transmembranei540 – 56021HelicalSequence analysisAdd
BLAST
Topological domaini561 – 62666CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 626610Leucine-rich repeat and fibronectin type-III domain-containing protein 3PRO_0000014842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence analysis
Disulfide bondi317 ↔ 366PROSITE-ProRule annotation
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence analysis
Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence analysis
Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8BLY3.
PaxDbiQ8BLY3.
PRIDEiQ8BLY3.

PTM databases

iPTMnetiQ8BLY3.
PhosphoSiteiQ8BLY3.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ8BLY3.
GenevisibleiQ8BLY3. MM.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000037616.

Structurei

3D structure databases

ProteinModelPortaliQ8BLY3.
SMRiQ8BLY3. Positions 27-387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5941LRRNTAdd
BLAST
Repeati84 – 10522LRR 1Add
BLAST
Repeati108 – 12922LRR 2Add
BLAST
Repeati132 – 15322LRR 3Add
BLAST
Repeati157 – 17822LRR 4Add
BLAST
Repeati181 – 20222LRR 5Add
BLAST
Repeati205 – 22622LRR 6Add
BLAST
Domaini249 – 29547LRRCTAdd
BLAST
Domaini295 – 38288Ig-likeAdd
BLAST
Domaini425 – 52399Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the LRFN family.Curated
Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 6 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000237343.
HOVERGENiHBG052352.
InParanoidiQ8BLY3.
KOiK16356.
OMAiWAVGEEE.
OrthoDBiEOG75B84P.
PhylomeDBiQ8BLY3.
TreeFamiTF350185.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
PF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 6 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BLY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLPLLLCL LPLAPASSPP QPAISSPCPR RCRCQTQSMP LSVLCPGAGL
60 70 80 90 100
LFVPPSLDRR AAELRLADNF IAAVRRRDLA NMTGLLHLSL SRNTIRHVAA
110 120 130 140 150
GAFADLRALR ALHLDGNRLT SLGEGQLRGL VNLRHLILSN NQLAALAAGA
160 170 180 190 200
LDDCAETLED LDLSYNNLEQ LPWEALGRLG NVNTLGLDHN LLASVPAGAF
210 220 230 240 250
SRLHKLARLD MTSNRLTTIP PDPLFSRLPL LARPRGSPAS ALVLAFGGNP
260 270 280 290 300
LHCNCELVWL RRLAREDDLE ACASPPALGG RYFWAVGEEE FVCEPPVVTH
310 320 330 340 350
RSPPLAVPAG RPAALRCRAV GDPEPRVRWV SPQGRLLGNS SRARAFPNGT
360 370 380 390 400
LELLVTEPED GGTFTCIAAN AAGEATAAVE LTVGPPPPPQ LANSTSCDPP
410 420 430 440 450
RDGEPDALTP PSAASASAKV ADTVAPTDRG VQVTEHGATA ALVQWPDQRP
460 470 480 490 500
VPGIRMYQIQ YNSSADDILV YRMIPADSRS FLLTDLASGR TYDLCVLAVY
510 520 530 540 550
EDSATGLTAT RPVGCARFST EPALRPCAAP HAPFLGGTMI IALGGVIVAS
560 570 580 590 600
VLVFIFVLLL RYKVHGGQPP GKAKATAPVS SVCSQTNGAL GPVPSAPAPE
610 620
PAAPRAHTVV QLDCEPWGPS HEPAGP
Length:626
Mass (Da):66,056
Last modified:March 1, 2003 - v1
Checksum:i95321B8D058E0079
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21088.1.
RefSeqiNP_780687.1. NM_175478.2.
UniGeneiMm.23157.

Genome annotation databases

EnsembliENSMUST00000046351; ENSMUSP00000037616; ENSMUSG00000036957.
GeneIDi233067.
KEGGimmu:233067.
UCSCiuc009gee.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21088.1.
RefSeqiNP_780687.1. NM_175478.2.
UniGeneiMm.23157.

3D structure databases

ProteinModelPortaliQ8BLY3.
SMRiQ8BLY3. Positions 27-387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000037616.

PTM databases

iPTMnetiQ8BLY3.
PhosphoSiteiQ8BLY3.

Proteomic databases

MaxQBiQ8BLY3.
PaxDbiQ8BLY3.
PRIDEiQ8BLY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046351; ENSMUSP00000037616; ENSMUSG00000036957.
GeneIDi233067.
KEGGimmu:233067.
UCSCiuc009gee.1. mouse.

Organism-specific databases

CTDi79414.
MGIiMGI:2442512. Lrfn3.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000237343.
HOVERGENiHBG052352.
InParanoidiQ8BLY3.
KOiK16356.
OMAiWAVGEEE.
OrthoDBiEOG75B84P.
PhylomeDBiQ8BLY3.
TreeFamiTF350185.

Enzyme and pathway databases

ReactomeiR-MMU-8849932. SALM protein interactions at the synapse.

Miscellaneous databases

PROiQ8BLY3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BLY3.
GenevisibleiQ8BLY3. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
PF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 6 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/cJ.
  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.
    , 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/6J.
    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.

Entry informationi

Entry nameiLRFN3_MOUSE
AccessioniPrimary (citable) accession number: Q8BLY3
Secondary accession number(s): Q505E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.