LRFN3_RAT
ID LRFN3_RAT Reviewed; 626 AA.
AC B0BNK7;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 3;
DE AltName: Full=Synaptic adhesion-like molecule 4 {ECO:0000303|PubMed:18227064};
DE Flags: Precursor;
GN Name=Lrfn3 {ECO:0000312|EMBL:AAI58863.1, ECO:0000312|RGD:1305567};
GN Synonyms=Salm4 {ECO:0000303|PubMed:18227064};
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] {ECO:0000312|EMBL:EDM07768.1}
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 [2] {ECO:0000312|EMBL:AAI58863.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAI58863.1};
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 [3] {ECO:0000305}
RP INTERACTION WITH LRFN1; LRFN2; LRFN3; LRFN4 AND LRFN5, AND SUBCELLULAR
RP LOCATION.
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).
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18227064};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:18227064}. Cell
CC projection, axon {ECO:0000269|PubMed:18227064}. Cell projection,
CC dendrite {ECO:0000269|PubMed:18227064}. Synapse
CC {ECO:0000269|PubMed:18227064}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:18227064}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:18227064}. Note=Detected also in intracellular
CC vesicular and tubovesicular structures and in membranes of cell soma.
CC On overexpression, detected throughout hippocampal neurons in soma,
CC axons, dendrites and growth cones. {ECO:0000255,
CC ECO:0000269|PubMed:18227064}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Within brain, expressed in
CC hippocampus, cerebellum, olfactory bulb and forebrain (at protein
CC level). {ECO:0000269|PubMed:18227064}.
CC -!- DOMAIN: Lacks a cytoplasmic PDZ-binding domain, which has been
CC implicated in function of related LRFN proteins.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BLY3}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000255}.
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DR EMBL; CH473979; EDM07768.1; -; Genomic_DNA.
DR EMBL; BC158862; AAI58863.1; -; mRNA.
DR RefSeq; NP_001100972.1; NM_001107502.1.
DR RefSeq; XP_006228833.1; XM_006228771.2.
DR AlphaFoldDB; B0BNK7; -.
DR SMR; B0BNK7; -.
DR STRING; 10116.ENSRNOP00000028275; -.
DR GlyGen; B0BNK7; 3 sites.
DR PaxDb; B0BNK7; -.
DR PRIDE; B0BNK7; -.
DR Ensembl; ENSRNOT00000028275; ENSRNOP00000028275; ENSRNOG00000020839.
DR GeneID; 308495; -.
DR KEGG; rno:308495; -.
DR UCSC; RGD:1305567; rat.
DR CTD; 79414; -.
DR RGD; 1305567; Lrfn3.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161203; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; B0BNK7; -.
DR OMA; EPALQPC; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; B0BNK7; -.
DR TreeFam; TF350185; -.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:B0BNK7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000020839; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; B0BNK7; RN.
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; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0099560; P:synaptic membrane adhesion; 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.
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 /evidence="ECO:0000255"
FT /id="PRO_0000391358"
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 /evidence="ECO:0000255"
FT DOMAIN 308..395
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 425..523
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 382..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 DISULFID 317..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 626 AA; 66068 MW; 250D1BBDCC4C8338 CRC64;
MAVLPLLLCL LPLAPASSPP QPATSSPCPR RCRCQTQSLP 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 RYKVHGVQPP GKAKATAPVS SVCSQTNGAL GPVPSAPAPE
PAAPRAHTVV QLDCEPWGPS HEPAGP
