LRFN2_RAT
ID LRFN2_RAT Reviewed; 788 AA.
AC Q460M5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 2;
DE Flags: Precursor;
GN Name=Lrfn2; Synonyms=Salm1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH DLG1; DLG3; DLG4; GRIN1 AND GRIN2A, AND MUTAGENESIS OF
RP 785-GLU--VAL-788.
RC STRAIN=Sprague-Dawley;
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 INTERACTION WITH LRFN1 AND LRFN4, AND MUTAGENESIS OF 785-GLU--VAL-788.
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 [3]
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: Promotes neurite outgrowth in hippocampal neurons. Enhances
CC the cell surface expression of GRIN1 and GRIN2A NMDA receptor subunits.
CC May play a role in redistributing DLG4 to the cell periphery (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16495444,
CC ECO:0000269|PubMed:18585462}.
CC -!- SUBUNIT: Forms heteromeric complexes with LRFN1, LRFN3 and LRFN4. Can
CC form homomeric complexes, but not across cell junctions. Can form
CC heteromeric complexes with LRFN5 (By similarity). Interacts with DLG1,
CC DLG3 and DLG4; interaction with DLG4 is mediated by the PDZ-binding
CC domain. Interacts also with DLG2 (By similarity). Interacts with 2 NMDA
CC receptor subunits GRIN1 and GRIN2A. {ECO:0000250,
CC ECO:0000269|PubMed:16495444, ECO:0000269|PubMed:18227064}.
CC -!- INTERACTION:
CC Q460M5; Q62696: Dlg1; NbExp=2; IntAct=EBI-877185, EBI-389325;
CC Q460M5; Q62936: Dlg3; NbExp=2; IntAct=EBI-877185, EBI-349596;
CC Q460M5; P31016: Dlg4; NbExp=3; IntAct=EBI-877185, EBI-375655;
CC Q460M5; P35439: Grin1; NbExp=2; IntAct=EBI-877185, EBI-877897;
CC Q460M5; Q8CGM3: GRIN2A; NbExp=2; IntAct=EBI-877185, EBI-877440;
CC Q460M5; Q00960: Grin2b; NbExp=2; IntAct=EBI-877185, EBI-396905;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16495444}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16495444}. Synapse
CC {ECO:0000269|PubMed:16495444}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:16495444}.
CC -!- DOMAIN: The PDZ-binding motif is required for cell surface expression,
CC neurite outgrowth promotion and interaction with DLG4.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; DQ070869; AAZ20638.1; -; mRNA.
DR AlphaFoldDB; Q460M5; -.
DR SMR; Q460M5; -.
DR IntAct; Q460M5; 6.
DR STRING; 10116.ENSRNOP00000015705; -.
DR GlyGen; Q460M5; 6 sites.
DR PhosphoSitePlus; Q460M5; -.
DR PaxDb; Q460M5; -.
DR PRIDE; Q460M5; -.
DR UCSC; RGD:1311831; rat.
DR RGD; 1311831; Lrfn2.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q460M5; -.
DR PhylomeDB; Q460M5; -.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:Q460M5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
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_0000394519"
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..707
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 74
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 CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 785..788
FT /note="Missing: Severe decrease in cell surface expression.
FT Loss of neurite outgrowth promotion. Loss of DLG4-binding.
FT No effect on LRFN1-,LRFN3-, and LRFN4-binding, nor on
FT homomeric interactions."
FT /evidence="ECO:0000269|PubMed:16495444,
FT ECO:0000269|PubMed:18227064"
SQ SEQUENCE 788 AA; 84917 MW; 1C0837EAFF3F36EC 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 DLKTCGSPGG 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 NHDAPGKMAA ATVSNVYSQT NGAQPPPLGG MPVGQLPQAP
PKVVVRNELM DFSTSLARAC DSSSSSSLGS GEAAGLSRGP WRLPPPAPRP KPSLDRLMGA
FASLDLKSQR KEELLDSRTP AGRGAGTSAR GHHSDREPLL GPPATRARSL LPLPLEGKAK
RSHSFDMGDF AAAAAAAPGG YSPPRRVSNI WTKRSLSVNG MLLPFEENDL VGARGTFGSS
EWVMESTV
