LRFN4_RAT
ID LRFN4_RAT Reviewed; 636 AA.
AC D4ABX8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 4;
DE Flags: Precursor;
GN Name=Lrfn4; Synonyms=Salm3;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH LRFN1 AND LRFN2.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons. May play a
CC role in redistributing DLG4 to the cell periphery (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms heteromeric complexes with LRFN1 and LRFN2. Can form
CC heteromeric complexes with LRFN3 and LRFN5 (By similarity). Unable to
CC form homophilic interactions across cell junctions (By similarity).
CC Interacts with DLG1, DLG2, DLG3 and DLG4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The PDZ-binding motif is required for neurite outgrowth
CC promotion and interaction with DLG1, DLG3- and DLG4. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; CH473953; EDM12411.1; -; Genomic_DNA.
DR RefSeq; NP_001102978.1; NM_001109508.1.
DR RefSeq; XP_017445222.1; XM_017589733.1.
DR AlphaFoldDB; D4ABX8; -.
DR SMR; D4ABX8; -.
DR STRING; 10116.ENSRNOP00000026169; -.
DR GlyGen; D4ABX8; 2 sites.
DR iPTMnet; D4ABX8; -.
DR PhosphoSitePlus; D4ABX8; -.
DR PaxDb; D4ABX8; -.
DR PRIDE; D4ABX8; -.
DR Ensembl; ENSRNOT00000026169; ENSRNOP00000026169; ENSRNOG00000019356.
DR GeneID; 688721; -.
DR KEGG; rno:688721; -.
DR UCSC; RGD:1585286; rat.
DR CTD; 78999; -.
DR RGD; 1585286; Lrfn4.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000162195; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; D4ABX8; -.
DR OMA; EAYPDCH; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; D4ABX8; -.
DR TreeFam; TF350185; -.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:D4ABX8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000019356; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; D4ABX8; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
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:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; 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; SM00060; FN3; 1.
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 Disulfide bond; Glycoprotein; Immunoglobulin domain; Leucine-rich repeat;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..636
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 4"
FT /id="PRO_0000394522"
FT TOPO_DOM 17..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..48
FT /note="LRRNT"
FT REPEAT 49..70
FT /note="LRR 1"
FT REPEAT 73..94
FT /note="LRR 2"
FT REPEAT 97..118
FT /note="LRR 3"
FT REPEAT 121..142
FT /note="LRR 4"
FT REPEAT 146..169
FT /note="LRR 5"
FT REPEAT 170..191
FT /note="LRR 6"
FT REPEAT 194..215
FT /note="LRR 7"
FT DOMAIN 234..280
FT /note="LRRCT"
FT DOMAIN 281..367
FT /note="Ig-like"
FT DOMAIN 405..502
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 556..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 633..636
FT /note="PDZ-binding"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJG9"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 302..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 636 AA; 67259 MW; AAA1F65443176B9A CRC64;
MAPPLLLLLL ASGAAACPLP CVCQNLSESL STLCAHRGLL FVPPNVDRRT VELRLADNFI
QALGPPDFRN MTGLVDLTLS RNAITRIGAR SFGDLESLRS LHLDGNRLVE LGSSSLRGPV
NLQHLILSGN QLGRIAPGAF DDFLDSLEDL DVSYNNLRQV PWAGIGSMPA LHTLNLDHNL
IDALPPGVFA QLSQLSRLDL TSNRLATLAP DPLFSRGRDA EASPSPLVLS FSGNPLHCNC
ELLWLRRLAR PDDLETCASP PTLAGRYFWA VPEGEFSCEP PLIARHTQRL WVLEGQRATL
RCRALGDPVP TMHWVGPDDR LVGNSSRAWA FPNGTLEIGV TGAGDAGAYT CIATNPAGEA
TARVELRVLA LPHGGNTSAE GGRPGPSDIA ASARTAAEGE GTLESEPAVQ VTEVTATSGL
VSWGPGRPAD PVWMFQIQYN SSEDETLIYR IVPASSQHFL LKHLVPGADY DLCLLALSPA
AGPSDLTATR LLGCAHFSTL PATPLCHALQ AHVLGGTLTV AVGGVLVAAL LVFTVALLVR
GRGAGNGRLP LKLSHVQSQT NGGTSPMPKS HPPRSPPPRP QRSCSLDLGD TGGCYGYARR
LGGAWARRSH SVHGGLLGAG CRGMGGSAER LEESVV
