LRFN5_RAT
ID LRFN5_RAT Reviewed; 719 AA.
AC D4A1J9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 5;
DE Flags: Precursor;
GN Name=Lrfn5; Synonyms=Salm5;
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.
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 LRFN2, LRFN3 and LFRN4 (By
CC similarity). Weakly interacts with LRFN1. Able to form homomeric
CC complexes across cell junctions, between adjacent cells (By
CC similarity). Does not interact with DLG1, DLG2, DLG3, nor with DLG4 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: Lacks a cytoplasmic PDZ-binding motif, which has been
CC implicated in function of related LRFN proteins.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; CH473947; EDM03478.1; -; Genomic_DNA.
DR RefSeq; NP_001101494.1; NM_001108024.1.
DR AlphaFoldDB; D4A1J9; -.
DR SMR; D4A1J9; -.
DR STRING; 10116.ENSRNOP00000007600; -.
DR GlyGen; D4A1J9; 2 sites.
DR PaxDb; D4A1J9; -.
DR Ensembl; ENSRNOT00000007600; ENSRNOP00000007600; ENSRNOG00000005550.
DR GeneID; 314164; -.
DR KEGG; rno:314164; -.
DR CTD; 145581; -.
DR RGD; 1309357; Lrfn5.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158296; -.
DR HOGENOM; CLU_016998_0_0_1; -.
DR InParanoid; D4A1J9; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; D4A1J9; -.
DR TreeFam; TF350185; -.
DR PRO; PR:D4A1J9; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000005550; Expressed in frontal cortex and 1 other tissue.
DR ExpressionAtlas; D4A1J9; baseline and differential.
DR Genevisible; D4A1J9; 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; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0043031; P:negative regulation of macrophage activation; ISS:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
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; IPR026879; Lrfn5.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR45842:SF10; PTHR45842:SF10; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13306; LRR_5; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..719
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 5"
FT /id="PRO_0000394523"
FT TOPO_DOM 18..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..51
FT /note="LRRNT"
FT REPEAT 52..73
FT /note="LRR 1"
FT REPEAT 76..97
FT /note="LRR 2"
FT REPEAT 100..121
FT /note="LRR 3"
FT REPEAT 124..145
FT /note="LRR 4"
FT REPEAT 148..169
FT /note="LRR 5"
FT REPEAT 172..193
FT /note="LRR 6"
FT REPEAT 196..217
FT /note="LRR 7"
FT DOMAIN 240..286
FT /note="LRRCT"
FT DOMAIN 287..373
FT /note="Ig-like"
FT DOMAIN 414..503
FT /note="Fibronectin type-III"
FT REGION 383..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..719
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 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 719 AA; 79339 MW; 783F0A68B17C4707 CRC64;
MEKFLFYLFL IGIAVRAQIC PKRCVCQILS PNLATLCAKK GLLFVPPNID RRTVELRLAD
NFVTNIKRKD FANMTSLVDL TLSRNTISFI TPHAFADLRN LRALHLNSNR LTKITNDMFS
GLSNLHHLIL NNNQLTLISS TAFDDVFALE ELDLSYNNLE TIPWDAVEKM VSLHTLSLDH
NMIDNIPKGT FSHLHKMTRL DVTSNKLQKL PPDPLFQRAQ VLATSGIISP STFALSFGGN
PLHCNCELLW LRRLSREDDL ETCASPALLT GRYFWSIPEE EFLCEPPLIT RHTHEMRVLE
GQRATLRCKA RGDPEPAIHW ISPEGKLISN ATRSLVYDNG TLDILITTVK DTGAFTCIAS
NPAGEATQTM DLHIIKLPHL LNSTNNIHEP DPGSSDISTS TKSGSNASSS NGDTKMSQDK
IVVAEASSST ALLKFNFQRN IPGIRMFQIQ YNGTYDDTLV YRMIPPTSKT FLVNNLASGT
MYDLCVLAIY DDGITSLTAT RVVGCIQFTT EQDYVRCHFM QSQFLGGTMI IIIGGIIVAS
VLVFIIILMI RYKVCNNNGQ HKVTKVSNVY SQTNGAQMQG CSVTLPQSMS KQAMGHEENA
QCCKVASDSA IQSSETCSSQ DSSTTTSALP PTWTSSAPVS QKQKRKTGTK PSAEPQSEAV
TNVESQNTNR NNSTALQLAS CPPDSVTEGP TSQRAHTKPN ALLTNVDQNV QETQRLESI
