LRFN1_DANRE
ID LRFN1_DANRE Reviewed; 584 AA.
AC Q6PGX3; A8BBG4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Leucine-rich repeat and fibronectin type III domain-containing protein 1;
DE Flags: Precursor;
GN Name=lrfn1; ORFNames=zgc:63670;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=18296487; DOI=10.1101/gr.7187808;
RA Bushell K.M., Soellner C., Schuster-Boeckler B., Bateman A., Wright G.J.;
RT "Large-scale screening for novel low-affinity extracellular protein
RT interactions.";
RL Genome Res. 18:622-630(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of excitatory synapses.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGX3-2; Sequence=VSP_033620;
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; CU468795; CAP08019.1; -; mRNA.
DR EMBL; BC056798; AAH56798.1; -; mRNA.
DR RefSeq; NP_956909.1; NM_200615.1. [Q6PGX3-1]
DR AlphaFoldDB; Q6PGX3; -.
DR SMR; Q6PGX3; -.
DR STRING; 7955.ENSDARP00000111665; -.
DR GeneID; 393587; -.
DR KEGG; dre:393587; -.
DR CTD; 57622; -.
DR ZFIN; ZDB-GENE-040426-1227; lrfn1.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q6PGX3; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; Q6PGX3; -.
DR Reactome; R-DRE-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:Q6PGX3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; 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 PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..584
FT /note="Leucine-rich repeat and fibronectin type III domain-
FT containing protein 1"
FT /id="PRO_0000334148"
FT TOPO_DOM 18..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..584
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 149..170
FT /note="LRR 5"
FT REPEAT 173..194
FT /note="LRR 6"
FT REPEAT 197..218
FT /note="LRR 7"
FT DOMAIN 241..287
FT /note="LRRCT"
FT DOMAIN 288..375
FT /note="Ig-like"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
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 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 447
FT /note="Y -> YNSTVDDTLVYRMIPSASKTFRINDLAAGREY (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:18296487"
FT /id="VSP_033620"
SQ SEQUENCE 584 AA; 64563 MW; CF9030EB73C340C5 CRC64;
MERLVFCVLV FGALAKAQLC PGRCICQTIS PTLTLLCAKT GLLFVPPTVD RKTVELRLTD
NFITAVRRKD FLNMTSLVHL TLSRNTISQI APHAFMGLKS LRALHMDGNR LSVINSDQLK
GLMNLRHLIL GNNQIHHIEE SSFDEFVATI EDLDLSYNNL RTLPWEAIAR MTNINTLTLD
HNLIDHIGVG TFTLLTKLVR LDMTSNRLQT LPPDTLFQHA QVLSEPKTSS SSRLTVSFGG
NPLHCNCELL WLRRLTREDD LETCASPEHL MDKYFWSIQE EEFICEPPLI TKHQVTKPYV
MEGQGVTLKC KAMGDPDPAI HWRFPDGKLV HNNSRTILYD NGTLDILITT LKDSGAFNCV
ASNAAGIATA AVHVHMIPLP LLVNNTGHMR EADPGLSDIS TSSRSSSNDS KTHSKRVLVE
NLTAHSAVIH WPSERHIPGI RMYQIQYELC VLAVYDDGIT SLTATRVVGC VHFHTLPETN
QCRFVPSQFL GGTMIIIIGG IIVASVLVFI IILMIRYKAY SGGGGDTAKA KAGGDVSVHV
HSQTNGSRSA ATKQSEEPPE SPAGKHCKAL VLLKMVLPIL HLLF
