LFN1L_DANRE
ID LFN1L_DANRE Reviewed; 687 AA.
AC A8WGA3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Leucine-rich repeat and fibronectin type III domain-containing protein 1-like protein;
DE Flags: Precursor;
GN Name=lrfn1l; ORFNames=zgc:172282;
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].
RC STRAIN=WIK;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be 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 -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; BC154635; AAI54636.1; -; mRNA.
DR RefSeq; NP_001107121.1; NM_001113649.1.
DR AlphaFoldDB; A8WGA3; -.
DR SMR; A8WGA3; -.
DR PaxDb; A8WGA3; -.
DR GeneID; 100003690; -.
DR KEGG; dre:100003690; -.
DR ZFIN; ZDB-GENE-080219-38; zgc:172282.
DR InParanoid; A8WGA3; -.
DR PhylomeDB; A8WGA3; -.
DR TreeFam; TF350185; -.
DR PRO; PR:A8WGA3; -.
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:0099059; C:integral component of presynaptic active zone membrane; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..687
FT /note="Leucine-rich repeat and fibronectin type III domain-
FT containing protein 1-like protein"
FT /id="PRO_0000334149"
FT TOPO_DOM 18..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..687
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 287..376
FT /note="Ig-like"
FT DOMAIN 415..510
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 384..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 309..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 687 AA; 75776 MW; 6A8D527F8F0768EA CRC64;
MEWLIFSLLL LAVSASGQLC PKRCMCQNLS PSLAILCAKT GLLFVPTVID RRTVELRLTE
NFITAVKRRD FANMTSLLHL TLSRNTISQI MPYTFADLKR LRALHLDSNR LSVITDDHFR
GLTNLRHLIL ANNQLHNISP HAFDDFLGTL EDLDLSYNNL VDIPWDTIGR LTNVNTLNMD
HNLIEHVPLG IFSNLHKLAR LDMTSNKLKK IPPDPLFLRI PVYAKSKGSP LSSLVLSFGG
NPLHCNCELL WLRRLTREDD LETCASPPDL TAKYFWTIPE EEFICDPPVI TRKSPKTFAM
EGQPTSLKCK ANGDPDPDVH WISPEGRLIA NTSRTLSFSN GSLEINITSL KDTGIFTCIA
SNAAGESTGT VELVVSPLPH LANSTNRIRE PDPGPSDILT SAKSTSSVSN ETRSQERKVV
LAELSANSAL IRWPSQQHFP GIRMYQIQYN SSVDDTLVYR MIPSTSFDFL VRDLVSGREY
DLCVLAVYDD GVTSLTATRQ VGCVTFVTET EFSQCQSLRS HFLGGTMIII IGGIIVASVL
VFIIILMIRY KVYSQHGADS GKGTAMTNVR SQTNGGQAAG QVPRSSSKIV EGQEASGGSL
GGAANIKDST ALVLVTDSET AVQISEISSE DIVSPTQRHH PRTCIELKRR PSLSCKEGTS
SDTQEDTASP QVSDEKKAQR DWSDFKI
