LRFN3_AILME
ID LRFN3_AILME Reviewed; 628 AA.
AC D2HFT7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 3;
DE AltName: Full=Synaptic adhesion-like molecule 4;
DE Flags: Precursor;
GN Name=LRFN3; Synonyms=SALM4; ORFNames=PANDA_009783;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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 LRFN1, LRFN2, LRFN4 and
CC LRFN5. Able to form homomeric complexes across cell junctions, between
CC adjacent cells. Does not interact with DLG4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell projection, axon. Cell projection, dendrite. Synapse.
CC Presynaptic cell membrane. Postsynaptic cell membrane {ECO:0000250}.
CC -!- DOMAIN: Lacks a cytoplasmic PDZ-binding domain, which has been
CC implicated in function of related Lrfn proteins.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; GL192794; EFB29885.1; -; Genomic_DNA.
DR RefSeq; XP_002920951.1; XM_002920905.3.
DR AlphaFoldDB; D2HFT7; -.
DR SMR; D2HFT7; -.
DR STRING; 9646.ENSAMEP00000000896; -.
DR Ensembl; ENSAMET00000000932; ENSAMEP00000000896; ENSAMEG00000000862.
DR GeneID; 100472610; -.
DR KEGG; aml:100472610; -.
DR CTD; 79414; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161203; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; D2HFT7; -.
DR OMA; EPALQPC; -.
DR OrthoDB; 151757at2759; -.
DR TreeFam; TF350185; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..628
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 3"
FT /id="PRO_0000394520"
FT TOPO_DOM 17..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..59
FT /note="LRRNT"
FT REPEAT 84..105
FT /note="LRR 1"
FT REPEAT 108..129
FT /note="LRR 2"
FT REPEAT 132..153
FT /note="LRR 3"
FT REPEAT 157..178
FT /note="LRR 4"
FT REPEAT 181..202
FT /note="LRR 5"
FT REPEAT 205..226
FT /note="LRR 6"
FT DOMAIN 249..295
FT /note="LRRCT"
FT DOMAIN 295..382
FT /note="Ig-like"
FT DOMAIN 427..525
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 380..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 317..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 628 AA; 66170 MW; 799E0276005F826F CRC64;
MAVLPLLLCL LPLAPASSPS QPATPSPCPR RCRCQTQSLP LSVLCPGAGL LFVPPSLDRR
AAELRLADNF IAAVRRRDLA NMTGLLHLSL SRNTIRHVAA GAFADLRALR ALHLDGNRLT
SLGEGQLRGL VNLRHLILSN NQLAALAAGA LDDCAETLED LDLSYNNLEQ LPWEALGRLG
NVNTLGLDHN LLASVPAGAF SRLHKLARLD MTSNRLTTIP PDPLFSRLPL LARPRGSPAS
ALVLAFGGNP LHCNCELVWL RRLAREDDLE ACASPPALGG RYFWAVGEEE FVCEPPVVTH
RSPPLAVPAG RPAALRCRAV GDPEPRVRWV SPQGRLVGNS SRARAFPNGT LELLVTEPGD
GGIFTCIAAN AAGEATAAVE LTVGPPPPPQ LANSTSCDPP RDGDPDALTP PSAASASAAA
KAADTGPPTD RGVQVTEHGA TAALVQWPDQ RPIPGIRMYQ IQYNSSADDI LVYRMIPADS
HSFLLSDLAS GRTYDLCVLA VYEDGATGLT ATRPVGCARF STEPALRPCG APHAPFLGGT
MIIALGGVIV ASVLVFIFVL LMRYKVHGGQ PPGKAKAPAP VSSVCLQTNG SLGPTPAPPA
PEPAAPRAHT VVQLDCEPWR PSHEPTGP
