LRFN3_BOVIN
ID LRFN3_BOVIN Reviewed; 628 AA.
AC Q1RMS4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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; BC114740; AAI14741.1; -; mRNA.
DR RefSeq; NP_001070427.1; NM_001076959.1.
DR RefSeq; XP_005219090.1; XM_005219033.3.
DR AlphaFoldDB; Q1RMS4; -.
DR SMR; Q1RMS4; -.
DR STRING; 9913.ENSBTAP00000000176; -.
DR PaxDb; Q1RMS4; -.
DR PRIDE; Q1RMS4; -.
DR Ensembl; ENSBTAT00000000176; ENSBTAP00000000176; ENSBTAG00000000153.
DR GeneID; 767839; -.
DR KEGG; bta:767839; -.
DR CTD; 79414; -.
DR VEuPathDB; HostDB:ENSBTAG00000000153; -.
DR VGNC; VGNC:30977; LRFN3.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161203; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; Q1RMS4; -.
DR OrthoDB; 151757at2759; -.
DR TreeFam; TF350185; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000000153; Expressed in vas deferens and 103 other tissues.
DR ExpressionAtlas; Q1RMS4; baseline.
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; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic 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 2: Evidence at transcript level;
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_0000394521"
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 60..83
FT /note="LRR 1"
FT REPEAT 84..105
FT /note="LRR 2"
FT REPEAT 108..129
FT /note="LRR 3"
FT REPEAT 132..153
FT /note="LRR 4"
FT REPEAT 157..178
FT /note="LRR 5"
FT REPEAT 181..202
FT /note="LRR 6"
FT REPEAT 205..226
FT /note="LRR 7"
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..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Polar residues"
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; 66260 MW; 6A8C5D2FFE30A88A CRC64;
MAVLPLLLCL LPLAPASSPP QPASPSPCPR RCRCQTQSLP LSVLCPGAGL LFVPPSLDRR
AAELRLADNF IATVRRRDLA NMTGLLHLSL SRNTIRHVAA GAFSDLRALR ALHLDGNRLT
SLGEGQLRGL VNLRHLILSN NQLAALAAGA LDDCAETLED LDLSYNNLEQ LPWEALGRLG
NVNTLGLDHN LLASVPAGAF SRLHKLARLD MTSNRLTTIP PDPLFSRLPL LARPRGSPAS
ALVLAFGGNP LHCNCELVWL RRLAREDDLE ACASPPALGG RYFWAVGEEE FVCEPPVVTH
RSPPLAVPAG RPAALRCRAV GDPEPRVRWV SPQGRLLGNS SRARAFPNGT LELLVTEPGD
GGIFTCIAAN AAGEATAAVE LTVGPPPPPQ LANSTSCDPP RDGEPDALTP PSAASASASA
KAAEAGPPTD RGVQVTEHGA TAALIQWPDQ RPIPGIRMYQ IQYNSSADDI LVYRMIPAES
SSFLLTDLAS GRTYDLCVLA VYEDSATGLT ATRPVGCNRF STEPALRPCG APHAPFLGGT
MIIALGGVIV ASVLVFIFVL LMRYKVHGGQ PPGKTKASAP VSSVCSQTNG ALGPMPAPPA
PEPSAPRAHT VVQLDCEPWG PSHEPMGP
