LRFN3_HUMAN
ID LRFN3_HUMAN Reviewed; 628 AA.
AC Q9BTN0; Q6UY10;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
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=UNQ5865/PRO34192;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Smooth muscle cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}.
CC Cell projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}.
CC Presynaptic cell membrane {ECO:0000250}. Postsynaptic cell membrane
CC {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; AK172754; BAD18740.1; -; mRNA.
DR EMBL; AY358127; AAQ88494.1; -; mRNA.
DR EMBL; BC003578; AAH03578.1; -; mRNA.
DR CCDS; CCDS12483.1; -.
DR RefSeq; NP_078785.1; NM_024509.1.
DR RefSeq; XP_016882791.1; XM_017027302.1.
DR AlphaFoldDB; Q9BTN0; -.
DR SMR; Q9BTN0; -.
DR BioGRID; 122664; 97.
DR IntAct; Q9BTN0; 13.
DR STRING; 9606.ENSP00000466989; -.
DR GlyGen; Q9BTN0; 5 sites.
DR iPTMnet; Q9BTN0; -.
DR PhosphoSitePlus; Q9BTN0; -.
DR BioMuta; LRFN3; -.
DR DMDM; 62286945; -.
DR EPD; Q9BTN0; -.
DR MassIVE; Q9BTN0; -.
DR PaxDb; Q9BTN0; -.
DR PeptideAtlas; Q9BTN0; -.
DR PRIDE; Q9BTN0; -.
DR ProteomicsDB; 79001; -.
DR Antibodypedia; 29620; 83 antibodies from 25 providers.
DR DNASU; 79414; -.
DR Ensembl; ENST00000246529.4; ENSP00000246529.3; ENSG00000126243.9.
DR Ensembl; ENST00000588831.5; ENSP00000466989.1; ENSG00000126243.9.
DR GeneID; 79414; -.
DR KEGG; hsa:79414; -.
DR MANE-Select; ENST00000246529.4; ENSP00000246529.3; NM_024509.2; NP_078785.1.
DR UCSC; uc002oco.4; human.
DR CTD; 79414; -.
DR DisGeNET; 79414; -.
DR GeneCards; LRFN3; -.
DR HGNC; HGNC:28370; LRFN3.
DR HPA; ENSG00000126243; Low tissue specificity.
DR MIM; 612809; gene.
DR neXtProt; NX_Q9BTN0; -.
DR OpenTargets; ENSG00000126243; -.
DR PharmGKB; PA134880779; -.
DR VEuPathDB; HostDB:ENSG00000126243; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161203; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; Q9BTN0; -.
DR OMA; EPALQPC; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; Q9BTN0; -.
DR PathwayCommons; Q9BTN0; -.
DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR SignaLink; Q9BTN0; -.
DR SIGNOR; Q9BTN0; -.
DR BioGRID-ORCS; 79414; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; LRFN3; human.
DR GenomeRNAi; 79414; -.
DR Pharos; Q9BTN0; Tdark.
DR PRO; PR:Q9BTN0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BTN0; protein.
DR Bgee; ENSG00000126243; Expressed in cortical plate and 99 other tissues.
DR Genevisible; Q9BTN0; HS.
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:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IEA:Ensembl.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
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_0000014841"
FT TOPO_DOM 17..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..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 425..523
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 382..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 317..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 14
FT /note="A -> V (in dbSNP:rs34933126)"
FT /id="VAR_049895"
FT CONFLICT 197
FT /note="Missing (in Ref. 2; AAQ88494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 66260 MW; FEDC5A5056ABC5FC CRC64;
MAILPLLLCL LPLAPASSPP QSATPSPCPR RCRCQTQSLP LSVLCPGAGL LFVPPSLDRR
AAELRLADNF IASVRRRDLA 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 SPQGRLLGNS SRARAFPNGT LELLVTEPGD
GGIFTCIAAN AAGEATAAVE LTVGPPPPPQ LANSTSCDPP RDGDPDALTP PSAASASAKV
ADTGPPTDRG VQVTEHGATA ALVQWPDQRP IPGIRMYQIQ YNSSADDILV YRMIPAESRS
FLLTDLASGR TYDLCVLAVY EDSATGLTAT RPVGCARFST EPALRPCGAP HAPFLGGTMI
IALGGVIVAS VLVFIFVLLM RYKVHGGQPP GKAKIPAPVS SVCSQTNGAL GPTPTPAPPA
PEPAALRAHT VVQLDCEPWG PGHEPVGP
