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   02-OCT-2024, entry version 184.
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; 46.
DR   STRING; 9606.ENSP00000246529; -.
DR   GlyCosmos; Q9BTN0; 5 sites, No reported glycans.
DR   GlyGen; Q9BTN0; 5 sites.
DR   iPTMnet; Q9BTN0; -.
DR   PhosphoSitePlus; Q9BTN0; -.
DR   BioMuta; LRFN3; -.
DR   DMDM; 62286945; -.
DR   MassIVE; Q9BTN0; -.
DR   PaxDb; 9606-ENSP00000466989; -.
DR   PeptideAtlas; Q9BTN0; -.
DR   ProteomicsDB; 79001; -.
DR   Antibodypedia; 29620; 93 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   AGR; HGNC:28370; -.
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; 2942402at2759; -.
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; 12 hits in 1147 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 101 other cell types or tissues.
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:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
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; Immunoglobulins; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; IPR050467; LRFN.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45842:SF5; LEUCINE-RICH REPEAT AND FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
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; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW   Postsynaptic cell membrane; Proteomics identification; Reference proteome;
KW   Repeat; Signal; Synapse; 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
//