ID LRFN5_MOUSE Reviewed; 719 AA.
AC Q8BXA0; Q5DTH4; Q8BJH4; Q8BZL0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 163.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 5;
DE Flags: Precursor;
GN Name=Lrfn5; Synonyms=Kiaa4208, Salm5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [4]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GLYCOSYLATION, LACK OF INTERACTION
RP WITH DLG4, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA Morimura N., Inoue T., Katayama K., Aruga J.;
RT "Comparative analysis of structure, expression and PSD95-binding capacity
RT of Lrfn, a novel family of neuronal transmembrane proteins.";
RL Gene 380:72-83(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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, LRFN3 and
CC LFRN4 (By similarity). Able to form homomeric complexes across cell
CC junctions, between adjacent cells (By similarity). Does not interact
CC with DLG1, DLG2 or DLG3 (By similarity). Does not interact with DLG4.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16828986}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BXA0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BXA0-2; Sequence=VSP_009299;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with a weak,
CC but broad expression in the cerebral cortex and diencephalic nuclei.
CC Strongly expressed in both the pyramidal layer and the dentate gyrus of
CC the hippocampus. Also detected in other parts of the central nervous
CC system, including the olfactory bulb, pons, cerebellum, and medulla
CC oblongata, as well as in the peripheral nervous system, such as the
CC ganglia of cranial nerves and the dorsal root ganglion during
CC gestation. {ECO:0000269|PubMed:16828986}.
CC -!- DEVELOPMENTAL STAGE: Expression starts around 11.5-12.5 dpc. At 11.5
CC dpc, detected in the outer layer of the telencephalic vesicles. This
CC pattern of expression continues until 17.5 dpc with expression in the
CC cortical plate, but not in the inner layer of the cerebral cortex,
CC including subplate, ventricular zone, and subventricular zone. As also
CC detected in the hippocampus, amygdala and widely in diencephalic
CC nuclei. {ECO:0000269|PubMed:16828986}.
CC -!- DOMAIN: Lacks a cytoplasmic PDZ-binding motif, which has been
CC implicated in function of related LRFN proteins.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16828986}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90535.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK034245; BAC28645.1; -; mRNA.
DR EMBL; AK048443; BAC33339.1; -; mRNA.
DR EMBL; AK220546; BAD90535.1; ALT_INIT; mRNA.
DR EMBL; BC052038; AAH52038.1; -; mRNA.
DR CCDS; CCDS25936.1; -. [Q8BXA0-2]
DR CCDS; CCDS79117.1; -. [Q8BXA0-1]
DR RefSeq; NP_001297515.1; NM_001310586.1. [Q8BXA0-1]
DR RefSeq; NP_848829.2; NM_178714.5. [Q8BXA0-2]
DR RefSeq; XP_006515893.1; XM_006515830.2. [Q8BXA0-2]
DR RefSeq; XP_006515894.1; XM_006515831.3. [Q8BXA0-2]
DR RefSeq; XP_017170545.1; XM_017315056.1. [Q8BXA0-1]
DR PDB; 6F2O; X-ray; 3.00 A; A=18-376.
DR PDBsum; 6F2O; -.
DR AlphaFoldDB; Q8BXA0; -.
DR SASBDB; Q8BXA0; -.
DR SMR; Q8BXA0; -.
DR STRING; 10090.ENSMUSP00000051546; -.
DR GlyConnect; 2424; 3 N-Linked glycans (1 site). [Q8BXA0-2]
DR GlyCosmos; Q8BXA0; 6 sites, 3 glycans.
DR GlyGen; Q8BXA0; 7 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q8BXA0; -.
DR PhosphoSitePlus; Q8BXA0; -.
DR PaxDb; 10090-ENSMUSP00000051546; -.
DR PeptideAtlas; Q8BXA0; -.
DR ProteomicsDB; 290167; -. [Q8BXA0-1]
DR ProteomicsDB; 290168; -. [Q8BXA0-2]
DR ABCD; Q8BXA0; 1 sequenced antibody.
DR Antibodypedia; 78; 77 antibodies from 23 providers.
DR Ensembl; ENSMUST00000055815.14; ENSMUSP00000051546.8; ENSMUSG00000035653.17. [Q8BXA0-2]
DR Ensembl; ENSMUST00000119481.2; ENSMUSP00000113123.2; ENSMUSG00000035653.17. [Q8BXA0-1]
DR GeneID; 238205; -.
DR KEGG; mmu:238205; -.
DR UCSC; uc007nqm.1; mouse. [Q8BXA0-2]
DR UCSC; uc007nqn.1; mouse. [Q8BXA0-1]
DR AGR; MGI:2144814; -.
DR CTD; 145581; -.
DR MGI; MGI:2144814; Lrfn5.
DR VEuPathDB; HostDB:ENSMUSG00000035653; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158296; -.
DR HOGENOM; CLU_016998_0_0_1; -.
DR InParanoid; Q8BXA0; -.
DR OMA; NGQHKAT; -.
DR OrthoDB; 2942402at2759; -.
DR PhylomeDB; Q8BXA0; -.
DR TreeFam; TF350185; -.
DR BioGRID-ORCS; 238205; 2 hits in 60 CRISPR screens.
DR ChiTaRS; Lrfn5; mouse.
DR PRO; PR:Q8BXA0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BXA0; Protein.
DR Bgee; ENSMUSG00000035653; Expressed in cortical plate and 99 other cell types or tissues.
DR Genevisible; Q8BXA0; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IMP:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
DR CDD; cd05764; IgI_SALM5_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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 PANTHER; PTHR45842:SF10; LEUCINE-RICH REPEAT AND FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 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 SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..719
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 5"
FT /id="PRO_0000014846"
FT TOPO_DOM 18..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..719
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 148..169
FT /note="LRR 5"
FT REPEAT 172..193
FT /note="LRR 6"
FT REPEAT 196..217
FT /note="LRR 7"
FT DOMAIN 240..286
FT /note="LRRCT"
FT DOMAIN 287..373
FT /note="Ig-like"
FT DOMAIN 414..503
FT /note="Fibronectin type-III"
FT REGION 385..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
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 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 700..719
FT /note="NALLTNVDQNVQETQRLESI -> SKFLTVPAEGSRARHRASLSGGLKDSFH
FT YGNSQLSLKRSMSMNAMWT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009299"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6F2O"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6F2O"
FT TURN 92..97
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6F2O"
FT TURN 116..121
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6F2O"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6F2O"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6F2O"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:6F2O"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:6F2O"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:6F2O"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:6F2O"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:6F2O"
SQ SEQUENCE 719 AA; 79371 MW; DCA5D8C68F7D6FEC CRC64;
MEKFLFYLFL IGIAVRAQIC PKRCVCQILS PNLATLCAKK GLLFVPPNID RRTVELRLAD
NFVTNIKRKD FANMTSLVDL TLSRNTISFI TPHAFADLRN LRALHLNSNR LTKITNDMFS
GLSNLHHLIL NNNQLTLISS TAFDDVFALE ELDLSYNNLE TIPWDAVEKM VSLHTLSLDH
NMIDNIPKGT FSHLHKMTRL DVTSNKLQKL PPDPLFQRAQ VLATSGIISP STFALSFGGN
PLHCNCELLW LRRLSREDDL ETCASPALLT GRYFWSIPEE EFLCEPPLIT RHTHEMRVLE
GQRATLRCKA RGDPEPAIHW ISPEGKLISN ATRSLVYDNG TLDILITTVK DTGAFTCIAS
NPAGEATQTV DLHIIKLPHL LNSTNHIHEP DPGSSDISTS TKSGSNASSS NGDTKMSQDK
IVVAEATSST ALLKFNFQRN IPGIRMFQIQ YNGTYDDTLV YRMIPPTSKT FLVNNLASGT
MYDLCVLAIY DDGITSLTAT RVVGCIQFTT EQDYVRCHFM QSQFLGGTMI IIIGGIIVAS
VLVFIIILMI RYKVCNNNGQ HKVTKVSNVY SQTNGAQMQG CSVTLPQSMS KQAMGHEENA
QCCKVASDNA IQSSETCSSQ DSSTTTSALP PTWTSSAPVS QKQKRKTGTK PSAEPQSEAV
TNVESQNTNR NNSTALQLAS CPPDSVTEGP TSQRAHTKPN ALLTNVDQNV QETQRLESI
//
