LRFN4_MOUSE
ID LRFN4_MOUSE Reviewed; 636 AA.
AC Q80XU8; Q3TQG8; Q460G5; Q8K3C4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 4;
DE Flags: Precursor;
GN Name=Lrfn4; Synonyms=Salm3;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=16495444; DOI=10.1523/jneurosci.3799-05.2006;
RA Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.;
RT "A novel family of adhesion-like molecules that interacts with the NMDA
RT receptor.";
RL J. Neurosci. 26:2174-2183(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 FUNCTION, INTERACTION WITH DLG4, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP GLYCOSYLATION, 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 INTERACTION WITH LRFN1; LRFN2; LRFN3 AND LRFN5, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=18227064; DOI=10.1074/jbc.m709456200;
RA Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X., Petralia R.S.,
RA Wenthold R.J.;
RT "The SALM family of adhesion-like molecules forms heteromeric and homomeric
RT complexes.";
RL J. Biol. Chem. 283:8395-8405(2008).
RN [6]
RP FUNCTION.
RX PubMed=18585462; DOI=10.1016/j.mcn.2008.05.019;
RA Wang P.Y., Seabold G.K., Wenthold R.J.;
RT "Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.";
RL Mol. Cell. Neurosci. 39:83-94(2008).
RN [7]
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: Promotes neurite outgrowth in hippocampal neurons. May play a
CC role in redistributing DLG4 to the cell periphery.
CC {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18585462}.
CC -!- SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN3 and
CC LRFN5. Unable to form homophilic interactions across cell junctions.
CC Interacts with DLG1, DLG2 and DLG3 (By similarity). Also interacts with
CC DLG4. {ECO:0000250, ECO:0000269|PubMed:16828986,
CC ECO:0000269|PubMed:18227064}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986,
CC ECO:0000269|PubMed:18227064}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis. In the brain, weak,
CC but broad expression in the cerebral cortex and diencephalic nuclei.
CC Also detected in other parts of the central nervous system, including
CC the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as
CC in the peripheral nervous system, such as the ganglia of cranial nerves
CC and the dorsal root ganglion during gestation.
CC {ECO:0000269|PubMed:16828986}.
CC -!- DEVELOPMENTAL STAGE: Low expression from 4.5 dpc onwards. Expression
CC increases at 10.5 dpc and decreases after 15.5 dpc. At 11.5 dpc,
CC broadly expressed in the telencephalic and diencephalic vesicles. This
CC pattern of expression continues until 17.5 dpc.
CC {ECO:0000269|PubMed:16828986}.
CC -!- DOMAIN: The PDZ-binding motif is required for neurite outgrowth
CC promotion. This motif is also involved in DLG1-, DLG3- and DLG4-binding
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16828986}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; DQ078786; AAZ23615.1; -; mRNA.
DR EMBL; AK081560; BAC38259.1; -; mRNA.
DR EMBL; AK163603; BAE37415.1; -; mRNA.
DR EMBL; BC023036; AAH23036.1; -; mRNA.
DR EMBL; BC023156; AAH23156.1; -; mRNA.
DR CCDS; CCDS29431.1; -.
DR RefSeq; NP_700437.2; NM_153388.4.
DR RefSeq; XP_017173631.1; XM_017318142.1.
DR PDB; 6TL8; X-ray; 2.80 A; A/B/C/D=17-284.
DR PDBsum; 6TL8; -.
DR AlphaFoldDB; Q80XU8; -.
DR SASBDB; Q80XU8; -.
DR SMR; Q80XU8; -.
DR BioGRID; 230437; 1.
DR STRING; 10090.ENSMUSP00000109453; -.
DR GlyGen; Q80XU8; 6 sites.
DR iPTMnet; Q80XU8; -.
DR PhosphoSitePlus; Q80XU8; -.
DR MaxQB; Q80XU8; -.
DR PaxDb; Q80XU8; -.
DR PeptideAtlas; Q80XU8; -.
DR PRIDE; Q80XU8; -.
DR ProteomicsDB; 290166; -.
DR Antibodypedia; 30278; 51 antibodies from 21 providers.
DR DNASU; 225875; -.
DR Ensembl; ENSMUST00000053597; ENSMUSP00000050039; ENSMUSG00000045045.
DR Ensembl; ENSMUST00000113822; ENSMUSP00000109453; ENSMUSG00000045045.
DR GeneID; 225875; -.
DR KEGG; mmu:225875; -.
DR UCSC; uc008gah.2; mouse.
DR CTD; 78999; -.
DR MGI; MGI:2385612; Lrfn4.
DR VEuPathDB; HostDB:ENSMUSG00000045045; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000162195; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; Q80XU8; -.
DR OMA; EAYPDCH; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; Q80XU8; -.
DR TreeFam; TF350185; -.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 225875; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q80XU8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q80XU8; protein.
DR Bgee; ENSMUSG00000045045; Expressed in embryonic brain and 167 other tissues.
DR Genevisible; Q80XU8; 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:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..636
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 4"
FT /id="PRO_0000014844"
FT TOPO_DOM 17..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..48
FT /note="LRRNT"
FT REPEAT 49..70
FT /note="LRR 1"
FT REPEAT 73..94
FT /note="LRR 2"
FT REPEAT 97..118
FT /note="LRR 3"
FT REPEAT 121..142
FT /note="LRR 4"
FT REPEAT 146..169
FT /note="LRR 5"
FT REPEAT 170..191
FT /note="LRR 6"
FT REPEAT 194..215
FT /note="LRR 7"
FT DOMAIN 234..280
FT /note="LRRCT"
FT DOMAIN 281..367
FT /note="Ig-like"
FT DOMAIN 405..502
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 556..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 633..636
FT /note="PDZ-binding"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJG9"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJG9"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 302..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 503
FT /note="T -> N (in Ref. 1; AAZ23615 and 3; AAH23156)"
FT /evidence="ECO:0000305"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6TL8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6TL8"
FT TURN 89..94
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6TL8"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6TL8"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6TL8"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6TL8"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6TL8"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6TL8"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:6TL8"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:6TL8"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:6TL8"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:6TL8"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6TL8"
SQ SEQUENCE 636 AA; 67252 MW; 1EE86E96CB88BA91 CRC64;
MAPPLLLLLL ASGAAACPLP CVCQNLSESL STLCAHRGLL FVPPNVDRRT VELRLADNFI
QALGPPDFRN MTGLVDLTLS RNAITRIGAR SFGDLESLRS LHLDGNRLVE LGSSSLRGPV
NLQHLILSGN QLGRIAPGAF DDFLDSLEDL DVSYNNLRQV PWAGIGSMPA LHTLNLDHNL
IDALPPGVFA QLSQLSRLDL TSNRLATLAP DPLFSRGRDA EASPSPLVLS FSGNPLHCNC
ELLWLRRLAR PDDLETCASP PTLAGRYFWA VPEGEFSCEP PLIARHTQRL WVLEGQRATL
RCRALGDPVP TMHWVGPDDR LVGNSSRAWA FPNGTLEIGV TGAGDAGAYT CIATNPAGEA
TARVELRVLA LPHGGNTSAE GGRPGPSDIA ASARTAAEGE GTLESEPAVQ VTEVTATSGL
VSWGLGRPAD PVWMFQIQYN SSEDETLIYR IVPASSHHFL LKHLVPGADY DLCLLALSPA
AGPSDLTATR LLGCAHFSTL PATPLCHALQ AHVLGGTLTV AVGGVLVAAL LVFTVALLVR
GRGAGNGRLP LKLSHVQSQT NGGTSPMPKS HPPRSPPPRP QRSCSLDLGD TGGCYGYARR
LGGAWARRSH SVHGGLLGAG CRGVGGSAER LEESVV
