LRFN1_RAT
ID LRFN1_RAT Reviewed; 766 AA.
AC P0C7J6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Leucine-rich repeat and fibronectin type III domain-containing protein 1;
DE AltName: Full=Synaptic adhesion-like molecule 2;
DE Flags: Precursor;
GN Name=Lrfn1; Synonyms=Salm2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP GLYCOSYLATION, INTERACTION WITH DLG1; DLG2; DLG4; GRIA1; GRIA2 AND GRIN1,
RP AND MUTAGENESIS OF 764-SER--VAL-766.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [3]
RP INTERACTION WITH LRFN2; LRFN4 AND LRFN5.
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).
CC -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons (By
CC similarity). Involved in the regulation of the differentiation and
CC maintenance of excitatory synapses. Induces the clustering of
CC excitatory postsynaptic proteins, including DLG4, DLGAP1, GRIA1 and
CC GRIN1. {ECO:0000250, ECO:0000269|PubMed:16630835}.
CC -!- SUBUNIT: Forms heteromeric complexes with LRFN2, LRFN4 and LRFN5;
CC binding to LRFN2 and LRFN5 may be weaker than that to LRFN4. Also
CC interacts with LRFN3 (By similarity). Forms homomeric complexes, but
CC not across cell junctions (By similarity). Interacts with DLG1, DLG2
CC and DLG4, but not with MAGI2, not CASK. Interacts with DLG3 (By
CC similarity). Interacts with 2 AMPA receptor subunits GRIA1 and GRIA2
CC and NMDA receptor subunit GRIN1. {ECO:0000250,
CC ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:18227064}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16630835}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16630835}. Synapse
CC {ECO:0000269|PubMed:16630835}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:16630835}. Note=Detected in excitatory, but not
CC inhibitory, synaptic plasma membrane.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain (at protein level) and
CC testis. In brain, found in cerebral cortex (including pyramidal
CC neurons), hippocampus (including CA3 and CA1 neurons), dentate gyrus,
CC cerebellum (including Purkinje neurons) (at protein level) (at protein
CC level). Also expressed in the olfactory bulb.
CC {ECO:0000269|PubMed:16630835}.
CC -!- DEVELOPMENTAL STAGE: Expression increases steadily during postnatal rat
CC brain development. {ECO:0000269|PubMed:16630835}.
CC -!- DOMAIN: The PDZ-binding motif is required for neurite outgrowth
CC promotion (By similarity). This motif is also involved in DLG1-,
CC DLG3- and DLG4-binding. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16630835}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; AABR03001365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001121166.1; NM_001127694.1.
DR RefSeq; XP_006228688.1; XM_006228626.3.
DR RefSeq; XP_006228690.1; XM_006228628.3.
DR RefSeq; XP_008757396.1; XM_008759174.2.
DR RefSeq; XP_008757397.1; XM_008759175.2.
DR RefSeq; XP_017444960.1; XM_017589471.1.
DR RefSeq; XP_017444961.1; XM_017589472.1.
DR RefSeq; XP_017444962.1; XM_017589473.1.
DR AlphaFoldDB; P0C7J6; -.
DR SMR; P0C7J6; -.
DR STRING; 10116.ENSRNOP00000053905; -.
DR GlyGen; P0C7J6; 2 sites.
DR iPTMnet; P0C7J6; -.
DR PhosphoSitePlus; P0C7J6; -.
DR PaxDb; P0C7J6; -.
DR PRIDE; P0C7J6; -.
DR Ensembl; ENSRNOT00000057073; ENSRNOP00000053905; ENSRNOG00000019869.
DR GeneID; 365222; -.
DR KEGG; rno:365222; -.
DR UCSC; RGD:1304707; rat.
DR CTD; 57622; -.
DR RGD; 1304707; Lrfn1.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160922; -.
DR HOGENOM; CLU_016998_0_1_1; -.
DR InParanoid; P0C7J6; -.
DR OMA; TRVRWDG; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; P0C7J6; -.
DR TreeFam; TF350185; -.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:P0C7J6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019869; Expressed in frontal cortex and 15 other tissues.
DR ExpressionAtlas; P0C7J6; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; 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.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..766
FT /note="Leucine-rich repeat and fibronectin type III domain-
FT containing protein 1"
FT /id="PRO_0000334147"
FT TOPO_DOM 32..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..65
FT /note="LRRNT"
FT REPEAT 66..87
FT /note="LRR 1"
FT REPEAT 90..111
FT /note="LRR 2"
FT REPEAT 114..135
FT /note="LRR 3"
FT REPEAT 138..159
FT /note="LRR 4"
FT REPEAT 163..184
FT /note="LRR 5"
FT REPEAT 187..208
FT /note="LRR 6"
FT REPEAT 211..232
FT /note="LRR 7"
FT DOMAIN 252..298
FT /note="LRRCT"
FT DOMAIN 299..386
FT /note="Ig-like"
FT DOMAIN 424..520
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 397..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P244"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 321..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 764..766
FT /note="Missing: Loss of DLG1-, DLG3- and DLG4-binding."
FT /evidence="ECO:0000269|PubMed:16630835"
SQ SEQUENCE 766 AA; 81970 MW; D2A39C2449E8F62E CRC64;
MAPGPFSSGL LSPPPAALPF LLLLWAGASR GQPCPGRCIC QNVAPTLTML CAKTGLLFVP
PAIDRRVVEL RLTDNFIAAV RRRDFANMTS LVHLTLSRNT IGQVAAGAFA DLRALRALHL
DSNRLAEVRG DQLRGLGNLR HLILGNNQIR KVESAAFDAF LSTVEDLDLS YNNLEALPWE
AVGQMVNLNT LTLDHNLIDH IAEGTFVQLH KLVRLDMTSN RLHKLPPDGL FLRSQGGGPK
PPTPLTVSFG GNPLHCNCEL LWLRRLTRED DLETCATPEH LTDRYFWSIP EEEFLCEPPL
ITRQAGGRAL VVEGQAVSLR CRAVGDPEPV VHWVAPDGRL LGNSSRTRVR GDGTLDVTIT
TLRDSGTFTC IASNAAGEAT APVEVCVVPL PLMAPPPAAP PPLTEPGSSD IATPGRPGAN
DSATERRLVA AELTSSSVLI RWPAQRPVPG IRMYQVQYNS SADDSLVYRM IPSTSQTFLV
NDLAAGRAYD LCVLAVYDDG ATALPATRVV GCVQFTTAGD PAPCRPLRAH FLGGTMIIAI
GGVIVASVLV FIVLLMIRYK VYGDGDSRRI KGTSRSPPRV SHVCSQTNGS SAQQASAPPA
PDRYEALREV AVPAAIEAKA MEAEATSTEL EVVLGRSLGG SATSLCLLPS EETSGEESRA
VTGPRRSRSG ALGPPTSAPP TLALVRGGSP ARPRPQQRYS FDGDYGALFQ SHSYPRRARR
TKRHRSTPHL DGAGGGAAGE DGDLGLGSAR ARLAFTSTEW MLESTV
