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LRFN2_MACFA
ID   LRFN2_MACFA             Reviewed;         789 AA.
AC   Q9BE71;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 2;
DE   Flags: Precursor;
GN   Name=LRFN2; Synonyms=SALM1; ORFNames=QflA-11865;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Enhances
CC       the cell surface expression of 2 NMDA receptor subunits GRIN1 and
CC       GRIN2A. May play a role in redistributing DLG4 to the cell periphery
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms heteromeric complexes with LRFN1, LRFN3, LRFN4 and
CC       LRFN5. Can form homomeric complexes, but not across cell junctions.
CC       Interacts with 2 NMDA receptor subunits GRIN1 and GRIN2A. Interacts
CC       with DLG1, DLG2, DLG3 and DLG4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC       Synapse. Postsynaptic cell membrane {ECO:0000250}.
CC   -!- DOMAIN: The PDZ-binding motif is required for cell surface expression,
CC       neurite outgrowth promotion and interaction with DLG1, DLG3 and DLG4.
CC       {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR   EMBL; AB056799; BAB39323.1; -; mRNA.
DR   RefSeq; NP_001270797.1; NM_001283868.1.
DR   AlphaFoldDB; Q9BE71; -.
DR   SMR; Q9BE71; -.
DR   STRING; 9541.XP_005553145.1; -.
DR   GeneID; 102141033; -.
DR   CTD; 57497; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   OrthoDB; 151757at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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; 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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Leucine-rich repeat; Membrane; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..789
FT                   /note="Leucine-rich repeat and fibronectin type-III domain-
FT                   containing protein 2"
FT                   /id="PRO_0000014839"
FT   TOPO_DOM        21..534
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        535..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        556..789
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          21..52
FT                   /note="LRRNT"
FT   REPEAT          53..74
FT                   /note="LRR 1"
FT   REPEAT          77..98
FT                   /note="LRR 2"
FT   REPEAT          101..122
FT                   /note="LRR 3"
FT   REPEAT          125..146
FT                   /note="LRR 4"
FT   REPEAT          150..171
FT                   /note="LRR 5"
FT   REPEAT          174..195
FT                   /note="LRR 6"
FT   REPEAT          198..219
FT                   /note="LRR 7"
FT   DOMAIN          242..288
FT                   /note="LRRCT"
FT   DOMAIN          289..375
FT                   /note="Ig-like"
FT   DOMAIN          421..518
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          383..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           786..789
FT                   /note="PDZ-binding"
FT   COMPBIAS        383..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..598
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        310..359
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   789 AA;  84730 MW;  BB86DE81BC284B23 CRC64;
     METLLGGLLA FGMAFAVVDA CPKYCVCQNL SESLGTLCPS KGLLFVPPDI DRRTVELRLG
     GNFIIHISRQ DFANMTGLVD LTLSRNTISH IQPFSFLDLE SLRSLHLDSN RLPSLGEDTL
     RGLVNLQHLI VNNNQLGGIA DEAFEDFLLT LEDLDLSYNN LHGLPWDSVR RMVNLHQLSL
     DHNLLDHIAE GTFADLQKLA RLDLTSNRLQ KLPPDPIFAR SQASALTATP FAPPLSFSFG
     GNPLHCNCEL LWLRRLERDD DLETCGSPGG LKGRYFWHVR EEEFVCEPPL ITQHTHKLLV
     LEGQAATLKC KAIGDPSPLI HWVAPDDRLV GNSSRTAVYD NGTLDIFITT SQDSGAFTCI
     AANAAGEATA TVEVSIVQLP HLSNSTSRTA PPKSRLSDIT GSSKTSRGGG GSGGGEPPKS
     PPERAVLVSE VTTTSALAKW SVSKSTPRVK MYQLQYNCSD DEVLIYRMIP ASNKAFVVNN
     LVSGTGYDLC VLAMWDDTAT TLTATNIVGC AQFFTKADYP QCQSMHSQIL GGTMILVIGG
     IIVATLLVFI VILMVRYKVC NHEAPSKMAA AVSNVYSQTN GAQPPPPSSA PAGAPPQGPP
     KVVVRNELLD FTASLARASD SSSSSSLGSG EAAGLGRAPW RLPPSAPRPK PSLDRLMGAF
     ASLDLKSQRK EELLDSRTPA GRGAGTSARG HHSDREPLLG PPAARARSLL PLPLEGKAKR
     SHSFDMGDFA AAAAGGVVPG GYSPPRRVSN IWTKRSLSVN GMLLPFEESD LVGARGTFGS
     SEWVMESTV
 
 
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