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Database: UniProt
Entry: U3K8H3_FICAL
LinkDB: U3K8H3_FICAL
Original site: U3K8H3_FICAL 
ID   U3K8H3_FICAL            Unreviewed;       763 AA.
AC   U3K8H3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Leucine rich repeat and fibronectin type III domain containing 2 {ECO:0000313|Ensembl:ENSFALP00000011327.1};
GN   Name=LRFN2 {ECO:0000313|Ensembl:ENSFALP00000011327.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000011327.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000011327.1, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000011327.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_005043281.1; XM_005043224.1.
DR   AlphaFoldDB; U3K8H3; -.
DR   STRING; 59894.ENSFALP00000011327; -.
DR   Ensembl; ENSFALT00000011372.2; ENSFALP00000011327.1; ENSFALG00000010855.2.
DR   GeneID; 101810930; -.
DR   KEGG; fab:101810930; -.
DR   CTD; 57497; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000156417; -.
DR   HOGENOM; CLU_016998_1_0_1; -.
DR   OMA; ELMDFSA; -.
DR   OrthoDB; 2942402at2759; -.
DR   Proteomes; UP000016665; Chromosome 3.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR   CDD; cd00063; FN3; 1.
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; 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   PANTHER; PTHR45842:SF6; LEUCINE-RICH REPEAT AND FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00060; FN3; 1.
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.
DR   PROSITE; PS51450; LRR; 3.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..763
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004646219"
FT   TRANSMEM        520..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          288..374
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          412..509
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          383..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  84718 MW;  D501001D61F56141 CRC64;
     MEKLLCGILV FGMAVTVNAC PKYCVCQNLS ESLGTLCPSK GLLFVPLDID RRTVELRLGG
     NFIINISRQD FANMSGLVDL TLSRNTISYI QPYSFTDLES LRSLHLDSNR LPEIEEDTLR
     GLINLQHLIL NNNQLSSISD DAFEDFLLTL EDLDLSYNNL RSIPWESIRK MINLHQLSLD
     HNLIDYITEG TFADLQKLAR LDLTSNRLQK LPPDPIFARS QVIPLVVTPF SPPLSLSFGG
     NPLHCNCELL WLRRLDRDDD METCASPPSL KGRYFWYIRE EEFVCEPPLI TQHTHKLLVL
     EGQTATLKCK AIGDPTPIIH WVAPDDRLIG NSSRTAVYDN GTLDIHITTS KDYGTFTCIA
     ANAAGESTAT IELSIVQLPH LSNGTGKAAP PKSRLSDITS STKSNRGETK GPPERAVLVS
     DVTTTSALVK WTVSKSAPRV KMYQLQYNCS DDEVLIYRMI PATNKAFVVT NLVSGTGYDL
     CVLAMWDDTA TTLTATNIVG CAQFFTKEDY PQCQSMHSQF LGGTMILIIG GIIVATLLVF
     IVILMVRYKV CSNSQGKMSN VSNVYSQTNG AQPVQNGVLP QVNPKVVVRN ELMEFNCQSA
     RSSISSSSSS ANSRDCDNYS LQSEQGTLSS KWRPPSRSKH NIDRLMGAFA SLELKCQKKE
     EMTDSRTSTV ARHSDKEPLL GQTESKFRSF LMLPLEGKTK RSHSFDMGDF ATSQCCTYPK
     KITNIWTKRS LSVNGMLLQY DDSDLTGAKG TFGSSEWVME STV
//
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