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Database: UniProt
Entry: A0A6I9HFR7_GEOFO
LinkDB: A0A6I9HFR7_GEOFO
Original site: A0A6I9HFR7_GEOFO 
ID   A0A6I9HFR7_GEOFO        Unreviewed;       796 AA.
AC   A0A6I9HFR7;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   28-JAN-2026, entry version 25.
DE   SubName: Full=Protein ELFN1 {ECO:0000313|RefSeq:XP_005420411.1, ECO:0000313|RefSeq:XP_030912438.1};
GN   Name=ELFN1 {ECO:0000313|RefSeq:XP_005420411.1,
GN   ECO:0000313|RefSeq:XP_030912438.1};
OS   Geospiza fortis (Medium ground-finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Thraupidae; Geospiza.
OX   NCBI_TaxID=48883 {ECO:0000313|Proteomes:UP000504602, ECO:0000313|RefSeq:XP_005420411.1};
RN   [1] {ECO:0000313|RefSeq:XP_005420411.1, ECO:0000313|RefSeq:XP_030912438.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (APR-2025) to UniProtKB.
CC   -!- SUBUNIT: Interacts with PPP1CA. {ECO:0000256|ARBA:ARBA00065735}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   RefSeq; XP_005420411.1; XM_005420354.2.
DR   RefSeq; XP_030912438.1; XM_031056578.1.
DR   AlphaFoldDB; A0A6I9HFR7; -.
DR   GeneID; 102043781; -.
DR   KEGG; gfr:102043781; -.
DR   CTD; 392617; -.
DR   GeneTree; ENSGT00940000161391; -.
DR   OrthoDB; 676979at2759; -.
DR   Proteomes; UP000504602; Unplaced.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR   GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR   FunFam; 3.80.10.10:FF:000047; protein phosphatase 1 regulatory subunit 29; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR055106; ELFN_Fn3.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR050541; LRR_TM_domain-containing.
DR   PANTHER; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR24369:SF204; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 29-RELATED; 1.
DR   Pfam; PF22986; Fn3_ELFN; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein phosphatase inhibitor {ECO:0000256|ARBA:ARBA00023272};
KW   Reference proteome {ECO:0000313|Proteomes:UP000504602};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..796
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5044634668"
FT   TRANSMEM        407..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          192..239
FT                   /note="LRRCT"
FT                   /evidence="ECO:0000259|SMART:SM00082"
FT   REGION          609..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..633
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   796 AA;  89645 MW;  B87565E2B33E9190 CRC64;
     MAGRRWAATS ALCMCVAAVS LLHAGGVRAD CWLIEGDKGF VWLAICSQNQ PPYESIPQQI
     NSTIVDLRLN DNKIKSVQYA SLSRFGNLTY LNLTKNEISY IEDGAFSGQF NLQVLQLGYN
     RLRNLTEGIL RGLGKLEYLY LQANLIETVT PNAFWECPNI VNIDLSMNRI QRLDSNTFRG
     LNKLSVCELY SNPFYCSCEL LGFLQWLEAF TNMTRTYDRM QCDSPPDYMG YYLLGQGRTG
     YRNALSMLSS LCTGGSYTVI PRFIPPRYQV TTVPSESPCS EEECSSGDGT TPQFSLFTPI
     GETEVRPNIQ VKHLNHNSAV LTVQIPYPFS KMYILSQFEN GFSSMITKLR KKEENITVSN
     LVAQRDYTYC VVSVHQYSKY NHTCVTITPT RPNRKEPVPT PSTATHYIMT ILGCLFGMVI
     VLGVVYYCLR KRRQQEEKHK KAAGSMKKTI IELKYGPEME TTSITQLSQG QILGGETVTR
     IPYLPSAGEV EQYKLIESSE TPKATKGNYM EVRTGEQPER RDCELSLPPD TQGSVAEIST
     IAKEVDKVNQ IINNCIDALK SESTSFQGVK SGAVSTVEPQ LVLLSEQIPS KHGFLSPVYK
     ESYNHPLQRP HSMEAAPKRS STSSSGSIRS PRSYRSEGSG HKSEAKYIEK TSPTTDTILT
     VTPAAAILRA EAEKIRQYSE HRHSYPSSHP GEQHDSMGGR KPSILEPLTR PRPRDLAYSQ
     LSPQYHNLSY TSSPEYTCKP SHSIWERFKL NRKRHKDEEE YMAAGHALRK KVQFAKDEDL
     HDILDYWKGV SAQQKS
//
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