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Database: UniProt
Entry: A0A3L8SKB3_CHLGU
LinkDB: A0A3L8SKB3_CHLGU
Original site: A0A3L8SKB3_CHLGU 
ID   A0A3L8SKB3_CHLGU        Unreviewed;       828 AA.
AC   A0A3L8SKB3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DV515_00007013 {ECO:0000313|EMBL:RLW03028.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW03028.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW03028.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW03028.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW03028.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
CC       {ECO:0000256|ARBA:ARBA00004632}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLW03028.1}.
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DR   EMBL; QUSF01000017; RLW03028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SKB3; -.
DR   STRING; 44316.ENSEGOP00005017306; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   CDD; cd13295; PH_EFA6; 1.
DR   CDD; cd00171; Sec7; 1.
DR   Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041681; PH_9.
DR   InterPro; IPR001605; PH_dom-spectrin-type.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR10663:SF329; PH AND SEC7 DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF15410; PH_9; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48425; Sec7 domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT   DOMAIN          351..518
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          568..681
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          709..736
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        16..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  91623 MW;  4B44B5933A98A806 CRC64;
     MSESSPLPWS AACESEPHSP RSQPSPLAGS DGDEQPSQPA EPASGRASPR HDAQPSREEG
     EQRDEHLEAV TEPGERLSER GQGPGAGGQS GRADGAGLPN GVDAAPAAGP ERPQDGDGAG
     RSSPQPGDNR GSPGPQAASG ALSKQRWHSV LGSSEALSAD EAEEQFGFAS GDVKLSCSDD
     DREHFQFKDI RDGFSSTFEK IVESDLMKGT YYSSLDSLDV LSLTDETDSC VSFEAPLTPL
     IQQRAKESPE LLEQKLAAQQ REALHHMAAD KQEQAAAKPV EGDFGSPLRH SITSSRSENV
     LSRLSLKSIP NGFHVEGSEE DATKIINSIS DASLKDTLSD SDSDMGSTEQ LDQGSTDTLA
     NGCRADSEAA KRLAKRLYNL EGFKRCDVAR QLGKNNEFSK LVAEEYLSFF DFTGLTLDKA
     LRTFLKAFPL MGETQERERV LIHFSRRYCQ CNPEESTSED GIHTLTCALM LLNTDLHGHN
     IGKKMSCQQF IANLDGLNDG KDFAKDLLKT LYNSIKNEKL EWAIDEDELR KSLSELVDDK
     FGASAKKVTR IVDSSNPFLD IPQALNAVTY KHGVLTRKTH ADMDGKRTPR GRRGWKKFYA
     VLKGTVLYLQ KDEYKPDKDL SEVDLKNAIR VHHALATKAS DYSKKSNVLK LKTADWRVFL
     FQAPSKEEML SWILRINLVA AIFSAPAFPA AICSMKKFCR PLLPSSMTKL CQEEQLRSHE
     NKMKQIADEL AEHKLHPVEK SLKSKEAEEY RLKEHYLIFE KSRYETYINL LCMKIKVGTD
     DLERIETSFF KVEADDIALR KTHSSPSLSQ GHMSISCKAE KDILEQNT
//
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