ID A0A452G0X9_CAPHI Unreviewed; 1108 AA.
AC A0A452G0X9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=IQ motif and Sec7 domain ArfGEF 1 {ECO:0000313|Ensembl:ENSCHIP00000030273.1};
GN Name=IQSEC1 {ECO:0000313|Ensembl:ENSCHIP00000030273.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000030273.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000030273.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000030273.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the BRAG family.
CC {ECO:0000256|ARBA:ARBA00006248}.
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DR EMBL; LWLT01000024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017922701.1; XM_018067212.1.
DR AlphaFoldDB; A0A452G0X9; -.
DR Ensembl; ENSCHIT00000038144.1; ENSCHIP00000030273.1; ENSCHIG00000025033.1.
DR GeneID; 102172773; -.
DR KEGG; chx:102172773; -.
DR CTD; 9922; -.
DR GeneTree; ENSGT00940000156915; -.
DR OrthoDB; 204547at2759; -.
DR Proteomes; UP000291000; Chromosome 22.
DR Bgee; ENSCHIG00000025033; Expressed in prefrontal cortex and 16 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd13318; PH_IQSEC; 1.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.220.20; -; 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; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR033742; IQSEC_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
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:SF327; IQ MOTIF AND SEC7 DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF16453; IQ_SEC7_PH; 1.
DR Pfam; PF01369; Sec7; 1.
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; PS50096; IQ; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT DOMAIN 511..704
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 21..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1058
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 122106 MW; B57B12918345643D CRC64;
MWCLHCNSER TQSLLELELD SGVEGEAPSS EPGTSLDSPS AYHQGPLAPG SGLSPEPYEH
APGGAYGLYA GPPGQQQRAR RPRLQHSTSI LRKQAEEEAI KRSRSLSESY ELSSDLQDKQ
VEMLERKYGG RLVTRHAART IQTAFRQYQM NKNFERLRSS MSEKRLSRRI VLSNMRVQLS
FEGPEKAHSS FFEGKQVSVT DGDSPLGSLG PAECGDLGPP PPPALQAPAP AGDFADAITE
LEDAFSRQVK SLAESIDDAL NCRSLHAVEG APAPAAEPSS GLHGAAEQRR LDEMTASYSD
VTLYIDEDEL SPPPPAVQAG CRPSSGESDL RLRAGAAAQD YWALAHKDDQ GDTDTSCRST
PSLEPRARVE HLPLLTIEPP SDSSADLSDR SDRSSLKRQG AYERGLGGPQ GSPKHGPHGP
PRGLPREEPE PRARPPRPLD AHLAINGSAN RQSKSESDYS DGDNDSLNST SNSNDTINCS
SESSSRDSLR EQTLSKQTYH KEARNSWDSP AFSNDVIRKR HYRIGLNLFN KKPEKGVQYL
IERGFVPDTP VGVAHFLLQR KGLSRQMIGE FLGNRQKQFN RDVLDCVVDE MDFSAMELDE
ALRKFQAHIR VQGEAQKVER LIEAFSQRYC ICNPGVVRQF RNPDTIFILA FAIILLNTDM
YSPNVKPERK MKLEDFVKNL RGVDDGEDIP REMLVGIYER IRKRELKTNE DHVSQVQKVE
KLIVGKKPIG SLHHGLGCVL SLPHRRLVCY CRLFEVPDPN KPQKLGLHQR EIFLFNDLLV
VTKIFQKKKN SVTYSFRQSF SLYGMQVLLF ENQYYPNGIR LTSAVPGADI KVLINFNAPN
PQDRKKFTDD LRESIAEAQE MEKHRIEAEL EKQKGVVRPS MSQCPSLKKE SGGGTLSRAC
LDDSYAGGEG LKRSALSSSL RDLSEAGKRG RRSSAGSLES NVEGSIISSP HMRRRAASTR
DCPPRPHQAM PSSSSLLGSL FGSKRGKPPP QAHLPPAPPP PHPAAGHPQG PVEGPLSGPV
HGHHAQYCHL QQNPPPYHHH HHHHPPQHFQ HAHQCHHGPH GGHPAYGAHA HGHPPLPAGH
AAHHHGQPPA PPPPTSSKAK PSGISTIV
//
