ID A0A2Y9NJ56_DELLE Unreviewed; 1061 AA.
AC A0A2Y9NJ56;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=IQ motif and SEC7 domain-containing protein 3 isoform X3 {ECO:0000313|RefSeq:XP_022432966.1, ECO:0000313|RefSeq:XP_022432967.1};
GN Name=IQSEC3 {ECO:0000313|RefSeq:XP_022432966.1,
GN ECO:0000313|RefSeq:XP_022432967.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022432966.1};
RN [1] {ECO:0000313|RefSeq:XP_022432966.1, ECO:0000313|RefSeq:XP_022432967.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022432966.1,
RC ECO:0000313|RefSeq:XP_022432967.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the BRAG family.
CC {ECO:0000256|ARBA:ARBA00006248}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022432966.1; XM_022577258.2.
DR RefSeq; XP_022432967.1; XM_022577259.2.
DR Proteomes; UP000248483; Unplaced.
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; cd14686; bZIP; 1.
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; 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:SF318; IQ MOTIF AND SEC7 DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF16453; IQ_SEC7_PH; 1.
DR Pfam; PF01369; Sec7; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 643..836
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 63..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..56
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 64..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 114276 MW; EBFFF86C5EE8D37C CRC64;
MESLLENPVR AVLYLKELTA IVQNQQSLIH TQRQRIDELE RRLDELSAEN RSLWEHQQLL
QAVPPPGLVP PSPAPLPATP ATAASGAQEQ LRDHGQLPPT APEKPPLQHH GQLLAQPQAG
PSGRAHASQP PHHHPAGPGA VADKEKERPP SCCAAAGTLL QHKSPAALGK GVLSRRPENE
TVLHQFCCPA ADAEQKPACS DLASQSDGSC AQAGAGTEDS VAAAAAAAAG RPSAHAPKAQ
AQELQEEEKR PGAGGASPRA GLHCAASPSR QQPVPAAALC ARAPAASDYE LSLDLKNKQI
EMLEHKYGGH LVSRRAACTI QTAFRQYQLS KNFEKIRNSL LESRLPRRIS LRKARAPTAE
SLAAERALLE GCGLSGLPLA RSPSLPPTIA GTLTELEDSF TEQVQSLAKS IDDALSTWSL
KTVCSLQESG AYQVHRALRA GTGPPGLETE AREPEGAHSG DWAEPTEPAG PPQGHGSTLM
MAFRDVTVQI ASRNISVSSS TALSVANCLG APTASAPAES AAGKAEQDEA GGQEAPEAPS
AGQEDVPAED ASAEAGPDGA LRASPPGAAV PAAEEEEDGE EEAEEAGKGA EAEAGDSSEQ
LSSSSASAKS AASASASKEA LQAMILSLPR YHCENPASCK SPTLSTDTLR KRLYRIGLNL
FNINPDKGIQ FLISRGFIPD TPIGVAHFLL QRKGLSRQMI GEFLGNSKKQ FNRDVLDCVV
DEMDFSAMEL DEALRKFQAH IRVQGEAQKV ERLIETFSQR YCMCNPEVVR QFHNPDTVFI
LAFAVILLNT DMYSPNIKPD RKMMLEDFIR NLRGVDDGAD IPRELVVGIY ERIQQKELKS
NEDHVTYVTK VEKSIVGMKT VLSEPHRRLV CCSRLFEVTD VNKLQKQAAH QREVFLFNDL
LVILKLCPKK KSSSTYTFCK SVGLLGMQFH LFENEYYSHG ITLVTPLSGS EKKQVLHFCA
LGLDEMRKFV EDLKESIAEV TELEQIRIEW ELEKQQGTKT LSFKAGGAQV EPQSKQGSPT
AKRGAAPAEK AVESTAEVLI NASPARLTIL PISRDTIKSY C
//
