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Database: UniProt
Entry: A0A3B5RBV9_XIPMA
LinkDB: A0A3B5RBV9_XIPMA
Original site: A0A3B5RBV9_XIPMA 
ID   A0A3B5RBV9_XIPMA        Unreviewed;      1232 AA.
AC   A0A3B5RBV9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=IQ motif and SEC7 domain-containing protein 1-like {ECO:0000313|Ensembl:ENSXMAP00000041278.1};
GN   Name=IQSEC1 {ECO:0000313|Ensembl:ENSXMAP00000041278.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000041278.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000041278.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000041278.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the BRAG family.
CC       {ECO:0000256|ARBA:ARBA00006248}.
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DR   AlphaFoldDB; A0A3B5RBV9; -.
DR   STRING; 8083.ENSXMAP00000041278; -.
DR   Ensembl; ENSXMAT00000023718.1; ENSXMAP00000041278.1; ENSXMAG00000007488.2.
DR   GeneTree; ENSGT00940000156915; -.
DR   InParanoid; A0A3B5RBV9; -.
DR   OMA; AGHSAHH; -.
DR   OrthoDB; 204547at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0001946; P:lymphangiogenesis; IEA:Ensembl.
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; 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:SF398; IQ MOTIF AND SEC7 DOMAIN-CONTAINING PROTEIN 1-LIKE; 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:UP000002852}.
FT   DOMAIN          624..817
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   REGION          365..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..65
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        427..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1013
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1118
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1217..1232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1232 AA;  138914 MW;  2D21CA605DE426FC CRC64;
     MDGQRILAEM ENPTENPSKA AEYLQELNNI IETQQVLLEK QRIRIEELEL QVTDLCKENA
     CLKDQHRRHL TTCGLAQGNP GTLGGIEENV VQEKRHASLP ARVFEIHQNV FDPLCRTSYP
     CLKWKSASFG VEGDAPGSDV SVSVDPCVIY GCKPVTHGGR PGLDYLDSQL YGHIFLPSHV
     RPRRPKLQHS QSILRKHAEE EAIKRSRSMS ESYELSSDLQ DKQVEMLERK YGGRFITRHA
     ARTIQTAFRQ YQMNKNFERL RSSMSENRMS RRIVLSNMRM QLSFEGPEKV HSSYFEGKHL
     SLSDEGANIG ALVQSEHGRE RGVQMKIPST QSDLTYAVTE LEDAFSRQVK SLAESIDDAL
     NCRSLHGEDS TSEQGRSHPD TDRELSRQLE SSHSPSDHRK LDEMTASYSD VTLYIDEEEL
     SPPLPLSQSV DRPSSTESDL RQRSLNSSQD YWSLAHKDEK GDTDTSCRST PSLECQEQRL
     RVDHLPLLTI EPPSDSSVEL SDRSDRSSLK RQSTYDRSPS NQQSSPKHIG HGLPPRGPSR
     EEDPSRHCAR QLEAHLAING TPNRQSKSES DFSDGDNDSI NSTSNSNDTI NCSSESSSRD
     SLREQTLSKQ TYHKETRNSW DSPAFSNDII RKRHYRIGLN LFNKKPEKGI QYLIERSYVP
     DTPVGVAHFL LQRKGLSRQM IGEFLGNRQK QFNRDVLDCV VDEMDFSGLE LDEGLRKFQA
     HIRVQGEAQK VERLIEAYSQ RYCICNPGVV RQFRNPDTIF ILAFAIILLN TDMYSPNVKP
     ERKMKLEDFV KNLRGVDDGE DIPREMLVGI YERIRKRELR TNEDHVSQVQ KVEKLIVGKK
     PIGSLHQGLG CVLSLPHRRL VCYCRLFEVP DPNKLQKLGL HQREIFLFND LLVVTKIFQK
     KKNSVTYSFR QSFSLYSMQV LLFENQYYPN GLRLTSAIPG ADIKVLINFN APNPQDRKRF
     TDDLRESIAE VQEMEKYRIE TELEKQKGLV RPSMSQCSGL KKETGNGNLS RASLDDSYAI
     GEGLKRSALS SSLRDLSDAG KRGRRSSAGS LDSNLEGSII SSPHMRRRTP SGRDCASRHS
     GHSLPSSSSL LGSLFGTRRV RSPGPCPGPV PQSPHPTLIS HAPHPANLHH AARAESDSSV
     PVHPHPVPFC HVTQNPPPYH HHHHYHPPPH LQRAPHQCHA PPSHSQHPPY PQHSHGSHSA
     HGGHLHGPPP TPASQVPSSS TKPKHSGIST VV
//
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