Full text data of IQSEC1
IQSEC1
(ARFGEP100, BRAG2, KIAA0763)
[Confidence: low (only semi-automatic identification from reviews)]
IQ motif and SEC7 domain-containing protein 1 (ADP-ribosylation factors guanine nucleotide-exchange protein 100; ADP-ribosylation factors guanine nucleotide-exchange protein 2; Brefeldin-resistant Arf-GEF 2 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
IQ motif and SEC7 domain-containing protein 1 (ADP-ribosylation factors guanine nucleotide-exchange protein 100; ADP-ribosylation factors guanine nucleotide-exchange protein 2; Brefeldin-resistant Arf-GEF 2 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6DN90
ID IQEC1_HUMAN Reviewed; 963 AA.
AC Q6DN90; O94863; Q96D85;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 1;
DE AltName: Full=ADP-ribosylation factors guanine nucleotide-exchange protein 100;
DE AltName: Full=ADP-ribosylation factors guanine nucleotide-exchange protein 2;
DE AltName: Full=Brefeldin-resistant Arf-GEF 2 protein;
GN Name=IQSEC1; Synonyms=ARFGEP100, BRAG2, KIAA0763;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=16461286; DOI=10.1016/j.cub.2005.12.032;
RA Dunphy J.L., Moravec R., Ly K., Lasell T.K., Melancon P.,
RA Casanova J.E.;
RT "The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling
RT endocytosis of beta1 integrins.";
RL Curr. Biol. 16:315-320(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-936 (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION
RP WITH ARF6.
RX PubMed=11226253; DOI=10.1073/pnas.051634798;
RA Someya A., Sata M., Takeda K., Pacheco-Rodriguez G., Ferrans V.J.,
RA Moss J., Vaughan M.;
RT "ARF-GEP(100), a guanine nucleotide-exchange protein for ADP-
RT ribosylation factor 6.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2413-2418(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-512, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: In addition to accelerate GTP gamma S binding by ARFs of
CC all three classes, it appears to function preferentially as a
CC guanine nucleotide exchange protein for ARF6, mediating
CC internalisation of beta-1 integrin.
CC -!- SUBUNIT: Interacts with ARF6.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=At steady state,
CC may be preferentially cytosolic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BRAG2b;
CC IsoId=Q6DN90-1; Sequence=Displayed;
CC Name=2; Synonyms=BRAG2a;
CC IsoId=Q6DN90-2; Sequence=VSP_019758;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in brain, ovary, heart, lung, liver,
CC kidney and leukocytes. Moderate expression was also detected in
CC lung, skeletal muscle, placenta, small intestine, pancreas, spleen
CC and testis.
CC -!- SIMILARITY: Belongs to the BRAG family.
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 SEC7 domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY653734; AAT72063.1; -; mRNA.
DR EMBL; AB018306; BAA34483.2; -; mRNA.
DR EMBL; BC010267; AAH10267.1; -; mRNA.
DR RefSeq; NP_001127854.1; NM_001134382.2.
DR RefSeq; NP_055684.3; NM_014869.5.
DR UniGene; Hs.475506; -.
DR PDB; 3QWM; X-ray; 2.39 A; A=743-880.
DR PDB; 4C0A; X-ray; 3.30 A; A/B/E/F=512-885.
DR PDBsum; 3QWM; -.
DR PDBsum; 4C0A; -.
DR ProteinModelPortal; Q6DN90; -.
DR SMR; Q6DN90; 531-712, 750-879.
DR IntAct; Q6DN90; 6.
DR STRING; 9606.ENSP00000273221; -.
DR DMDM; 74748429; -.
DR PaxDb; Q6DN90; -.
DR PRIDE; Q6DN90; -.
DR DNASU; 9922; -.
DR Ensembl; ENST00000273221; ENSP00000273221; ENSG00000144711.
DR GeneID; 9922; -.
DR KEGG; hsa:9922; -.
DR UCSC; uc003bxt.3; human.
DR CTD; 9922; -.
DR GeneCards; GC03M012938; -.
DR HGNC; HGNC:29112; IQSEC1.
DR HPA; HPA038143; -.
DR MIM; 610166; gene.
DR neXtProt; NX_Q6DN90; -.
DR PharmGKB; PA128394566; -.
DR eggNOG; COG5307; -.
DR HOGENOM; HOG000113099; -.
DR HOVERGEN; HBG056324; -.
DR InParanoid; Q6DN90; -.
DR KO; K12495; -.
DR PhylomeDB; Q6DN90; -.
DR ChiTaRS; IQSEC1; human.
DR GeneWiki; IQSEC1; -.
DR GenomeRNAi; 9922; -.
DR NextBio; 37432; -.
DR PRO; PR:Q6DN90; -.
DR ArrayExpress; Q6DN90; -.
DR Bgee; Q6DN90; -.
DR CleanEx; HS_IQSEC1; -.
DR Genevestigator; Q6DN90; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:RefGenome.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:RefGenome.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR023394; Sec7_alpha_orthog.
DR InterPro; IPR000904; Sec7_dom.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Guanine-nucleotide releasing factor; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 963 IQ motif and SEC7 domain-containing
FT protein 1.
FT /FTId=PRO_0000245606.
FT DOMAIN 134 163 IQ.
FT DOMAIN 517 710 SEC7.
FT DOMAIN 774 866 PH.
FT COILED 848 879 Potential.
FT MOD_RES 180 180 Phosphoserine.
FT MOD_RES 512 512 Phosphoserine.
FT MOD_RES 515 515 Phosphoserine (By similarity).
FT VAR_SEQ 1 122 Missing (in isoform 2).
FT /FTId=VSP_019758.
FT VARIANT 640 640 P -> S (in dbSNP:rs35319679).
FT /FTId=VAR_051927.
FT VARIANT 882 882 V -> I (in dbSNP:rs17541405).
FT /FTId=VAR_027004.
FT CONFLICT 934 936 KRG -> VHH (in Ref. 3).
FT HELIX 522 537
FT HELIX 539 548
FT HELIX 556 565
FT HELIX 571 578
FT HELIX 584 595
FT HELIX 604 614
FT HELIX 621 638
FT HELIX 640 646
FT HELIX 650 667
FT TURN 669 671
FT STRAND 673 676
FT HELIX 679 685
FT TURN 686 689
FT HELIX 697 709
FT HELIX 718 728
FT STRAND 753 761
FT TURN 771 774
FT STRAND 775 783
FT STRAND 785 789
FT STRAND 803 806
FT STRAND 811 816
FT STRAND 824 829
FT STRAND 832 834
FT STRAND 837 843
FT HELIX 847 878
SQ SEQUENCE 963 AA; 108314 MW; 5B31F9918F9CFF11 CRC64;
MWCLHCNSER TQSLLELELD SGVEGEAPSS ETGTSLDSPS AYPQGPLVPG SSLSPDHYEH
TSVGAYGLYS GPPGQQQRTR RPKLQHSTSI LRKQAEEEAI KRSRSLSESY ELSSDLQDKQ
VEMLERKYGG RLVTRHAART IQTAFRQYQM NKNFERLRSS MSENRMSRRI VLSNMRMQFS
FEGPEKVHSS YFEGKQVSVT NDGSQLGALV SPECGDLSEP TTLKSPAPSS DFADAITELE
DAFSRQVKSL AESIDDALNC RSLHTEEAPA LDAARARDTE PQTALHGMDH RKLDEMTASY
SDVTLYIDEE ELSPPLPLSQ AGDRPSSTES DLRLRAGGAA PDYWALAHKE DKADTDTSCR
STPSLERQEQ RLRVEHLPLL TIEPPSDSSV DLSDRSERGS LKRQSAYERS LGGQQGSPKH
GPHSGAPKSL PREEPELRPR PPRPLDSHLA INGSANRQSK SESDYSDGDN DSINSTSNSN
DTINCSSESS SRDSLREQTL SKQTYHKEAR NSWDSPAFSN DVIRKRHYRI GLNLFNKKPE
KGVQYLIERG FVPDTPVGVA HFLLQRKGLS RQMIGEFLGN RQKQFNRDVL DCVVDEMDFS
TMELDEALRK FQAHIRVQGE AQKVERLIEA FSQRYCICNP GVVRQFRNPD TIFILAFAII
LLNTDMYSPN VKPERKMKLE DFIKNLRGVD DGEDIPREML MGIYERIRKR ELKTNEDHVS
QVQKVEKLIV GKKPIGSLHP GLGCVLSLPH RRLVCYCRLF EVPDPNKPQK LGLHQREIFL
FNDLLVVTKI FQKKKNSVTY SFRQSFSLYG MQVLLFENQY YPNGIRLTSS VPGADIKVLI
NFNAPNPQDR KKFTDDLRES IAEVQEMEKH RIESELEKQK GVVRPSMSQC SSLKKESGNG
TLSRACLDDS YASGEGLKRS ALSSSLRDLS EAGKRGRRSS AGSLESNVEF QPFEPLQPSV
LCS
//
ID IQEC1_HUMAN Reviewed; 963 AA.
AC Q6DN90; O94863; Q96D85;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 1;
DE AltName: Full=ADP-ribosylation factors guanine nucleotide-exchange protein 100;
DE AltName: Full=ADP-ribosylation factors guanine nucleotide-exchange protein 2;
DE AltName: Full=Brefeldin-resistant Arf-GEF 2 protein;
GN Name=IQSEC1; Synonyms=ARFGEP100, BRAG2, KIAA0763;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=16461286; DOI=10.1016/j.cub.2005.12.032;
RA Dunphy J.L., Moravec R., Ly K., Lasell T.K., Melancon P.,
RA Casanova J.E.;
RT "The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling
RT endocytosis of beta1 integrins.";
RL Curr. Biol. 16:315-320(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-936 (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION
RP WITH ARF6.
RX PubMed=11226253; DOI=10.1073/pnas.051634798;
RA Someya A., Sata M., Takeda K., Pacheco-Rodriguez G., Ferrans V.J.,
RA Moss J., Vaughan M.;
RT "ARF-GEP(100), a guanine nucleotide-exchange protein for ADP-
RT ribosylation factor 6.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2413-2418(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-512, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: In addition to accelerate GTP gamma S binding by ARFs of
CC all three classes, it appears to function preferentially as a
CC guanine nucleotide exchange protein for ARF6, mediating
CC internalisation of beta-1 integrin.
CC -!- SUBUNIT: Interacts with ARF6.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=At steady state,
CC may be preferentially cytosolic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BRAG2b;
CC IsoId=Q6DN90-1; Sequence=Displayed;
CC Name=2; Synonyms=BRAG2a;
CC IsoId=Q6DN90-2; Sequence=VSP_019758;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in brain, ovary, heart, lung, liver,
CC kidney and leukocytes. Moderate expression was also detected in
CC lung, skeletal muscle, placenta, small intestine, pancreas, spleen
CC and testis.
CC -!- SIMILARITY: Belongs to the BRAG family.
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 SEC7 domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY653734; AAT72063.1; -; mRNA.
DR EMBL; AB018306; BAA34483.2; -; mRNA.
DR EMBL; BC010267; AAH10267.1; -; mRNA.
DR RefSeq; NP_001127854.1; NM_001134382.2.
DR RefSeq; NP_055684.3; NM_014869.5.
DR UniGene; Hs.475506; -.
DR PDB; 3QWM; X-ray; 2.39 A; A=743-880.
DR PDB; 4C0A; X-ray; 3.30 A; A/B/E/F=512-885.
DR PDBsum; 3QWM; -.
DR PDBsum; 4C0A; -.
DR ProteinModelPortal; Q6DN90; -.
DR SMR; Q6DN90; 531-712, 750-879.
DR IntAct; Q6DN90; 6.
DR STRING; 9606.ENSP00000273221; -.
DR DMDM; 74748429; -.
DR PaxDb; Q6DN90; -.
DR PRIDE; Q6DN90; -.
DR DNASU; 9922; -.
DR Ensembl; ENST00000273221; ENSP00000273221; ENSG00000144711.
DR GeneID; 9922; -.
DR KEGG; hsa:9922; -.
DR UCSC; uc003bxt.3; human.
DR CTD; 9922; -.
DR GeneCards; GC03M012938; -.
DR HGNC; HGNC:29112; IQSEC1.
DR HPA; HPA038143; -.
DR MIM; 610166; gene.
DR neXtProt; NX_Q6DN90; -.
DR PharmGKB; PA128394566; -.
DR eggNOG; COG5307; -.
DR HOGENOM; HOG000113099; -.
DR HOVERGEN; HBG056324; -.
DR InParanoid; Q6DN90; -.
DR KO; K12495; -.
DR PhylomeDB; Q6DN90; -.
DR ChiTaRS; IQSEC1; human.
DR GeneWiki; IQSEC1; -.
DR GenomeRNAi; 9922; -.
DR NextBio; 37432; -.
DR PRO; PR:Q6DN90; -.
DR ArrayExpress; Q6DN90; -.
DR Bgee; Q6DN90; -.
DR CleanEx; HS_IQSEC1; -.
DR Genevestigator; Q6DN90; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:RefGenome.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:RefGenome.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR023394; Sec7_alpha_orthog.
DR InterPro; IPR000904; Sec7_dom.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Guanine-nucleotide releasing factor; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 963 IQ motif and SEC7 domain-containing
FT protein 1.
FT /FTId=PRO_0000245606.
FT DOMAIN 134 163 IQ.
FT DOMAIN 517 710 SEC7.
FT DOMAIN 774 866 PH.
FT COILED 848 879 Potential.
FT MOD_RES 180 180 Phosphoserine.
FT MOD_RES 512 512 Phosphoserine.
FT MOD_RES 515 515 Phosphoserine (By similarity).
FT VAR_SEQ 1 122 Missing (in isoform 2).
FT /FTId=VSP_019758.
FT VARIANT 640 640 P -> S (in dbSNP:rs35319679).
FT /FTId=VAR_051927.
FT VARIANT 882 882 V -> I (in dbSNP:rs17541405).
FT /FTId=VAR_027004.
FT CONFLICT 934 936 KRG -> VHH (in Ref. 3).
FT HELIX 522 537
FT HELIX 539 548
FT HELIX 556 565
FT HELIX 571 578
FT HELIX 584 595
FT HELIX 604 614
FT HELIX 621 638
FT HELIX 640 646
FT HELIX 650 667
FT TURN 669 671
FT STRAND 673 676
FT HELIX 679 685
FT TURN 686 689
FT HELIX 697 709
FT HELIX 718 728
FT STRAND 753 761
FT TURN 771 774
FT STRAND 775 783
FT STRAND 785 789
FT STRAND 803 806
FT STRAND 811 816
FT STRAND 824 829
FT STRAND 832 834
FT STRAND 837 843
FT HELIX 847 878
SQ SEQUENCE 963 AA; 108314 MW; 5B31F9918F9CFF11 CRC64;
MWCLHCNSER TQSLLELELD SGVEGEAPSS ETGTSLDSPS AYPQGPLVPG SSLSPDHYEH
TSVGAYGLYS GPPGQQQRTR RPKLQHSTSI LRKQAEEEAI KRSRSLSESY ELSSDLQDKQ
VEMLERKYGG RLVTRHAART IQTAFRQYQM NKNFERLRSS MSENRMSRRI VLSNMRMQFS
FEGPEKVHSS YFEGKQVSVT NDGSQLGALV SPECGDLSEP TTLKSPAPSS DFADAITELE
DAFSRQVKSL AESIDDALNC RSLHTEEAPA LDAARARDTE PQTALHGMDH RKLDEMTASY
SDVTLYIDEE ELSPPLPLSQ AGDRPSSTES DLRLRAGGAA PDYWALAHKE DKADTDTSCR
STPSLERQEQ RLRVEHLPLL TIEPPSDSSV DLSDRSERGS LKRQSAYERS LGGQQGSPKH
GPHSGAPKSL PREEPELRPR PPRPLDSHLA INGSANRQSK SESDYSDGDN DSINSTSNSN
DTINCSSESS SRDSLREQTL SKQTYHKEAR NSWDSPAFSN DVIRKRHYRI GLNLFNKKPE
KGVQYLIERG FVPDTPVGVA HFLLQRKGLS RQMIGEFLGN RQKQFNRDVL DCVVDEMDFS
TMELDEALRK FQAHIRVQGE AQKVERLIEA FSQRYCICNP GVVRQFRNPD TIFILAFAII
LLNTDMYSPN VKPERKMKLE DFIKNLRGVD DGEDIPREML MGIYERIRKR ELKTNEDHVS
QVQKVEKLIV GKKPIGSLHP GLGCVLSLPH RRLVCYCRLF EVPDPNKPQK LGLHQREIFL
FNDLLVVTKI FQKKKNSVTY SFRQSFSLYG MQVLLFENQY YPNGIRLTSS VPGADIKVLI
NFNAPNPQDR KKFTDDLRES IAEVQEMEKH RIESELEKQK GVVRPSMSQC SSLKKESGNG
TLSRACLDDS YASGEGLKRS ALSSSLRDLS EAGKRGRRSS AGSLESNVEF QPFEPLQPSV
LCS
//
MIM
610166
*RECORD*
*FIELD* NO
610166
*FIELD* TI
*610166 IQ MOTIF- AND SEC7 DOMAIN-CONTAINING PROTEIN 1; IQSEC1
;;ADP-RIBOSYLATION FACTOR GUANINE NUCLEOTIDE EXCHANGE PROTEIN, 100-KD;
read moreARFGEP100;;
LONER, DROSOPHILA, HOMOLOG OF;;
KIAA0763
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1998) cloned IQSEC1, which they designated
KIAA0763. The deduced protein contains 841 amino acids. RT-PCR ELISA
detected highest IQSEC1 expression in brain, ovary, heart, lung, liver,
and kidney. Moderate expression was detected in skeletal muscle,
pancreas, spleen, and testis.
Someya et al. (2001) further characterized the KIAA0763 clone, which
they designated ARFGEP100. The deduced protein contains an N-terminal
IQ-like motif, a central serine-rich region and Sec7 domain, and a
C-terminal pleckstrin homology domain. Northern blot analysis detected
an 8-kb transcript expressed abundantly in leukocytes, brain, and spleen
and at lower levels in lung, placenta, small intestine, liver, and
kidney. A 7-kb transcript was also detected in brain. Endogenous
ARFGEP100 distributed with the cytosolic fraction of a fractionated
human glioblastoma cells. Western blot analysis detected ARFGEP100 at an
apparent molecular mass of 100 kD. Immunofluorescence microscopy
revealed ARFGEP100 in a cytosolic punctate pattern, and it colocalized
with ARF6 (600464) in peripheral areas.
GENE FUNCTION
Someya et al. (2001) found that ARFGEP100 accelerated binding of a
nonhydrolyzable GTP analog to recombinant ARF1 (103180) and ARF5
(103188) 2- to 3-fold and to ARF6 12-fold. ARFGEP100 activity was not
altered by brefeldin A or phospholipids.
Chen et al. (2003) found that Drosophila Loner, the homolog of human
IQSEC1, was required for myoblast fusion. In Drosophila embryos, Loner
localized to subcellular sites of fusion and acted downstream of cell
surface fusion receptors by recruiting Arf6 and stimulating guanine
nucleotide exchange.
By yeast 2-hybrid analysis of a fetal brain cDNA library, Hiroi et al.
(2006) found that GEP100 specifically interacted with alpha-catenin
(CTNNA1; 116805). Coimmunoprecipitation analysis of hepatoma (HepG2) and
cervical carcinoma (CaSki) cell lines confirmed interaction between
endogenous GEP100 and alpha-catenin. Depletion of GEP100 by small
interfering RNA in HepG2 and CaSki cells increased E-cadherin (CDH1;
192090) content 3-fold and blocked hepatocyte growth factor (HGF;
142409)-induced redistribution of E-cadherin, consistent with a known
role of ARF6 in this process. F-actin was markedly decreased in rat
kidney cells overexpressing wildtype GEP100, but not its GEP-inactive
mutants. Hiroi et al. (2006) concluded that GEP100 has a role in
activation of ARF6 for its functions in E-cadherin recycling and actin
remodeling.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the IQSEC1
gene to chromosome 3.
*FIELD* RF
1. Chen, E. H.; Pryce, B. A.; Tzeng, J. A.; Gonzalez, G. A.; Olson,
E. N.: Control of myoblast fusion by a guanine nucleotide exchange
factor, Loner, and its effector ARF6. Cell 114: 751-762, 2003.
2. Hiroi, T.; Someya, A.; Thompson, W.; Moss, J.; Vaughan, M.: GEP-100/BRAG2:
activator of ADP-ribosylation factor 6 for regulation of cell adhesion
and actin cytoskeleton via E-cadherin and alpha-catenin. Proc. Nat.
Acad. Sci. 103: 10672-10677, 2006.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
4. Someya, A.; Sata, M.; Takeda, K.; Pacheco-Rodriguez, G.; Ferrans,
V. J.; Moss, J.; Vaughan, M.: ARF-GEP100, a guanine nucleotide-exchange
protein for ADP-ribosylation factor 6. Proc. Nat. Acad. Sci. 98:
2413-2418, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 09/01/2006
*FIELD* CD
Patricia A. Hartz: 6/7/2006
*FIELD* ED
mgross: 09/01/2006
mgross: 6/7/2006
*RECORD*
*FIELD* NO
610166
*FIELD* TI
*610166 IQ MOTIF- AND SEC7 DOMAIN-CONTAINING PROTEIN 1; IQSEC1
;;ADP-RIBOSYLATION FACTOR GUANINE NUCLEOTIDE EXCHANGE PROTEIN, 100-KD;
read moreARFGEP100;;
LONER, DROSOPHILA, HOMOLOG OF;;
KIAA0763
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1998) cloned IQSEC1, which they designated
KIAA0763. The deduced protein contains 841 amino acids. RT-PCR ELISA
detected highest IQSEC1 expression in brain, ovary, heart, lung, liver,
and kidney. Moderate expression was detected in skeletal muscle,
pancreas, spleen, and testis.
Someya et al. (2001) further characterized the KIAA0763 clone, which
they designated ARFGEP100. The deduced protein contains an N-terminal
IQ-like motif, a central serine-rich region and Sec7 domain, and a
C-terminal pleckstrin homology domain. Northern blot analysis detected
an 8-kb transcript expressed abundantly in leukocytes, brain, and spleen
and at lower levels in lung, placenta, small intestine, liver, and
kidney. A 7-kb transcript was also detected in brain. Endogenous
ARFGEP100 distributed with the cytosolic fraction of a fractionated
human glioblastoma cells. Western blot analysis detected ARFGEP100 at an
apparent molecular mass of 100 kD. Immunofluorescence microscopy
revealed ARFGEP100 in a cytosolic punctate pattern, and it colocalized
with ARF6 (600464) in peripheral areas.
GENE FUNCTION
Someya et al. (2001) found that ARFGEP100 accelerated binding of a
nonhydrolyzable GTP analog to recombinant ARF1 (103180) and ARF5
(103188) 2- to 3-fold and to ARF6 12-fold. ARFGEP100 activity was not
altered by brefeldin A or phospholipids.
Chen et al. (2003) found that Drosophila Loner, the homolog of human
IQSEC1, was required for myoblast fusion. In Drosophila embryos, Loner
localized to subcellular sites of fusion and acted downstream of cell
surface fusion receptors by recruiting Arf6 and stimulating guanine
nucleotide exchange.
By yeast 2-hybrid analysis of a fetal brain cDNA library, Hiroi et al.
(2006) found that GEP100 specifically interacted with alpha-catenin
(CTNNA1; 116805). Coimmunoprecipitation analysis of hepatoma (HepG2) and
cervical carcinoma (CaSki) cell lines confirmed interaction between
endogenous GEP100 and alpha-catenin. Depletion of GEP100 by small
interfering RNA in HepG2 and CaSki cells increased E-cadherin (CDH1;
192090) content 3-fold and blocked hepatocyte growth factor (HGF;
142409)-induced redistribution of E-cadherin, consistent with a known
role of ARF6 in this process. F-actin was markedly decreased in rat
kidney cells overexpressing wildtype GEP100, but not its GEP-inactive
mutants. Hiroi et al. (2006) concluded that GEP100 has a role in
activation of ARF6 for its functions in E-cadherin recycling and actin
remodeling.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the IQSEC1
gene to chromosome 3.
*FIELD* RF
1. Chen, E. H.; Pryce, B. A.; Tzeng, J. A.; Gonzalez, G. A.; Olson,
E. N.: Control of myoblast fusion by a guanine nucleotide exchange
factor, Loner, and its effector ARF6. Cell 114: 751-762, 2003.
2. Hiroi, T.; Someya, A.; Thompson, W.; Moss, J.; Vaughan, M.: GEP-100/BRAG2:
activator of ADP-ribosylation factor 6 for regulation of cell adhesion
and actin cytoskeleton via E-cadherin and alpha-catenin. Proc. Nat.
Acad. Sci. 103: 10672-10677, 2006.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
4. Someya, A.; Sata, M.; Takeda, K.; Pacheco-Rodriguez, G.; Ferrans,
V. J.; Moss, J.; Vaughan, M.: ARF-GEP100, a guanine nucleotide-exchange
protein for ADP-ribosylation factor 6. Proc. Nat. Acad. Sci. 98:
2413-2418, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 09/01/2006
*FIELD* CD
Patricia A. Hartz: 6/7/2006
*FIELD* ED
mgross: 09/01/2006
mgross: 6/7/2006