IQEC1_RAT
ID IQEC1_RAT Reviewed; 962 AA.
AC A0A0G2JUG7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 1 {ECO:0000305};
GN Name=Iqsec1 {ECO:0000312|RGD:1596313};
GN Synonyms=Brag2 {ECO:0000303|PubMed:20547133};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP INTERACTION WITH GRIA2, AND FUNCTION.
RX PubMed=20547133; DOI=10.1016/j.neuron.2010.05.003;
RA Scholz R., Berberich S., Rathgeber L., Kolleker A., Koehr G., Kornau H.C.;
RT "AMPA receptor signaling through BRAG2 and Arf6 critical for long-term
RT synaptic depression.";
RL Neuron 66:768-780(2010).
CC -!- FUNCTION: Guanine nucleotide exchange factor for ARF1 and ARF6. Guanine
CC nucleotide exchange factor activity is enhanced by lipid binding.
CC Accelerates GTP binding by ARFs of all three classes. Guanine
CC nucleotide exchange protein for ARF6, mediating internalization of
CC beta-1 integrin. Involved in neuronal development (By similarity). In
CC neurons, plays a role in the control of vesicle formation by endocytoc
CC cargo. Upon long term depression, interacts with GRIA2 and mediates the
CC activation of ARF6 to internalize synaptic AMPAR receptors
CC (PubMed:20547133). {ECO:0000250|UniProtKB:Q6DN90,
CC ECO:0000250|UniProtKB:Q8R0S2, ECO:0000269|PubMed:20547133}.
CC -!- SUBUNIT: Interacts with ARF1 and ARF6. Interacts with GRIA2; the
CC interaction is required for ARF6 activation (PubMed:20547133).
CC {ECO:0000250|UniProtKB:Q6DN90, ECO:0000269|PubMed:20547133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6DN90}. Nucleus
CC {ECO:0000250|UniProtKB:Q6DN90}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q8R0S2}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:Q8R0S2}. Note=At steady state,
CC may be preferentially cytosolic. {ECO:0000250|UniProtKB:Q6DN90}.
CC -!- DOMAIN: The PH domain mediates interaction with lipid membranes that
CC contain phosphatidylinositol-4,5-bisphosphate, but does not bind
CC membranes that lack phosphatidylinositol-4,5-bisphosphate.
CC {ECO:0000250|UniProtKB:Q6DN90}.
CC -!- SIMILARITY: Belongs to the BRAG family. {ECO:0000305}.
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DR EMBL; AABR07061428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0G2JUG7; -.
DR SMR; A0A0G2JUG7; -.
DR STRING; 10116.ENSRNOP00000064590; -.
DR PaxDb; A0A0G2JUG7; -.
DR RGD; 1596313; Iqsec1.
DR VEuPathDB; HostDB:ENSRNOG00000060350; -.
DR eggNOG; KOG0931; Eukaryota.
DR OMA; SMDHHKL; -.
DR PRO; PR:A0A0G2JUG7; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000060350; Expressed in frontal cortex and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0060996; P:dendritic spine development; ISO:RGD.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:RGD.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR CDD; cd13318; PH_IQSEC; 1.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR030737; IQSEC1.
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:SF327; PTHR10663:SF327; 1.
DR Pfam; PF16453; IQ_SEC7_PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Lipid-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..962
FT /note="IQ motif and SEC7 domain-containing protein 1"
FT /id="PRO_0000450080"
FT DOMAIN 134..163
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 516..709
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 773..865
FT /note="PH"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 910
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0S2"
SQ SEQUENCE 962 AA; 108080 MW; 73B39FC4FCCF3EB6 CRC64;
MACRRRYLSS LETGSSLSTD RYSVEGEAPS SETGTSLDSP SAYHQGPLVP GSSLSPDHYE
HTSVGAYGLY AGPGPQQRTR RPRLQHSTSV LRKQAEEEAI KRSRSLSESY ELSSDLQDKQ
VEMLERKYGG RLVTRHAART IQTAFRQYQM NKNFERLRSS MSENRMSRRI VLSNMRMQFS
FEGPEKVHSS YFEGKQVSVT NDGSQLGALV PSECGDLSDP ALKSPAPSSD FADAITELED
AFSRQVKSLA ESIDDALNCR SLHSEEVPAS DTARARDTEP KPGLHGMDHR KLDEMTASYS
DVTLYIDEEE LSPPLPLSQA GDRPSSTESD LRLRSGGAAQ DYWALAHKED KADTDTSCRS
TPSLERPEPR LRVEHLPLLT IEPPSDSSVE LSDRSDRSSL KRQSAYERSL GGQQGSPKHG
PHGGPPKGLP REEPELRPRP PRPLESHLAI NGSANRQSKS ESDYSDGDND SINSTSNSND
TINCSSESSS RDSLREQTLS KQTYHKETRN SWDSPAFSND VIRKRHYRIG LNLFNKKPEK
GIQYLIERGF VPDTPVGVAH FLLQRKGLSR QMIGEFLGNR QKQFNRDVLD CVVDEMDFSA
MELDEALRKF QAHIRVQGEA QKVERLIEAF SQRYCVCNPG VVRQFRNPDT IFILAFAIIL
LNTDMYSPNV KPERKMKLED FVKNLRGVDD GEDIPRETLI GIYERIRKRE LKTNEDHVSQ
VQKVEKLIVG KKPIGSLHHG LGCVLSLPHR RLVCYCRLFE VPDPNKPQKL GLHQREIFLF
NDLLVVTKIF QKKKNSVTYS FRQSFSLYGM QVLLFENQYY PNGIRLTSAV PGADIKVLIN
FNAPNPQDRK KFTDDLRESV AEVQEMEKHR IESELEKQKG VVRPSMSQCS SLKKESGNGT
LSRACLDDSY ASGEGLKRSA LSSSLRDLSE AGKRGRRSSA GSLESNVEFQ PFQPSQPPVL
CS
