IQEC3_RAT
ID IQEC3_RAT Reviewed; 1194 AA.
AC Q76M68;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 3;
DE AltName: Full=Potential synaptic guanine nucleotide exchange factor for Arf;
DE AltName: Full=SynArfGEF-Po;
GN Name=Iqsec3; Synonyms=Sag;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH DLG1 AND DLG4.
RC TISSUE=Brain;
RX PubMed=15189337; DOI=10.1111/j.1471-4159.2004.02440.x;
RA Inaba Y., Tian Q.B., Okano A., Zhang J.-P., Sakagami H., Miyazawa S.,
RA Li W., Komiyama A., Inokuchi K., Kondo H., Suzuki T.;
RT "Brain-specific potential guanine nucleotide exchange factor for Arf,
RT synArfGEF (Po), is localized to postsynaptic density.";
RL J. Neurochem. 89:1347-1357(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for ARF1.
CC {ECO:0000250|UniProtKB:Q9UPP2}.
CC -!- SUBUNIT: Interacts with DLG1 and DLG4 (PubMed:15189337). Interacts with
CC GPHN (By similarity). {ECO:0000250|UniProtKB:Q3TES0,
CC ECO:0000269|PubMed:15189337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPP2}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q3TES0}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Localized to dendrites, as well
CC as somas of neuronal cells. {ECO:0000269|PubMed:15189337}.
CC -!- DEVELOPMENTAL STAGE: Expressed at E18 in hippocampal neurons.
CC {ECO:0000269|PubMed:15189337}.
CC -!- SIMILARITY: Belongs to the BRAG family. {ECO:0000305}.
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 EMBL; AB057643; BAD14305.1; -; mRNA.
DR RefSeq; NP_997500.1; NM_207617.1.
DR AlphaFoldDB; Q76M68; -.
DR SMR; Q76M68; -.
DR BioGRID; 267113; 1.
DR STRING; 10116.ENSRNOP00000018902; -.
DR CarbonylDB; Q76M68; -.
DR iPTMnet; Q76M68; -.
DR PhosphoSitePlus; Q76M68; -.
DR PaxDb; Q76M68; -.
DR PRIDE; Q76M68; -.
DR GeneID; 404781; -.
DR KEGG; rno:404781; -.
DR UCSC; RGD:1593191; rat.
DR CTD; 440073; -.
DR RGD; 1593191; Iqsec3.
DR eggNOG; KOG0931; Eukaryota.
DR InParanoid; Q76M68; -.
DR OrthoDB; 837077at2759; -.
DR PhylomeDB; Q76M68; -.
DR PRO; PR:Q76M68; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098690; C:glycinergic synapse; ISO:RGD.
DR GO; GO:0060077; C:inhibitory synapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0099629; C:postsynaptic specialization of symmetric synapse; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IDA:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IDA:SynGO.
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; 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 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; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1194
FT /note="IQ motif and SEC7 domain-containing protein 3"
FT /id="PRO_0000245612"
FT DOMAIN 311..340
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 646..839
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 852..985
FT /note="PH"
FT REGION 62..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..56
FT /evidence="ECO:0000255"
FT COMPBIAS 64..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1099
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1194 AA; 129018 MW; 4828FB1AA6F78B56 CRC64;
MESLLENPVR AVLYLKELTA IVQNQQSLIH TQRQRIDELE RRLDELSAEN RSLWEHQQLL
QAQPPPGLVP PPSAPLPAPA ATAPAATAAQ EPLQDHGQLI PATPEPPLQH HGQLLAQPQP
APSSRVQTPQ SPHQHPVAPG AVADKEKERP SSCCAAAGAL LQHASPAALG KGVLSRRPKN
ETVLHQFCCP ATDTEQKPAC SDLASQSDGS CAQAGGGMED SVVAAVAAGR PSAHAPKAQA
PELQQEEERP GAVGSPRAGP LRAASPGQQQ PALATALCSH TPAASEYELS LDLKNKQIEM
LEHKYGGHLV SRRAACTIQT AFRQYQLSKN FEKIRNSLLE SRLPRRISLR KVRAPTAESL
VAEKALLESC GLLGLPLGRS PSLPPTFAGS LTELEDSFTE QVQSLAKSID DALSTWSLKT
MCSLQESGAY QLHQALHPSA GQPGLETEAA REPDSGPGSG DEAGSLPQGH SGTLMMAFRD
VTVQIANQNI SVSSSTALSV ANCLGAQTAQ ATAEPAAVQT EQGDAATQEV SEVPASELMD
PPVEDSEAAE SGAQSAHEPT VAEAVVEEAV ATEAEEEEEG AGQAGKGAEA EVGDNSEQLS
SSSASTKSAK SGSEVSAAAS KEALQAVILS LPRYHCENPA SCRSPTLSTD TLRKRLYRIG
LNLFNINPDK GIQFLISRGF IPDTPIGVAH FLLQRKGLSR QMIGEFLGNS KKQFNRDVLD
CVVDEMDFSN MELDEALRKF QAHIRVQGEA QKVERLIEAF SQRYCMCNPE VVQQFHNPDT
IFILAFAIIL LNTDMYSPNI KPDRKMMLED FIRNLRGVDD GADIPRELVV GIYERIQQKE
LKSNEDHVTY VTKVEKSIVG MKTVLSMPHR RLVCCSRLFE VTDVNKLQKQ AAHQREVFLF
NDLLVILKLC PKKKSSFTYT FCKAVGLLGM RFHLFENEYY SHGITLATPL SGSEKKQVLH
FCALGSDEMQ KFVEDLKESI AEVTELEQIR IEWELERQQG TKTLSARSAG AQGDPQSKQG
SPTAKREAMA GEKATESSGE VSIHNRLQTF QHSPKLGVER GAPAPSPPTS PPPPLPPDPQ
PSPLREQPPP LPLPPPTPPG TLVQCQQIVK VIVLDKPCLA RMEPLLSQAL SCYASSSSDS
CGSTPLRGPG SPVKVIHQPP LPPPPPPYNH PHQFCPPGSL LLRRRYSSGS RSLV
