BIG1_MOUSE
ID BIG1_MOUSE Reviewed; 1846 AA.
AC G3X9K3; Q8BKL2;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
DE Short=BIG1;
DE Short=Brefeldin A-inhibited GEP 1;
DE AltName: Full=ADP-ribosylation factor guanine nucleotide-exchange factor 1;
GN Name=Arfgef1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1441-1846.
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-289, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3.
CC Promotes the activation of ARF1/ARF3 through replacement of GDP with
CC GTP. Involved in vesicular trafficking. Required for the maintenance of
CC Golgi structure; the function may be independent of its GEF activity.
CC Required for the maturaion of integrin beta-1 in the Golgi. Involved in
CC the establishment and persistence of cell polarity during directed cell
CC movement in wound healing. Proposed to act as A kinase-anchoring
CC protein (AKAP) and may mediate crosstalk between Arf and PKA pathways.
CC Inhibits GAP activity of MYO9B probably through competitive RhoA
CC binding. The function in the nucleus remains to be determined (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by brefeldin A. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with ARFGEF2/BIG2; both proteins are
CC probably part of the same or very similar macromolecular complexes.
CC Interacts with FKBP2. Interacts with MYO9B. Interacts with PRKAR1A and
CC PRKAR2A. Interacts with PPP1CC. Interacts with NCL, FBL, NUP62 and U3
CC small nucleolar RNA. Interacts with DPY30. Interacts with PDE3A.
CC Interacts with KANK1. Interacts with TBC1D22A and TBC1D22B.
CC {ECO:0000250|UniProtKB:Q9Y6D6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus,
CC trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus,
CC nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane
CC {ECO:0000250}. Note=Translocates from cytoplasm to membranes and
CC nucleus upon cAMP treatment. {ECO:0000250}.
CC -!- PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its GEF
CC activity and dephosphorylated by phosphatase PP1 (By similarity).
CC {ECO:0000250}.
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DR EMBL; AC102462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466536; EDL14306.1; -; Genomic_DNA.
DR EMBL; AK051592; BAC34685.1; -; mRNA.
DR CCDS; CCDS35512.1; -.
DR RefSeq; NP_001095900.1; NM_001102430.1.
DR AlphaFoldDB; G3X9K3; -.
DR SMR; G3X9K3; -.
DR BioGRID; 229258; 3.
DR IntAct; G3X9K3; 1.
DR MINT; G3X9K3; -.
DR STRING; 10090.ENSMUSP00000085986; -.
DR iPTMnet; G3X9K3; -.
DR PhosphoSitePlus; G3X9K3; -.
DR SwissPalm; G3X9K3; -.
DR EPD; G3X9K3; -.
DR jPOST; G3X9K3; -.
DR MaxQB; G3X9K3; -.
DR PaxDb; G3X9K3; -.
DR PeptideAtlas; G3X9K3; -.
DR PRIDE; G3X9K3; -.
DR ProteomicsDB; 273613; -.
DR Antibodypedia; 12092; 78 antibodies from 14 providers.
DR Ensembl; ENSMUST00000088615; ENSMUSP00000085986; ENSMUSG00000067851.
DR GeneID; 211673; -.
DR KEGG; mmu:211673; -.
DR UCSC; uc007ahn.1; mouse.
DR CTD; 10565; -.
DR MGI; MGI:2442988; Arfgef1.
DR VEuPathDB; HostDB:ENSMUSG00000067851; -.
DR eggNOG; KOG0929; Eukaryota.
DR GeneTree; ENSGT00940000157108; -.
DR HOGENOM; CLU_000691_1_0_1; -.
DR InParanoid; G3X9K3; -.
DR OMA; LLWNMEM; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; G3X9K3; -.
DR TreeFam; TF300714; -.
DR BioGRID-ORCS; 211673; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Arfgef1; mouse.
DR PRO; PR:G3X9K3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; G3X9K3; protein.
DR Bgee; ENSMUSG00000067851; Expressed in gastrula and 263 other tissues.
DR ExpressionAtlas; G3X9K3; baseline and differential.
DR Genevisible; G3X9K3; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISS:UniProtKB.
DR GO; GO:0010256; P:endomembrane system organization; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR015403; Sec7_C.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR InterPro; IPR032691; Sec7_N.
DR Pfam; PF16213; DCB; 1.
DR Pfam; PF09324; DUF1981; 1.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1846
FT /note="Brefeldin A-inhibited guanine nucleotide-exchange
FT protein 1"
FT /id="PRO_0000419330"
FT DOMAIN 688..877
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 2..224
FT /note="DCB; DCB:DCB domain and DCB:HUS domain interaction"
FT /evidence="ECO:0000250"
FT REGION 216..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..574
FT /note="HUS; DCB:HUS domain interaction"
FT /evidence="ECO:0000250"
FT REGION 631..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 708..712
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250"
FT COMPBIAS 264..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A631"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
FT MOD_RES 1563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A631"
FT MOD_RES 1566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
SQ SEQUENCE 1846 AA; 208500 MW; 7108F4430E610CB1 CRC64;
MYEGKKTKNM FLTRALEKIL ADKEVKKAHH SQLRKACEVA LEEIKVETEK QSPPHGEAKA
GSGTLPPVKS KTNFIEADKY FLPFELACQS KCPRIVSTSL DCLQKLIAYG HLTGRAPDST
TPGKKLIDRI IETICGCFQG PQTDEGVQLQ IIKALLTAVT SQHIEIHEGT VLQAVRTCYN
IYLASKNLIN QTTAKATLTQ MLNVIFARME NQALQEAKQM ERERHRQQQH LLQSPVSHHE
PESPHLRYLP PQTVDHINQE HEGDLEPQTH DVDKSLQDDT EPENGSDISS AENEQTEADQ
ATAAETLSKN DILYDGDYEE KPLDIVQSIV EEMVNIIVGD MGEGMAISAS TEGNTGTVED
GSDSENIQAN GIPGTPISVA YTPSLPDDRL SVSSNDTQES GNSSGPSPGA KFSHILQKDA
FLVFRSLCKL SMKPLSDGPP DPKSHELRSK ILSLQLLLSI LQNAGPVFRT NEMFINAIKQ
YLCVALSKNG VSSVPEVFEL SLSIFLTLLS NFKTHLKMQI EVFFKEIFLY ILETSTSSFD
HKWMVIQTLT RICADAQSVV DIYVNYDCDL NAANIFERLV NDLSKIAQGR GSQELGMSNV
QELSLRKKGL ECLVSILKCM VEWSKDQYVN PNSQTTLGQE KPSEQEISEV KHPETINRYG
SLNSLESTSS SGIGSYSTQM SGTDNPEQFE VLKQQKEIIE QGIDLFNKKP KRGIQYLQEQ
GMLGTTPEDI AQFLHQEERL DSTQVGEFLG DNDKFNKEVM YAYVDQHDFS GKDFVSALRL
FLEGFRLPGE AQKIDRLMEK FAARYLECNQ GQTLFASADT AYVLAYSIIM LTTDLHSPQV
KNKMTKEQYI KMNRGINDSK DLPEEYLSAI YNEIAGKKIS MKETKELTIP TKSTKQNVAS
EKQRRLLYNL EMEQMAKTAK ALMEAVSHVQ APFTSATHLE HVRPMFKLAW TPFLAAFSVG
LQDCDDTEVA SLCLEGIRCA IRIACIFSIQ LERDAYVQAL ARFTLLTVSS GITEMKQKNI
DTIKTLITVA HTDGNYLGNS WHEILKCISQ LELAQLIGTG VKPRYISGTV RGREGSLTGT
KDQAPDEFVG LGLVGGNVDW KQIASIQESI GETSSQSVVV AVDRIFTGST RLDGNAIVDF
VRWLCAVSMD ELLSTTHPRM FSLQKIVEIS YYNMGRIRLQ WSRIWEVIGD HFNKVGCNPN
EDVAIFAVDS LRQLSMKFLE KGELANFRFQ KDFLRPFEHI MKRNRSPTIR DMVVRCIAQM
VNSQAANIRS GWKNIFSVFH LAASDQDESI VELAFQTTGH IVTLVFEKHF PATIDSFQDA
VKCLSEFACN AAFPDTSMEA IRLIRHCAKY VSDRPQAFKE YTSDDMSVAP EDRVWVRGWF
PILFELSCII NRCKLDVRTR GLTVMFEIMK TYGHTYEKHW WQDLFRIVFR IFDNMKLPEQ
QTEKAEWMTT TCNHALYAIC DVFTQYLEVL SDVLLDDIFA QLYWCVQQDN EQLARSGTNC
LENVVILNGE KFTLEIWDKT CNCTLDIFKT TIPHALLTWR PTSGEAEPPS PSAVSEKPLD
AISQKSVDIH DSIQPRSSDN RQQAPLVSVS TVSEEVSKVK STAKFPEQKL FAALLIKCVV
QLELIQTIDN IVFFPATSKK EDAENLAAAQ RDAVDFDVRV DTQDQGMYRF LTSQQLFKLL
DCLLESHRFA KAFNSNNEQR TALWKAGFKG KSKPNLLKQE TSSLACGLRI LFRMYMDESR
VSAWEEVQQR LLNVCREALS YFLTLTSESH REAWTNLLLL FLTKVLKISD SRFKAHASFY
YPLLCEIMQF DLIPELRAVL RRFFLRIGIV FQISQPPEQE LGINRQ
