BIG1_RAT
ID BIG1_RAT Reviewed; 1846 AA.
AC D4A631;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 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]
RP SUBCELLULAR LOCATION.
RX PubMed=11809827; DOI=10.1091/mbc.01-08-0420;
RA Zhao X., Lasell T.K., Melancon P.;
RT "Localization of large ADP-ribosylation factor-guanine nucleotide exchange
RT factors to different Golgi compartments: evidence for distinct functions in
RT protein traffic.";
RL Mol. Biol. Cell 13:119-133(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-289; SER-290;
RP SER-1563 AND SER-1566, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: 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 -!- INTERACTION:
CC D4A631; Q63358: Myo9b; NbExp=4; IntAct=EBI-6251168, EBI-6251137;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:11809827}.
CC Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11809827}.
CC Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix
CC {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm
CC to membranes and nucleus upon cAMP treatment (By similarity). PRKAR1B.
CC {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; CH473984; EDM11544.1; -; Genomic_DNA.
DR RefSeq; NP_001263985.1; NM_001277056.1.
DR AlphaFoldDB; D4A631; -.
DR SMR; D4A631; -.
DR BioGRID; 260275; 1.
DR IntAct; D4A631; 4.
DR STRING; 10116.ENSRNOP00000007766; -.
DR iPTMnet; D4A631; -.
DR PhosphoSitePlus; D4A631; -.
DR jPOST; D4A631; -.
DR PaxDb; D4A631; -.
DR PeptideAtlas; D4A631; -.
DR PRIDE; D4A631; -.
DR GeneID; 312915; -.
DR KEGG; rno:312915; -.
DR UCSC; RGD:1560793; rat.
DR CTD; 10565; -.
DR RGD; 1560793; Arfgef1.
DR VEuPathDB; HostDB:ENSRNOG00000005703; -.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_000691_1_0_1; -.
DR InParanoid; D4A631; -.
DR OMA; LLWNMEM; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; D4A631; -.
DR TreeFam; TF300714; -.
DR PRO; PR:D4A631; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000005703; Expressed in jejunum and 20 other tissues.
DR Genevisible; D4A631; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
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; IMP:CACAO.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:CACAO.
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 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_0000419331"
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 217..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..302
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 REGION 1571..1600
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 217..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..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 COMPBIAS 1571..1590
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:22673903"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 1566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1846 AA; 207890 MW; 3C87F6050FAC8E7C CRC64;
MYEGKKTKNM FLTRALEKIL ADKEVKKAHH SQLRKACEVA LEEIKVETEK QSPPHGEAKA
GSGTLPPVKS KTNFIEADKY FLPFELACQS KCPRIVSTSL DCLQKLIAYG HLTGSAPDST
TPGKKLIDRI IETICGCFQG PQTDEGVQLQ IIKALLTAVT SQHIEIHEGT VLQAVRTCYN
IYLASKNLIN QTTAKATLTQ MLNVIFARME NQALQEAKQM ERERHRQQHH LLQSPVSHHE
PESPHLRYLP PQTVDHIAQE QEGDLDPQTH DVDKSLQDDI EPENGSDISS AENEQTEADQ
ATAAETLSKD DVLCDGECEE KPQDIVQSIV EEMVDIIVGD MGEGTAVSAS ADGNAGAVED
GSDSENVQAN GIPGTPISAA 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 KPSEQEISEI KHPETINRYG
SLNSLESTSS SGIGSYSTQM SGTDNPEQFE VLKQQKEIIE QGIDLFNKKP KRGIQYLQEQ
GMLGTTPEDI AQFLHQEERL DSTQAGEFLG DNDKFNKEVM YAYVDQHDFS GKDFVSALRL
FLEGFRLPGE AQKIDRLMEK FAARYLECNQ GQTLFASADT AYVLAYSIIM LTTDLHSPQV
KNKMTKEQYI KMNRGINDSK DLPEEYLSAI YNEIAGKKIS MKETKELTIP TKSTKQNVAS
EKQRRLLYNL EMEQMAKTAK ALMEAVSHVQ APFTSATHLE HVRPMFKLAW TPFLAAFSVG
LQDCDDTDVA 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 VELAFQTSGH IVTLVFEKHF PATIDSFQDA
VKCLSEFACN AAFPDTSMEA IRLIRHCAKY VSDRPQAFKE YTSDDMNVAP EDRVWVRGWF
PILFELSCVI NRCKLDVRTR GLTVMFEIMK TYGHTYEKHW WQDLFRIVFR IFDNMKLPEQ
QTEKAEWMTT TCNHALYAIC DVFTQYLEVL SDVLLDDIFA QLYWCVQQDN EQLARSGTNC
LENVVILNGE KFTLEIWDKT CNCTLDIFKT TIPHALLTWR PTSGEAAPPS PSAMSEKQLD
AISQKSVDIH DSAQPRSSDN RQQAPLVSVS PASEEVSKGR PTAKFPEQKL FAALLIKCVV
QLELIQTIDN IVFFPATSKK EDAENLAAAQ RDAVDFDVRV DTQDQGMYRF LTSQQLFKLL
DCLLESHRFA KAFNSNNEQR TALWKAGFKG KSKPNLLKQE TSSLACGLRI LFRMYTDESR
VSAWEEVQQR LLNVCSEALS YFLTLTSESH REAWTNLLLL FLTKVLKISD NRFKAHASFY
YPLLCEIMQF DLIPELRAVL RRFFLRIGIV FQISQPPEQE LGINKQ
