BIG1_BOVIN
ID BIG1_BOVIN Reviewed; 1849 AA.
AC O46382;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
DE Short=Brefeldin A-inhibited GEP 1;
DE AltName: Full=ADP-ribosylation factor guanine nucleotide-exchange factor 1;
DE AltName: Full=p200 ARF guanine nucleotide exchange factor;
DE AltName: Full=p200 ARF-GEP1;
GN Name=ARFGEF1; Synonyms=ARFGEP1, BIG1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9371777; DOI=10.1073/pnas.94.24.12926;
RA Morinaga N., Moss J., Vaughan M.;
RT "Cloning and expression of a cDNA encoding a bovine brain brefeldin A-
RT sensitive guanine nucleotide-exchange protein for ADP-ribosylation
RT factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12926-12931(1997).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=8917509; DOI=10.1073/pnas.93.23.12856;
RA Morinaga N., Tsai S.-C., Moss J., Vaughan M.;
RT "Isolation of a brefeldin A-inhibited guanine nucleotide-exchange protein
RT for ADP ribosylation factor (ARF) 1 and ARF3 that contains a Sec7-like
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12856-12860(1996).
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.
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 -!- TISSUE SPECIFICITY: Abundantly expressed in kidney, somewhat less
CC abundant in lung, spleen, and brain, and still less abundant in heart.
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; AF023451; AAC48782.1; -; mRNA.
DR PIR; T14096; T14096.
DR RefSeq; NP_776422.1; NM_173997.2.
DR AlphaFoldDB; O46382; -.
DR SMR; O46382; -.
DR STRING; 9913.ENSBTAP00000019553; -.
DR PaxDb; O46382; -.
DR PRIDE; O46382; -.
DR GeneID; 281022; -.
DR KEGG; bta:281022; -.
DR CTD; 10565; -.
DR eggNOG; KOG0929; Eukaryota.
DR InParanoid; O46382; -.
DR OrthoDB; 815698at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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: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; Direct protein sequencing; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1849
FT /note="Brefeldin A-inhibited guanine nucleotide-exchange
FT protein 1"
FT /id="PRO_0000120206"
FT DOMAIN 709..840
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 2..224
FT /note="DCB; DCB:DCB and DCB:HUS domain interaction"
FT /evidence="ECO:0000250"
FT REGION 46..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..577
FT /note="HUS; DCB:HUS domain interaction"
FT /evidence="ECO:0000250"
FT REGION 634..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 711..715
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250"
FT COMPBIAS 216..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..687
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:0000250|UniProtKB:G3X9K3"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3X9K3"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A631"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
FT MOD_RES 1566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A631"
FT MOD_RES 1569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6D6"
SQ SEQUENCE 1849 AA; 208712 MW; 8A8A9C864B899E7D CRC64;
MYEGKKTKNM FLTRALEKIL ADKEVKKAHH SQLRKACEVA LEEIKAETEK QSPPHGEAKA
GSSTLPPVKS KTNFIEADKY FLPFELACQS KCPRIVSTSL DCLQKLIAYG HLTGNAPDST
TPGKKLIDRI IETICGCFQG PQTDEGVQLQ IIKALLTAVT SQHIEIHEGT VLQAVRTCYN
IYLASKNLIN QTTAKATLTQ MLNVIFARME NQALQEAKQM EKERHRQHHH LLQSPVSHHE
PESPQLRYLP PQTVDHIPQE HEGDLDPQTN DVDKSLQDDT EPENGSDISS AENEQTEADQ
ATAAETLSKN DILYDGENHD CEEKPQDIVQ SIVEEMVNIV VGDTGERTTI NVSADGNNGT
IEDGSDSENI QANGIPGTPI SVAYTPSLPD DRLSVSSNDT QESGNSSGPS PGAKFSHILQ
KDAFLVFRSL CKLSMKPLSD GPPDPKSHEL RSKILSLQLL LSILQNAGPI FGTNEMFINA
IKQYLCVALS KNGVSSVPEV FELSLSIFLT LLSNFKTHLK MQIEVFFKEI FLYILETSTS
SFDHKWMVIQ TLTRICADAQ SVVDIYVNYD CDLNAANIFE RLVNDLSKIA QGRGSQELGM
SNVQELSLRK KGLECLVSIL KCMVEWSKDQ YVNPNSQTTL GQEKPSEQET SEMKHPETIN
RYGSLNSLES TSSSGIGSYS TQMSGTDNPE QFEVLKQQKE IIEQGIDLFT KKPKRGIQYL
QEQGMLGTTP EDIAQFLHQE ERLDSTQVGE FLGDNDKFNK EVMYAYVDQH DFSGKDFVSA
LRMFLEGFRL PGEAQKIDRL MEKFAARYLE CNQGQTLFAS ADTAYVLAYS IIMLTTDLHS
PQVKNKMTKE QYIKMNRGIN DSKDLPEEYL SAIYNEIAGK KISMKETKEL TIPAKSSKQN
VASEKQRRLL YNLEMEQMAK TAKALMEAVS HVQAPFTSAT HLEHVRPMFK LAWTPFLAAF
SVGLQDCDDT EVASLCLEGI RCAIRIACIF SIQLERDAYV QALARFTLLT VSSGITEMKQ
KNIDTIKTLI TVAHTDGNYL GNSWHEILKC ISQLELAQLI GTGVKPRYIS GTVRGREGSL
TGAKDQAPDE FVGLGLVGGN VDWKQIASIQ ESIGETSSQS VVVAVDRIFT GSTRLDGNAI
VDFVRWLCAV SMDELLSTTH PRMFSLQKIV EISYYNMGRI RLQWSRIWEV IGDHFNKVGC
NPNEDVAIFA VDSLRQLSMK FLEKGELANF RFQKDFLRPF EHIMKRNRSP TIRDMVVRCI
AQMVNSQAAN IRSGWKNIFS VFHLAASDQD ESIVELAFQT TGHIVTLVFE KHFPATIDSF
QDAVKCLSEF ACNAAFPDTS MEAIRLIRHC AKYVSDRPQA FKEYTSDDMN VAPEDRVWVR
GWFPILFELS CIINRCKLDV RTRGLTVMFE IMKTYGYTYE KHWWQDLFRI VFRIFDNMKL
PEQQTEKAEW MTTTCNHALY AICDVFTQYL EVLSDVLLDD IFAQLYWCVQ QDNEQLARSG
TNCLENVVIL NGEKFTLEIW DKTCNCTLDI FKTTIPHALL TWRPISGETA PPTPSPVSEN
QLDTISQKSV DIHDSIQPRS ADNRQQAPLA SVSTVNEEIS KIKPTAKFPE QKLFAALLIK
CVVQLELIQT IDNIVFFPAT SRKEDAENLA AAQRDAVDFD VRVDTQDQGM YRFLTSQQLF
KLLDCLLESH RFAKAFNSNN EQRTALWKAG FKGKSKPNLL KQETSSLACG LRILFRMYTD
ESRASAWEEV QQRLLNVCSE ALSYFLTLTS ESHREAWTNL LLLFLTKVLK ISDNRFKAHA
SFYYPLLCEI MQFDLIPELR AVLRRFFLRI GVVFQISQPP EQELGINKQ
