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Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)

 BIG1_BOVIN              Reviewed;        1849 AA.
O46382;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
28-FEB-2018, entry version 102.
RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
Short=Brefeldin A-inhibited GEP 1;
AltName: Full=ADP-ribosylation factor guanine nucleotide-exchange factor 1;
AltName: Full=p200 ARF guanine nucleotide exchange factor;
AltName: Full=p200 ARF-GEP1;
Name=ARFGEF1; Synonyms=ARFGEP1, BIG1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9371777; DOI=10.1073/pnas.94.24.12926;
Morinaga N., Moss J., Vaughan M.;
"Cloning and expression of a cDNA encoding a bovine brain brefeldin A-
sensitive guanine nucleotide-exchange protein for ADP-ribosylation
factor.";
Proc. Natl. Acad. Sci. U.S.A. 94:12926-12931(1997).
[2]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=8917509; DOI=10.1073/pnas.93.23.12856;
Morinaga N., Tsai S.-C., Moss J., Vaughan M.;
"Isolation of a brefeldin A-inhibited guanine nucleotide-exchange
protein for ADP ribosylation factor (ARF) 1 and ARF3 that contains a
Sec7-like domain.";
Proc. Natl. Acad. Sci. U.S.A. 93:12856-12860(1996).
-!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3.
Promotes the activation of ARF1/ARF3 through replacement of GDP
with GTP. Involved in vesicular trafficking. Required for the
maintenance of Golgi structure; the function may be independent of
its GEF activity. Required for the maturaion of integrin beta-1 in
the Golgi. Involved in the establishment and persistence of cell
polarity during directed cell movement in wound healing. Proposed
to act as A kinase-anchoring protein (AKAP) and may mediate
crosstalk between Arf and PKA pathways. Inhibits GAP activity of
MYO9B probably through competetive RhoA binding. The function in
the nucleus remains to be determined (By similarity).
{ECO:0000250}.
-!- ENZYME REGULATION: Inhibited by brefeldin A.
-!- SUBUNIT: Homodimer. Interacts with ARFGEF2/BIG2; both proteins are
probably part of the same or very similar macromolecular
complexes. Interacts with FKBP2. Interacts with MYO9B. Interacts
with PRKAR1A and PRKAR2A. Interacts with PPP1CC. Interacts with
NCL, FBL, NUP62 and U3 small nucleolar RNA. Interacts with DPY30.
Interacts with PDE3A. Interacts with KANK1. Interacts with
TBC1D22A and TBC1D22B. {ECO:0000250|UniProtKB:Q9Y6D6}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}.
Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus
{ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix
{ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from
cytoplasm to membranes and nucleus upon cAMP treatment.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Abundantly expressed in kidney, somewhat less
abundant in lung, spleen, and brain, and still less abundant in
heart.
-!- PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its
GEF activity and dephosphorylated by phosphatase PP1 (By
similarity). {ECO:0000250}.
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EMBL; AF023451; AAC48782.1; -; mRNA.
PIR; T14096; T14096.
RefSeq; NP_776422.1; NM_173997.2.
UniGene; Bt.4549; -.
ProteinModelPortal; O46382; -.
SMR; O46382; -.
STRING; 9913.ENSBTAP00000019553; -.
PaxDb; O46382; -.
PRIDE; O46382; -.
GeneID; 281022; -.
KEGG; bta:281022; -.
CTD; 10565; -.
eggNOG; KOG0929; Eukaryota.
eggNOG; COG5307; LUCA.
HOVERGEN; HBG004846; -.
InParanoid; O46382; -.
KO; K18442; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:GO_Central.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISS:UniProtKB.
GO; GO:0010256; P:endomembrane system organization; ISS:UniProtKB.
GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0090284; P:positive regulation of protein glycosylation in Golgi; ISS:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
Gene3D; 1.10.1000.11; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR032629; DCB_dom.
InterPro; IPR015403; Sec7_C.
InterPro; IPR023394; Sec7_C_sf.
InterPro; IPR000904; Sec7_dom.
InterPro; IPR035999; Sec7_dom_sf.
InterPro; IPR032691; Sec7_N.
Pfam; PF16213; DCB; 1.
Pfam; PF09324; DUF1981; 1.
Pfam; PF01369; Sec7; 1.
Pfam; PF12783; Sec7_N; 1.
SMART; SM00222; Sec7; 1.
SUPFAM; SSF48371; SSF48371; 3.
SUPFAM; SSF48425; SSF48425; 1.
PROSITE; PS50190; SEC7; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
Nucleus; Phosphoprotein; Protein transport; Reference proteome;
Transport.
CHAIN 1 1849 Brefeldin A-inhibited guanine nucleotide-
exchange protein 1.
/FTId=PRO_0000120206.
DOMAIN 709 840 SEC7. {ECO:0000255|PROSITE-
ProRule:PRU00189}.
REGION 2 224 DCB; DCB:DCB and DCB:HUS domain
interaction. {ECO:0000250}.
REGION 557 577 HUS; DCB:HUS domain interaction.
{ECO:0000250}.
MOTIF 711 715 Nuclear localization signal (NLS).
{ECO:0000250}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6D6}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000250|UniProtKB:G3X9K3}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000250|UniProtKB:G3X9K3}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:D4A631}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6D6}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6D6}.
MOD_RES 1079 1079 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6D6}.
MOD_RES 1566 1566 Phosphoserine.
{ECO:0000250|UniProtKB:D4A631}.
MOD_RES 1569 1569 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6D6}.
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


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