RANB3_MACFA
ID RANB3_MACFA Reviewed; 499 AA.
AC Q4R4T9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Ran-binding protein 3;
DE Short=RanBP3;
GN Name=RANBP3; ORFNames=QccE-19613;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear export,
CC perhaps as export complex scaffolding protein. Bound to XPO1/CRM1,
CC stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound
CC GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to
CC CHC1/RCC1 and increases the guanine nucleotide exchange activity of
CC CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner.
CC Negative regulator of TGF-beta signaling through interaction with the
CC R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CHC1 in a Ran-stimulated manner. Interacts with
CC XPO1. Interacts (via its C-terminal R domain) with SMAD2
CC (dephosphorylated form via its MH1 and MH2 domains); the interaction
CC results in the nuclear export of SMAD2 and termination of the TGF-beta
CC signaling. Interacts (via its C-terminal R domain) with SMAD3
CC (dephosphorylated form via its MH1 domain); the interaction results in
CC the nuclear export of SMAD3 and termination of the TGF-beta signaling
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; AB169805; BAE01886.1; -; mRNA.
DR AlphaFoldDB; Q4R4T9; -.
DR SMR; Q4R4T9; -.
DR eggNOG; KOG0866; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138; PTHR23138; 2.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT CHAIN 2..499
FT /note="Ran-binding protein 3"
FT /id="PRO_0000097166"
FT DOMAIN 310..450
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CT10"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 56
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CT10"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
SQ SEQUENCE 499 AA; 53471 MW; 4C30D4B885EEE232 CRC64;
MADLANEEKP AIAPPVFVFQ KDKGQKRSAG GSSPEGGEDS DREYGNYCPP VKRERTSSLT
QFPPSQSEER SSGFRLKPPT LIHGQAPSAG LPSQKPKEQQ RSVLRPAVLQ APQPKALSQT
VPSSGTNGVS LLADCTGAVP AASPDTVARR SPSEAADEVC ALEEKEPQKN ESSNASEEEA
CEKKGPATQQ AFVFGQNLRD RVKLINESVD EADMENAGHP SADTPTATNY FLQYISSSLE
NSTNSADASS NKFVFGQNMS ERVLSPPKLN EVSSDANREN AAVESGSESS SQEATPEKES
LAESAAAYTK ATARKCLLEK VEVITGEEAE SNVLQMQCKL FVFDKTSQSW VERGRGLLRL
NDMASTDDGT LQSRLVMRTQ GSLRLILNTK LWAQMQIDKA SEKSIRITAM DTEDQGVKVF
LISASSKDTG QLYAALHHRI LALRSRVEQE QEAKMPVPEP GAAPSNEEDD SDDDDVLAPS
GATAAGAGDE GDGQTTGST
