RANB3_PONAB
ID RANB3_PONAB Reviewed; 494 AA.
AC Q5R4Y2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Ran-binding protein 3;
DE Short=RanBP3;
GN Name=RANBP3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR861107; CAH93184.1; -; mRNA.
DR RefSeq; NP_001126873.1; NM_001133401.1.
DR AlphaFoldDB; Q5R4Y2; -.
DR SMR; Q5R4Y2; -.
DR STRING; 9601.ENSPPYP00000010589; -.
DR GeneID; 100173886; -.
DR KEGG; pon:100173886; -.
DR CTD; 8498; -.
DR eggNOG; KOG0866; Eukaryota.
DR InParanoid; Q5R4Y2; -.
DR OrthoDB; 918488at2759; -.
DR Proteomes; UP000001595; 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..494
FT /note="Ran-binding protein 3"
FT /id="PRO_0000097168"
FT DOMAIN 305..445
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Basic and acidic residues"
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..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..293
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 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
SQ SEQUENCE 494 AA; 52953 MW; EA0C4506027B9CC6 CRC64;
MADLANEEKP AIAPPVFVFQ KDKGQKRSAG SSSPEGGEDS DREDGNYRPP VKRERTSSLT
QFPPSQSEER SSGFRLKPPT LIRGQAPSAG LPSQKPKEQQ RSVLRPAVLQ APQPKALSQT
VPSSGTNGVS LPADCTGAVP AASPDTAARR SPAEAADEEK EPQKNESSNA SGEEACEKKD
PATQQAFVFG QNLRDRVKLI NESMDEADME NAGHPSADTP TATNYFLQYI SSSLENSTNS
ADASSNKFVF GQNMSERVLS PPKLNEVSSD ANRENAAAES GSESSSQEAT PEKESLAESA
AAYTKATARK CLLEKVEVIT GEEAESNVLQ MQCKLFVFDK TSQSWVERGR GLLRLNDMAS
TDDGTLQSRL VMRTQGSLRL ILNTKLWAQM QIDKASEKSI RITAMDTEDQ VVKVFLISAS
SKDTGQLYAA LHHRILALRS RVEQEQEAKM PAPEPGAAPS NEEDDSDDDD VLAPSGATAA
GAGDEGDGQT TGST
