RANG_BOVIN
ID RANG_BOVIN Reviewed; 206 AA.
AC Q3T0M7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ran-specific GTPase-activating protein;
DE AltName: Full=Ran-binding protein 1;
DE Short=RanBP1;
GN Name=RANBP1;
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 [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in RAN-dependent nucleocytoplasmic transport.
CC Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and
CC mediates the dissociation of RAN from proteins involved in transport
CC into the nucleus (By similarity). Induces a conformation change in the
CC complex formed by XPO1 and RAN that triggers the release of the nuclear
CC export signal of cargo proteins (By similarity). Promotes the
CC disassembly of the complex formed by RAN and importin beta. Promotes
CC dissociation of RAN from a complex with KPNA2 and CSE1L (By
CC similarity). Required for normal mitotic spindle assembly and normal
CC progress through mitosis via its effect on RAN. Does not increase the
CC RAN GTPase activity by itself, but increases GTP hydrolysis mediated by
CC RANGAP1. Inhibits RCC1-dependent exchange of RAN-bound GDP by GTP (By
CC similarity). {ECO:0000250|UniProtKB:P34022,
CC ECO:0000250|UniProtKB:P43487}.
CC -!- SUBUNIT: Interacts with RAN (via C-terminus of GTP-bound form) but not
CC with GDP-bound RAN. Identified in a complex composed of RAN, RANGAP1
CC and RANBP1 (By similarity). Identified in a complex that contains
CC TNPO1, RAN and RANBP1. Identified in a complex that contains CSE1L,
CC KPNA2, RAN and RANBP1 (By similarity). Identified in a complex with
CC nucleotide-free RAN and RCC1 (By similarity).
CC {ECO:0000250|UniProtKB:P34022, ECO:0000250|UniProtKB:P43487}.
CC -!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102327; AAI02328.1; -; mRNA.
DR RefSeq; NP_001029758.1; NM_001034586.1.
DR RefSeq; XP_005218370.2; XM_005218313.3.
DR RefSeq; XP_015322737.1; XM_015467251.1.
DR AlphaFoldDB; Q3T0M7; -.
DR SMR; Q3T0M7; -.
DR STRING; 9913.ENSBTAP00000008744; -.
DR iPTMnet; Q3T0M7; -.
DR PaxDb; Q3T0M7; -.
DR PeptideAtlas; Q3T0M7; -.
DR PRIDE; Q3T0M7; -.
DR Ensembl; ENSBTAT00000008744; ENSBTAP00000008744; ENSBTAG00000006656.
DR GeneID; 533251; -.
DR KEGG; bta:533251; -.
DR CTD; 5902; -.
DR VEuPathDB; HostDB:ENSBTAG00000006656; -.
DR VGNC; VGNC:106890; RANBP1.
DR eggNOG; KOG0864; Eukaryota.
DR GeneTree; ENSGT00900000141073; -.
DR InParanoid; Q3T0M7; -.
DR OMA; HLEQTGN; -.
DR OrthoDB; 1573143at2759; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000006656; Expressed in pharyngeal tonsil and 108 other tissues.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:InterPro.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IBA:GO_Central.
DR GO; GO:0007051; P:spindle organization; IEA:Ensembl.
DR CDD; cd13179; RanBD_RanBP1; 1.
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 InterPro; IPR045256; RanBP1_RanBD.
DR PANTHER; PTHR23138; PTHR23138; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; GTPase activation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT CHAIN 2..206
FT /note="Ran-specific GTPase-activating protein"
FT /id="PRO_0000330895"
FT DOMAIN 26..164
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 150
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 150
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P34022"
FT MOD_RES 182
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43487"
SQ SEQUENCE 206 AA; 23712 MW; EEF0602A7752B0D4 CRC64;
MAAAKDTHED HDTSTENADE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS
ENDLPEWKER GTGDVKLLKH KEKGTIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW
VWNTHADFAD ECPKQELLAI RFLNAENAQK FKTKFEECRK EIEEKEKKGS GKNDSTEKVV
EKLEALSVQE GEQPQDAAPA AVEEEQ
