RBP2_BOVIN
ID RBP2_BOVIN Reviewed; 1085 AA.
AC P48820; Q28091;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=E3 SUMO-protein ligase RanBP2;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P49792};
DE AltName: Full=358 kDa nucleoporin;
DE AltName: Full=Nuclear pore complex protein Nup358;
DE AltName: Full=Nucleoporin Nup358;
DE AltName: Full=Ran-binding protein 2;
DE Short=RanBP2;
DE AltName: Full=p270;
DE Flags: Fragment;
GN Name=RANBP2;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Retina;
RX PubMed=7559465; DOI=10.1074/jbc.270.39.23179;
RA Ferreira P.A., Hom J.T., Pak W.L.;
RT "Retina-specifically expressed novel subtypes of bovine cyclophilin.";
RL J. Biol. Chem. 270:23179-23188(1995).
CC -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2
CC conjugation by UBE2I. Involved in transport factor (Ran-GTP,
CC karyopherin)-mediated protein import via the F-G repeat-containing
CC domain which acts as a docking site for substrates. Binds single-
CC stranded RNA (in vitro). May bind DNA. Component of the nuclear export
CC pathway. Specific docking site for the nuclear export factor exportin-
CC 1. Sumoylates PML at 'Lys-490' which is essential for the proper
CC assembly of PML-NB. Recruits BICD2 to the nuclear envelope and
CC cytoplasmic stacks of nuclear pore complex known as annulate lamellae
CC during G2 phase of cell cycle. Probable inactive PPIase with no
CC peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Part of the nuclear pore complex. Forms a complex with NXT1,
CC NXF1 and RANGAP1. Forms a tight complex with RANBP1 and UBE2I.
CC Interacts with SUMO1 but not SUMO2. Interacts with PRKN. Interacts with
CC sumoylated RANGAP1. Interacts with CDCA8. Interacts with PML (isoform
CC PML-4). Interacts with BICD2. Interacts with MCM3AP isoform GANP.
CC Interacts with COX11 (By similarity). {ECO:0000250|UniProtKB:P49792}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49792}. Nucleus
CC membrane {ECO:0000250|UniProtKB:P49792}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P49792}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete
CC intranuclear foci. Cytoplasmic filaments.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48820-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48820-2; Sequence=VSP_003620;
CC -!- TISSUE SPECIFICITY: Retina.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC {ECO:0000305}.
CC -!- DOMAIN: The PPIase cyclophilin-type domain has high structural
CC similarity with PPIA, but has extremely low and barely detectable
CC proline isomerase activity (in vitro) (By similarity). Only about half
CC of the residues that surround the PPIA active site cleft are conserved.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- PTM: The inner channel of the NPC has a different redox environment
CC from the cytoplasm and allows the formation of interchain disulfide
CC bonds between some nucleoporins, the significant increase of these
CC linkages upon oxidative stress reduces the permeability of the NPC.
CC {ECO:0000250|UniProtKB:Q9ERU9}.
CC -!- SIMILARITY: Belongs to the RanBP2 E3 ligase family. {ECO:0000305}.
CC -!- CAUTION: Despite the presence of a PPIase cyclophilin-type domain, it
CC has probably no peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000250|UniProtKB:P49792}.
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DR EMBL; L41691; AAB00071.1; -; mRNA.
DR EMBL; L41692; AAB00072.1; -; mRNA.
DR AlphaFoldDB; P48820; -.
DR SMR; P48820; -.
DR STRING; 9913.ENSBTAP00000042908; -.
DR PaxDb; P48820; -.
DR PRIDE; P48820; -.
DR eggNOG; KOG0864; Eukaryota.
DR eggNOG; KOG0865; Eukaryota.
DR InParanoid; P48820; -.
DR OrthoDB; 201737at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005642; C:annulate lamellae; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR022011; IR1-M.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR Pfam; PF12185; IR1-M; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00638; Ran_BP1; 2.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 2.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50196; RANBD1; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Isopeptide bond; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; RNA-binding; Transferase;
KW Translocation; Transport; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN <1..1085
FT /note="E3 SUMO-protein ligase RanBP2"
FT /id="PRO_0000204912"
FT REPEAT 125..126
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 174..310
FT /note="RanBD1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 382..383
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 401..402
FT /note="3"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 411..412
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 499..551
FT /note="1"
FT REPEAT 577..627
FT /note="2"
FT REPEAT 706..707
FT /note="5"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 708..709
FT /note="6"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 729..730
FT /note="7"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 746..747
FT /note="8"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 772..907
FT /note="RanBD1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT DOMAIN 928..1084
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 967..968
FT /note="9"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1050..1051
FT /note="10"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1066..1067
FT /note="11"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REGION 12..152
FT /note="Interaction with BICD2"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REGION 53..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..1067
FT /note="11 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 139..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..501
FT /note="Interaction with sumoylated RANGAP1"
FT /evidence="ECO:0000250"
FT REGION 499..627
FT /note="2 X 50 AA approximate repeats"
FT REGION 499..576
FT /note="Required for E3 SUMO-ligase activity"
FT /evidence="ECO:0000250"
FT REGION 499..551
FT /note="Interaction with UBE2I"
FT /evidence="ECO:0000250"
FT REGION 552..627
FT /note="Interaction with SUMO1"
FT /evidence="ECO:0000250"
FT REGION 666..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 532
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 460
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 460
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 681
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT VAR_SEQ <1..833
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7559465"
FT /id="VSP_003620"
FT CONFLICT 868
FT /note="A -> E (in Ref. 1; AAB00072)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 1085 AA; 120456 MW; 52741DB81A09937A CRC64;
KQKFEECQRL LLDIPLQTPH KLVDTGRAAK LIQRAEEMKS GLKDFKTFLT NDQTKVSDEE
SKDSRAGATT AADVSGAPNT ETTGPTLEWD NYDLREDALD DSVSSSSVHA SPLASSPVRK
NLFRFGESTT GFNFSFKSAL SPSKSPGKLN QSGASVGTDE DSDVTQEEER DGQHFEPVVP
LPDLVEVSSG EENEQVVFSH RAKLYRYDKD AGQWKERGIG DIKILQNYEN KQVRIVMRRD
QVLKLCANHR ITPDMTLQNM KGTERVWVWT ACDFADGERK IEHLAVRFKL QDVADSFKKI
FDEAKVAQEK DFLITPHVAR SATPRESPCG KMAVAVLEET TRERTDLSQG DDAADTTSEV
GGVSGTPEPT TKAVVSPPKF VFGSESVKSI FSSEKSKPFA FGNSSATGSL FGFSFNTPLK
NNSSEASSAA QSGSERKVEP GGRQESQNSD LKSASDGKVK NTSPAFLKEQ FSTSHTFKTP
EKVEERKKPE DLPSDDDVLI VYELTPTPEQ RALASRLQLP PTFFCYKNRP DYISEEEEDD
EDFDTAVKKL NGKLYLDDSE TCRLSEENVT DNEKECVIVW EKKPTVEELA KADTLKLPPT
FFCGICSDTD EDNGNAEDFQ SELQKVQEAQ KSQDENIASS ADGMCTDDTK VTVPFLCKSE
EPEFTTKSVS SPSVSSGTVD KPVDLSTRKE NDADSTSQVE SKTVTFGFGS GPGLSFADLA
SSNSGDFAFG SKDKNFQWAN TGAAVFGAQS TSKVGEDEDG SDEEVVHNED IHFEPIVSLP
EVEVKSGEED EEILFKERAK LYRWDREASQ WKDRGVGDIK ILWHTVKNYF RILMRRDQVF
KVCANHVITK TMELKPLNVS NNALVWTASD YADGEAKVEQ LAVRFKTKEM ADCFKKKFEE
CQQNLLKPQK GQDSLTAEFS KETNPVVFFD ICADDEPLGR ITMELFSNIV PKTAENFRAL
CTGEKGFGFK SSIFHRVIPD FVCQGGDITK HDGTGGRSIY GDKFEDENFD VKHTGPGLLS
MANRGQDTNN SQFFITLKKA ERLDFKHVVF GFVKDGMDTV KKIESFGSPK GSVSRRIIIT
ECGQI
