ID I3LLK1_PIG Unreviewed; 3233 AA.
AC I3LLK1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=RAN binding protein 2 {ECO:0000313|Ensembl:ENSSSCP00000024971.3};
GN Name=RANBP2 {ECO:0000313|Ensembl:ENSSSCP00000024971.3};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000024971.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000024971.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000024971.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000024971.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR SMR; I3LLK1; -.
DR STRING; 9823.ENSSSCP00000024971; -.
DR PeptideAtlas; I3LLK1; -.
DR Ensembl; ENSSSCT00000031443.4; ENSSSCP00000024971.3; ENSSSCG00000008136.5.
DR GeneTree; ENSGT00940000154389; -.
DR HOGENOM; CLU_022433_0_0_1; -.
DR InParanoid; I3LLK1; -.
DR Reactome; R-SSC-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-SSC-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-SSC-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SSC-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SSC-191859; snRNP Assembly.
DR Reactome; R-SSC-2467813; Separation of Sister Chromatids.
DR Reactome; R-SSC-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SSC-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-SSC-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SSC-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-SSC-5663220; RHO GTPases Activate Formins.
DR Reactome; R-SSC-68877; Mitotic Prometaphase.
DR Reactome; R-SSC-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000008136; Expressed in caecum and 43 other cell types or tissues.
DR ExpressionAtlas; I3LLK1; baseline and differential.
DR GO; GO:0005642; C:annulate lamellae; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IEA:Ensembl.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0106068; C:SUMO ligase complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0061665; F:SUMO ligase activity; IEA:Ensembl.
DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:Ensembl.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR CDD; cd13177; RanBD2_RanBP2-like; 1.
DR CDD; cd14685; RanBD3_RanBP2-like; 1.
DR CDD; cd13178; RanBD4_RanBP2-like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 7.
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 InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23138:SF169; E3 SUMO-PROTEIN LIGASE RANBP2; 1.
DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
DR Pfam; PF12185; IR1-M; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00638; Ran_BP1; 4.
DR Pfam; PF00641; zf-RanBP; 7.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 1.
DR SMART; SM00547; ZnF_RBZ; 7.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 6.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 7.
DR PROSITE; PS50199; ZF_RANBP2_2; 7.
PE 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:I3LLK1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT REPEAT 113..146
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1213..1349
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1393..1423
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1457..1486
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1521..1550
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1585..1614
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1647..1676
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1704..1733
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1766..1795
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1998..2134
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2295..2431
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2919..3054
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 3075..3231
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1192..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2173..2209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2260..2298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2465..2491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2542..2600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2618..2640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2808..2847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2173..2196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2260..2281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2586..2600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2810..2829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3233 AA; 356813 MW; 9201F95E6D331E93 CRC64;
MTQHARTHAC THACLPLAGY GAASRTFGRR APETAAAAAS ALASLARTPL GGAMRRSKAD
VERYIASVQG SAPSPREKSM KGFYFAKLYY EAKEYDLAKK YISTYINVQE RDPKAHRFLG
LLYEAEENID KAVECYKRSV ELNPTQKDLV LKIAELLCKN DVSDGRAKYW VERAAKLFPG
SPAIYKLKER LLDCKGEDGW NKLFDLIQSE LYSRPDDVHV NIRLVELYRS DKRLKDAVSH
CHKAERNMAL RSSLEWNSCV VQTLKEYLES SECLESDDSN WRATNRDLLV AYGNLMFLTL
STRDVQESRE LLESFDSALQ SVKSCVGGND ELSDTFLEMK GHFYMHAGSL LLKMGQHSDV
QWRALSELAA LCYLIAFQVP RPKIKLIKEA GQNLLEMMAY DRLSQSGHML LNLSRDKQDF
LKEVVESFAN KSGQSALYDA LFSSQSPKAR SFLGNDDFGC IDVQAPEPDD LARYDVGAVR
AHNGCLQHLT WLGLQWKSLS ASPAVRKWLK QLFHHLPQET SRLETNAPES ICILDLEVFL
LGVIYTSHLQ LKEKCNSHCS FYEPLCLPLP VCKQLCTERQ KSWWDAVCNL LHRKAVPGAS
AKLRLLVQHD INTLRGQGKH GLQPALLVHW AQSLQKTGSG LNSFYDQREY IGRSVHYWKV
VLPLLKIIKK KSSIPEPIDP LFKHFHSADI QASEIGEYEE EAHITFAVLD AVNGNIEDAM
TAFESINNVI SYWNLALIFR RKAEDIENDA LSCEEQEECK NYLRKTRDYL IKVLDDTDVD
PSVVKKLPVS LESVKEMLNS VMEELAGCSE AGLLYRNTDS EIKHSTPSPT KYSLSPNKSY
KYSKTPPQWA EDQSSLLKMI CEQVEAIKKE MQELKLNSSN SGSPCRWPTE NYGPDSGPDG
YQGSQNYHGA PLTVATTGPS VYYSQSPAYN SQYLLRPAAN VTPTKGPVYG MNRLPPQQHM
YTYSQQVHTP PVQSSSACMF SQEVYAPPLR FESPATGILS PRGDDYFNYN VQQTSTNPPL
PEPGYFTKPP VASHASRSAE SKVIDFGKTS FVQPGPGEGM RPPLAAPAHT TQPTPFKFNS
NFKSNDGDFT FSSPQVVAQP PSTTYNNSES LLGLLTSDKP LQGDSFSGPK AAQTIGPRNA
FNFGSKNVPG ISFTENMGPV QQKNSGFRRS DDMFTFHSPG KSIFATPAAE LANRSHEADG
GSAHGDDDDD GPHFEPVVPL PDKIEVKTGE EDEEEFFCNR AKLFRFDVGS REWKERGTGN
VKILRHKTSG KIRLLMRREQ VLKICANHYI SPHMALVPNA ASDRSFVWYA VDYADESPKP
EQLAIRFKTP EEAALFKCKF EEAQSMLKAS GANTATTTNQ ATRSVKEPTS HDSKDLGNSD
AGNMNFEFQV PRKEGSWWHC SSCSLKNAAT AKKCVSCQNL NPSSKELLSQ PLVDTVSTPK
PGSENAPDRF TVMPPKKEGH WDCSICLLRN EPTVSRCTAC QNTKPASKSG SSFVQQASFK
FGQGDLPKSA GSDFRSVFSI KEGQWDCSVC LVRNEGSSMK CVACQNPKKQ SSPASAAPAP
PFFKFGTSET SKAPKNGFDG VFAKKEAQWD CSVCLVRNEG SSVRCVACQN PKKQSSPAAP
APASFKFGTS ETSKVPKNGF EGVFTKKEGQ WDCSVCLVRN EASAAKCVAC QNPGRQEPLG
SAAPASSETS KAPRSGLEGM FTKKEGQWDC SVCLVQNEGS SMKCVACQNA KSSPASAVPA
PASFKFGTSE TSKAPRSGFE GMFTKKEGQW DCSTCSVRNE SSSSKCVACD ASKPTHKPVV
EEPSAFTLGS TTKVNDSSGS QVGTGFKSNF SEKAFKFGNT KQGFKFGHVD QENTPSFTFQ
GSSNTDSKST KGGFSFSVPV SADGFKFGIQ EPGNQEKNEK PFGNDAGCQA QDAGGQKDGS
AVVFGQTGST FTFADLAKSA SGEGFQFGKK DPNFKGFSGA GEKLFSSQSG KMTDKAEISA
DLEKDDDAYK TEDSDDIHFE PVVQMPEKVE LVTGEEDEKV LYSQRVKLFR FDAEISQWKE
RGLGNLKILK NEVNGKLRML MRREQVLKVC ANHWITTTMH LKPLSGSDRA WMWLASDFSD
GDAKLEQLAA KFKTPELAEE FKQKFEECQR LLLDIPLQTP HKLVDTGRAA KLIQRAEEMK
SGLKDFKTFL TNEQTKVPDQ ESKSSGEGTA GALEASSTPN PEAPGPALEW DNYDLREDAL
DTSVSSSSVH ASPLASSPVK KNLFRFGEST TGFNFSFKSA LSPSKSPAKL NQSGASVGTD
EDSDVTQEEE RDGQHFEPVV PLPDLVEVSS GEENEQVVFS HRAKLYRYDK DAGQWKERGI
GDIKILQNYD NKQVRIVMRR DQVLKLCANH RITPDMTLQS MKGTERVWVW TACDFADGER
KVEHLAVRFK LQDVADSFKK IFDEAKIAQE KDFLITPHVS RSTTPRESPC GKIAVAVLEE
TTRERTDLVQ GDEGADAASE VGGVSGTPEA TTKAVVSPPK FVFGSESVKS IFSSEKSKPF
AFGNSSATGS LFGFSFNAPL KNNSSEASPA AQSGSGRRVE PGGCQESQNP SLRPSLDGGV
GAPSPASTKA ESSASHTLHT PEKGFNFSLF KSNPMAFWTS TPSSQPESKA EEKKKPEDLP
SDDDVLIVYE LTPTPEQKAL AIRLQLPPTF FCYKNRPGYV SEEEEDDEDF DTAVKKLNGK
LYLDDSEKCR PSEQSLTDNE KECVIVWEKK PTVEEKAKAD TLKLPPTFFC GVCSDTDEDN
GNGEDFQSEL HKVQEAQKSQ NVEITGMAYS VCTGGAKVTV PFLGKSEEPD FTTKSITSPP
FSSGTGDKPV DLSTKKESDA DSENQVDSTT VSFGFGSSTG LSFADLASSN SGDFAFGSKD
KNFQWANTGA AVFRAQSTSR GGEDEDGSDE EVVHNEDIHF EPIVSLPEVE VKSGEEDEEV
LFKERAKLYR WDREVSQWKE RGVGDIKILW HTMKSYYRIL MRRDQVFKVC ANHVITKTME
LKPLNVSNNA LVWTASDYAD GEAKVEQLAV RFKTKEMADC FKKTFEECQQ NLLKHQKGQT
SLTAELSKET NPVVFFDVCA DDQPLGRITM ELFSNVVPQT AENFRALCTG EKGFGYKHSI
FHRVIPDFVC QGGDITKHDG SGGRSIYGDK FEDENFDVKH TGPGLLSMAN RGQNTNNSQF
FITLKKAEHL DFKHVVFGFV KDGMDTVKKI ESFGSPKGSV SRRITIVECG QIQ
//
