ID G1KAA3_ANOCA Unreviewed; 3042 AA.
AC G1KAA3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=RAN binding protein 2 {ECO:0000313|Ensembl:ENSACAP00000002048.3};
GN Name=RANBP2 {ECO:0000313|Ensembl:ENSACAP00000002048.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000002048.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000002048.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000002048.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000002048.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_008105262.1; XM_008107055.2.
DR STRING; 28377.ENSACAP00000002048; -.
DR Ensembl; ENSACAT00000002100.4; ENSACAP00000002048.3; ENSACAG00000002091.4.
DR GeneID; 100562216; -.
DR KEGG; acs:100562216; -.
DR eggNOG; KOG0864; Eukaryota.
DR GeneTree; ENSGT00940000154389; -.
DR HOGENOM; CLU_000378_1_0_1; -.
DR InParanoid; G1KAA3; -.
DR TreeFam; TF314797; -.
DR Proteomes; UP000001646; Chromosome 3.
DR Bgee; ENSACAG00000002091; Expressed in forelimb bud and 13 other cell types or tissues.
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; cd14684; RanBD1_RanBP2-like; 1.
DR CDD; cd13177; RanBD2_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; 2.
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; 3.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 2.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
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; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
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 110..143
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1222..1358
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1464..1493
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1522..1551
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1584..1613
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1821..1957
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2116..2252
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2729..2864
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2885..3041
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2080..2117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2361..2407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2598..2660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2554..2581
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 824..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2080..2101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2361..2376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2604..2627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2644..2660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3042 AA; 338843 MW; E87F892FD19C6E7A CRC64;
MPTRVVASSP SLFERGSDET GSAVLCSPPF FAASSSFLAA PGRSVGAATM MRRNRAEVDR
YVTSLQASAS SPREKSMKGF FFAKLYYEAK EYELAKRYIS TYLGVQERDP KAHKFLGQLY
EVEDNVEKAV GCYKRSVELN PTQKDLILKI AELLCDNDIT DGRAKYWVER AAKQFPGSPL
VFRLKERLLD SKSEDGWNQL FDLIQSELYA RPDDIYVNIR LVKLYMSNKR LKDAVAHCQE
AEKKISLQSS LEWCSCVVQT LKEYLASVEE SESDKGNWRK IHRDLLLAYS NLVVMTLSSR
GVEESRESLE SFDHALHSVK PHTNGVDELS VTFLEMRGHF YMHAGTLLLK MAQQSEMQWR
AVSELAALCY LLSFQVPRPK SKQIKGDQAE QERLEILACD RLSQSGHMLL NLSYGKPDFF
KEVVESFANK SGQSTLFEAL FGSDSSRDSS FLGSDDIRNV GVQGPECIEL TRYDIGAIRA
HSGSLQHLTW LGLHWNSLPT LEVIRKWLKQ LFHLPQETSR LETNAPESIC MLDLEVFLLG
VIFTCHLQLK EKFNTQYSLH QPRFLPLPIY KQLCTERQRA WWDAVYSVTH KRAVPGTAAK
VRLLVQHEIS ILRALGKHGL QPALIVHWAK SLLKTGCGLN SFYDQREYIG RSIYYWKKVL
PMLETIRKKR SISEPIDPLF KHFHSEDIQV SQVDEYEEEA RIAFAVLDAV DGKTEDATQA
FEAIKNVVAY WNLALIYQRK AEEMENDGLS LEEQEEYRNH LKKSRDYLVK IINESCTDTS
VTEKLPVSIK TVKEMLDCVM QELGESEEEP CLPLNNDLSQ PAEAEIKHST PSPTKYSLSP
SKGYKFSPKT PPRWAEDQKS LLQMICQQVE SIKNEMQEMK LNNSNTNMSH RWPSESYGTE
TMSDGYQGAQ NFHGAPLTVA TTGPSVYYNS SPAYNSQYLL RTAATNVTPT KAPVYAMNRL
TPQQHIYTYQ QPMHTPPLPN TSACMFSQEM YGTPLRFDSP TTGILSPRGN EDYYNYSVPQ
TSTNPPLPEP GYFTKPSAAP PASKSAESKV IEFGKPNFGQ PIPAEGAKSS SLMASAQSTQ
PTTFKFNSNF KSNDGDFTFS SPQVVTQPHG TGYSNSDSLL GLLTSDKPIK EDRYTGQKPL
AECSAGQRSI FSFGGKNASA ISFTDKMGPN QPKPSGLGKG EAFSFQEPGR PIFGPPNSDV
ANRSHETDGS LHGGEEEEDG PHFEPVVPLP DKIEVKTGEE DEEEIFCNRA KLFRFDTECK
EWKERGVGNV KILKHKITGK IRLLMRREQV LKICANHYIN PDMTLKPNAG SEKSFVWHAL
DYADELPKPE QLAIRFKTPE EAMLFKSKFQ EAQNSLKGSG TDISQQAAQS VESSRENTRW
DASGSGKPNP GLLSSGFQFK SGTSTAIGNS QVPGPDLSNA TKNTNAKSTF TITSSGATPA
SFSFGEEVLG THPTHGFGEQ FMLKKDQWEC NTCLVRNKIT AQNCVACQTP NPQPALLPAD
SVSFKPTPEV TQGTFGLTST KKDNPWECRV CSMGNEASAS HCINCKNPSG INTSVFAPQP
GFKFGQIDTS KVSQSGFGSA FMKKEGQWDC SVCLVRNEGS SPTCAACQTP NPSSSVPVPP
PSAPQPVFGF KNKLSETSGG PQGTGFKCDI TDKGFKFGHP TEQGKSPFTF QIPTSTEAKP
LKGGFNFAMP VPSGEFKFGI QEPTKDVAKE QSKEGGPLKG LEEEAKTFEG NALAKSHDAS
SKQHGDLVFG QHSSTFTFAD LAKTGEGFKF GHQDPDFKGF SGAGEKLFSS QGAKTCSKAN
TSTDLEKDDE AYKTEDSDDI HFEPVVQMPE KVELVTGEED ETVLYSQRVK LFRFDADVSQ
WKERGVGNLK ILKNEVNGKL RMLMRREQVL KVCANHWITT TMNLKPLSGS DKAWMWLASD
FSDGDAKLEQ LAAKFKTPEQ AEEFKLKFEE CQRLLLDIPL QTPHKLVDTG KTAELIQKAE
EMKSGLKDLK TFLTDEKTKL ADEEGKNSTS ITNTSDLIIK PHAESTGPTL EWDNYDLRGE
ALDDGTDNSM FGLPRASSPV RKNLFRFGES TTGFNFSFKS ALSPSKSPSK LNQSRTSVGT
DEESDATQED ERDGQYFEPV VPLPDLVEVT SGEENEQVVF SHRAKLYRFD KEANQWKERG
IGDIKILQNY DTKQVRVVMR RDQVLKLCAN HRITPDMGIQ QMKGTERAWV WTACDFAEGE
RKMELLAVRF KLQDVADSFK QIFEEARHAQ EKDTLITPLS SRANTPKESP CGKMAVAVLE
ETTRERTDLK QDEETVIQTA EPSVVVSPTE TPTKAVVSPP KFVFGSESVK SIFNNGKSKP
FTFGNTSATG SLFGFSFNAP PKNQSDSSGC EPENSHDTTT CKPDECQESG AAGWKSSGGK
RDAEGATSKV EALPNFSFKI LEKAVEIKKV PDTDTSDDVF IVYEATPTTE QRALAESLRL
PPTFFCYKNK PGYLSEDDDD EDYETVVKRL NGQLYPEEPE KHVKLQEKDQ GENEAESKNE
CVLVWEKKPT PEEKAKAEIL KLPPTFLCGI SSDTDEDNEN LEDFQTELRK VQEAKEAQVE
EVTSSTDDTC VTKEEELVVG VSRSEEPAST TSKAEGPDST TKPIHTIQAL LGTDDKPVDL
STKKENDSSS VTSTDQENKP FSFALGNIPG LSFADLALNN SGDFAFGSKD SNFKWADTGA
TVFGVQSVTK GDNEEDGSDE DVVHNDEIHF EPIVSLPEVE VKSGEEDEEI IFKERAKLYR
WDRDVNQWKE RGVGEIKILF HTQKKCYRIL MRRDQVLKVC ANHIITKTMD LKPLNTSNNA
MVWTATDYAD GEAKIEQLAV RFKTQDLADA FKRRFEDCQL NLSGLQEGHI SLTTELSKET
NPVVYLEVSA DDEPLGHITI ELFSNIVPRT AENFRALCTG EKGFGFRNSV FHRIIPDFVC
QGGDITRHDG TGGKSIYGNS FEDENFEVKH TGPGLLSMAN RGRDTNNSQF FITLKKTEHL
DFKHVVFGFV KDGMDIVKKM ESFGSPTGAV SKRITITDCG QI
//
