ID A0A2K5UQ00_MACFA Unreviewed; 3212 AA.
AC A0A2K5UQ00;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=RAN binding protein 2 {ECO:0000313|Ensembl:ENSMFAP00000014498.2};
GN Name=RANBP2 {ECO:0000313|Ensembl:ENSMFAP00000014498.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000014498.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000014498.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000014498.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSMFAT00000064990.2; ENSMFAP00000014498.2; ENSMFAG00000029029.2.
DR VEuPathDB; HostDB:ENSMFAG00000029029; -.
DR GeneTree; ENSGT00940000154389; -.
DR Proteomes; UP000233100; Chromosome 13.
DR Bgee; ENSMFAG00000029029; Expressed in pituitary gland and 13 other cell types or tissues.
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:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR CDD; cd14684; RanBD1_RanBP2-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; 8.
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; 8.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 1.
DR SMART; SM00547; ZnF_RBZ; 8.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 7.
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; 8.
DR PROSITE; PS50199; ZF_RANBP2_2; 8.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
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 60..93
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1171..1307
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1351..1381
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1415..1444
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1479..1508
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1543..1572
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1606..1635
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1665..1694
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1724..1753
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1781..1810
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 2011..2147
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2308..2444
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2902..3037
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 3055..3211
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 757..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2187..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2272..2306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2555..2590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2630..2654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2816..2840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2194..2220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2555..2572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2573..2587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2639..2654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2818..2836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3212 AA; 357360 MW; DC0A71EBA0A64FD4 CRC64;
MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP
KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVELYRSNKR
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLEC LESDKSDWRA TNTDLLLAYA
NLTLLTLSTR DVQESRELLE SFDSALQSVK SSLGGNDELS ATFLEMKGHF YMHAGSLLLK
MGQHSDVQWR ALSELAALCY LIAFQVPRPK IKLIKGETGQ NLLEMMACDR LSQSGHMLLN
LSRGKQDFLK DIVESFANKS GQSALYDALF SSQSPKDTSF LGSDSIGNID VQEPELEDLA
RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL PAIRKWLKQL FHHLPQETSR LETNAPESIC
ILDLEVFLLG VVYTSHLQLK EKCNSYHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH
RKAVPGNSAK LRLLVQHEIN TLRAQEKHGL QPALLIHWAK CLQKTGSGLN SFYDQREYIG
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIGAYEEDA HITFAILDAV
NGNIEDAMTA FESIKSVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK
ILDDSDSNLS VVKKLPVPLE SVKEMLNSVM QELEDYSEGG PLYKNGSSRN ADSEIKHSTP
SPTKYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR
WPTESYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA TGILSPRGDD
YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE FGKTNFVQPM PGEGIRPSLP
TPAHTTQPPP FKFNSNFKSN DGDFTFSSPQ VVTQPPPAAY SNSESLLGLL TSDKPLQGDG
YSGPKPIPGG QTIGPRNTFN FGSKNVSGIS FTENMGSAQQ KNSGFRRSDD MFTFRGPGKS
VFGTPTLETA NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP DMKLTPNAGS
DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE AQSILKAPGT NVATASNQAI
RIVKEPTSHD NKDICKSDAG NMNFEFQVGK KEGSWWHCNS CSLKNAATAK KCVSCQNLNP
SNKELVGPPL AETVFTPKTG PENIQDRFAL MTPKKEGHWD CSICLVRNEP TVSRCIACQN
TKSANKSGSS FVHQASFTFG QGDLPKPVNS DFRSVFSTKE GQWECSVCLV QNEGSSTKCA
ACLNPRKQSL PATAIPTPAS FKFGTSETSK TPKSGFEDMF AKKEGQWDCS SCLVRNEANA
TRCVACQNPD KPSPSTSVSA PASFKFGTSE TSKAPKSGFE GMFTKKEGQW DCSVCLVRNE
ASATKCIACQ NPGKQNQTAS AISTPASSET SKAPKSGFEG MFTKKEGQWD CSVCLLRNEA
SATKCIACQN PGKQNQTTTA ISTPASSETS KAPKSGFEGM FTKKEGQWDC SMCLVRNEAS
ATKCIACQYP SKQNQTTAIS TPTSSEVSKA PKSGFEGMFI KKGQWDCSVC CVQNESSSLT
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAF KFGNTEQGFK
FGHVDQENSP SFMFQGSNTE FKSTKEGFSI PVSADGFKFG ISEPGNQEKK SEKPLENDSG
FQAQDISSQK NGSGVIFGQT SSTFTFADLA KSTSGEGFQF GKKDPNFKGF SGAGEKLFSS
QCGKMADKAN TSGDFEKDDD AYKTEDSDDI HFEPVVQMPE KVELVTGEED EKVLYSQRVK
LFRFDAEISQ WKERGLGNLK ILKNEVNGKL RMLMRREQVL KVCANHWITT TMNLKPLSGS
DRAWMWLASD FSDGDAKLEQ LAAKFKTPEL AEEFKQKFEE CQRLLLDIPL QTPHKLVDTG
RAAKLIQRAE EMKSGLKDFK TFLTNDQTKV TEEENKNSGT GSASASDTTI KPNPENTGPT
LEWDNYDLRE DALDDSVSSS SVHASPLASS PVRKNLFRFG ESTTGFNFSF KSALSPSKSP
AKLNQSGTSV GTDEESDVTQ EEERDGQYFE PVVPLPDLVE VSSGEENEQV VFSHRAKLYR
YDKDVGQWKE RGIGDIKILQ NYDNKQVRIV MRRDQVLKLC ANHRITPDMT LQNMKGTERV
WVWTACDFAD GERKVEHLAV RFKLQDVADS FKKIFDEAKT AQEKDSLITP HVSRSGTPRE
SPCGKIAVAV LEETTRERTD VIQGDDVADA TSEVEVSSTS ETTTKAVVSP PKFVFGSESV
KSIFSSEKSK PFAFGNSSAT GSLFGFSFNA PLKSNNSETS SVAQSGSESK VEPNKCELSK
NSDTEQSSDS KVKNLFASFP TEESSINYTF KTPEKGFNFS LFKSNPMAFW TSTPSSQPEN
KAKEKKKPED SPSDDDVLIV YELTPTAEQK ALATKLKLPP TFFCYKNRPD YVSEEEEDDE
DFETAVKKLN GKLYLDGSEK CRPLEENTAD NEKECIIVWE KKPTVEEKAK ADTLKLPPTF
FCGVCSDTDE DNGNGEDFQS ELQKVQEAQK SQTEEITSTT DSVYTVGTEV MVPSFCKSEE
PDSTTRSISS PSVSCETVDK PVDLSTRKEL DTDSTSQDKN FQWANTGAAV FGTQSVGTQS
IGKVGEDEDG SDEEVVHNED IHFEPIVSLP EVEVKSGEED EEILFKERAK LYRWDRDVSQ
WKERGVGDIK ILWHTMKNYY RILMRRDQVF KVCANHVITK TMELKPLNVS NNALVWTASD
YADGEAKVEQ LAVRFKTKEV ADCFKKTFEE CQQNLLQLQK GHAAELSKET NPVVFFDVCA
DGEPLGRITM ELFSNIVPRT AENFRALCTG EKGFGFKNSI FHRVIPDFVC QGGDITKHDG
TGGQSIYGDK FEDENFDVKH TGPGLLSMAN RGQNTNNSQF FITLKKAEHL DFKHVVFGFV
KDGMDTVKKI ESFGSPKGSV CRRITITECG QI
//
