ID A0A3B4GG91_9CICH Unreviewed; 3032 AA.
AC A0A3B4GG91;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=E3 SUMO-protein ligase RanBP2 isoform X2 {ECO:0000313|RefSeq:XP_005747884.1};
DE SubName: Full=RAN binding protein 2 {ECO:0000313|Ensembl:ENSPNYP00000021154.1};
GN Name=RANBP2 {ECO:0000313|Ensembl:ENSPNYP00000021154.1};
GN Synonyms=ranbp2 {ECO:0000313|RefSeq:XP_005747884.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000021154.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000021154.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005747884.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_005747884.1; XM_005747827.1.
DR Ensembl; ENSPNYT00000021664.1; ENSPNYP00000021154.1; ENSPNYG00000015971.1.
DR GeneID; 102202063; -.
DR CTD; 5903; -.
DR GeneTree; ENSGT00940000154389; -.
DR OrthoDB; 158765at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 CDD; cd13177; RanBD2_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; 5.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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; 5.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 1.
DR SMART; SM00547; ZnF_RBZ; 5.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 5.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 5.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000313|RefSeq:XP_005747884.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000695023};
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 1184..1320
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1348..1377
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1454..1483
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1520..1549
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1575..1604
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1614..1643
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1854..1990
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2150..2287
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2712..2847
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2875..3031
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2112..2148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2332..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2374..2395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2407..2430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2564..2637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2687..2713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 820..847
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1163..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2112..2135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2335..2353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2565..2637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3032 AA; 333805 MW; 991FE24A50F79AFA CRC64;
MRRSKAEVDR YVSSVQSSSP SLKEKPVKGF LFAKLYFEAK EYDLAKRHVS DYLKVQERDP
KAHKFLGQLY EREGDINKAV GCYKRSVDLN PAQKDLVLKV AELLVSKQEC DSRAEFWVEK
AAKLLPGSPA VFNLKERLLS RQGQQGWNQL FDLLQTELAA RPADAHVNVK LVQLFRQDGR
LEEAVKHCLA AEKRAMLCNS LDWYTEVVCT LQEYLAQLSN EKMSRCIRRE LLLARCSLLR
ITLSESSVQP SVDALKEFDQ AMQEVSSVAG RSADELLEVF VEMRGHLYLH AGTLLLKLAQ
DRQQTWRAVR DLAALCYLLA YQVPRPKTKV TKRDQTAPQF LELLANDRQS QAGHMLFNLS
TDSSALISEV VEAFGNRSGQ DSLFDLLRGP QASAGLSFIA NDDIHSLTAM APELSQMAKW
DTGSILLHSG QLQHLSWLGL QWNLLDQRPP LREWLQQLFP RLTLETSKLD TNAPESICLL
DLEVFLYGVV FCSHCQLQRT AKINAGVNQS QQLLFEPRCL PLPLLRLLTT DRQREWWDAI
YSLIHKRAAP GVSGKLRMIV QHGLSTLRAG EKHGLQPALV IHWAQCLSQT GDGVNSYYDQ
KEYIGRSVHY WKVALPLLEK IKNRRSIPEP LDPLFIHFLS KDIQISSVKS YEEEARIAYA
VLLDIEGKTE EAISTLESIN NMSSIWHLAQ IYQRLSEEAS NGVEETQDRC IMFLRKFRAY
LSKMYSANAD DIEKLPVSME EVVDLLNDVN QQLGENGEVM DEEDEKEEGG LRGPAHSSPA
HLGETSATIS HIKFSTPSPN KSIVSPSKRL ISPKTQPHWV EDQKSLLQML CQQVEALKNE
VHDLRHNSSG TTVSPHHKMY GETYGAEGLQ EPFTPVQSYH GAPLTVATTG PSVYYNQSQA
YNSQYLLRTA ANVTPTKTPM YGVNRMPPQH NMYAYQQPTH TPPLQTAPAC IYPPQEQVFG
APLRFESPAT SLLSPYGEDF YGQSVTQQTS NPTLPEPGYF TKPPVVPVQQ PKNIEGKPMD
FGKLSFSQQA PTEVPRVPSF GTGVTAQSTP SPAFKFNSNF KSNDGDFTFS ASQNKHSESL
LGLLTSDIPS KTDTVPEKPQ TQEQPTTQTG IFTFGNKNVT SFSFVDSAQS TAAGGLFGKV
DQPFQFGDMS KPAFGMSKPT AEQERAGESD NDSTRAEEDE DGPHFEPIVP LPDKVDVKTG
EEEEEEIFCT RAKLYRFDTE TKEWKERGIG NVKILKHSTK GKVRLLMRRE QVLKICANHY
ITPDMLLKPN AGSDKSWVWN AIDYADEEPK PEQLAIRFKT VDEAALFKAK FEEAQKIVLK
SLDKTNQQER KEKTVKDSES IAAQFALKEG EWECSVCCVR NKPTDVRCVS CQSPNPNASS
KPDIQAAGEV KPSSFTFKFG TDSAKPSSSG STFTGFGGFG SSEASSFTFG LSSSKSADTG
SSTFGGFGAL LTSKPGQWDC ESCSIKNEAN VDSCVSCKAL KPSAKTAAAA QAAPAAGAPA
AQPVLSSVDS AGVAAKFSKK PGQWDCDVCE VRNEASAGKC VSCGSPNPAA KPTEGASLGS
NLPTVSVPQA DFAKEDGQWD CNACLVRNDA SAAECVSCKA PNENASLAAR FGKKDGEWDC
DTCLVRNEAS ADKCVSCQTL NPNAKSTSST SSSSSSSKFT FGTKSSSSQP IGTGFTIPFV
SGGTFQFGQS KDKSSPASFK FEAPQTGSST ISSSSFSFSM PIGPGGFKFG VQDPPKESPS
NDNQTQTGSA SSMLKSIADK HKEKETVSTP SVEQTEEEQN PLISGKANAF SFADLAKSAG
GNFQFGTKDP EFKGFSGAGE QLFTSFQATP TKTEASNELE DDDMYKTEEN DDIQFEPVIQ
MPEKVDLVTG EEDEQVLYSQ RVKLFRFDVG TSQWKERGVG VLKFLKNTTN GRLRVLMRRE
QVLKVCANHW ITTTMNLKPL AGSDKAWIWL ANDFSDGDAK LEQLAAKFKS PELAQEFKEK
FEECQRLLLD IPLQTPHKLV DTGRTAHLIQ KAEEMKSGLK DLKSFLTDEK TKIKDNDTQG
DIATAGDLSS LVIKPQGDTT GPTLEWDNYD LREDALDDTA DSSVYASPLA SSPLRKNLFR
FGESTGGFSF SFQPGISPSK SPAKLNQSRA SVGTDDEQDV TQDEERDGQY FEPVVPLPDL
VETSTGEENE QVVFSHRAKL YRYDKESKQW KERGIGDLKI LQNYNDKRAR LVMRRDQVLK
ICANHWISPI MKLEPMKGAE KAWVWSALDF AEEGEGKLEQ LAVRFKLQET ANTFKQVFEE
ANVAQGKKEL MTPATSRVVA PQDSGTPGSA KTTPAVCGKA AIAVLEETTK ERTELPADTG
SSASASHSPV NPGKTVVSPP KFVFGIDTLQ KIFGTPKSHS EPEQSTASGL KANDSGYTAK
TSLQVPAFKI PEKGSPQAEG SSARSDEDSE VEIVYVREPT AEQAALARKL QLPITFFCYK
NEPGYISDDE TDDEDYESAV KALNGKLYPD PPEKNAAACG EESDCQVVWE KKPTPEEEKK
AKSLQLPPTF FCGLSTTDSD PDQDKPEDFE TEVRKVHEVL VAQLDKSNEA SSSPAVTPEM
PASGPSSSRA EAADSTSTAD KQTTATPSSS SPIDLSTKKS VELESNTESK PASLTATTSR
DLSTFGFNAS GFSFAELAKN TDGFAFGSKD ANFSWANAGA TVFGSAVTSQ PKTNADEGGS
DEEEAPNNVD IHFEPIVSLP EVETKSGEED EEILFKERAK LYRWDRDIGQ WKERGIGDIK
ILFHPTKHFY RILMRREQVL RVCANHNISE AMELKPMNAS ANALIWTATD YSDGEGVIEQ
LAAKFKTPEI AESFKKTFCE CQNRMGQIDG DASSLCSPQM SRIQEHSRDT NPQVFLKLAA
DGQPLGTITI ELFSHIVPKT AENFRALCTG EKGFGLRDSI FHRIIPDFMC QGGDITKNNG
TGGKSIYGDK FEDENFDVRH TGPGILSMAN RGRDTNNSQF FITLKKAEHL DFKHVAFGWV
RDGMDVVQQM GELGSKAGPP TKKIIITDCG QL
//
