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Database: UniProt
Entry: A0A6Q2Y8M7_ESOLU
LinkDB: A0A6Q2Y8M7_ESOLU
Original site: A0A6Q2Y8M7_ESOLU 
ID   A0A6Q2Y8M7_ESOLU        Unreviewed;      2804 AA.
AC   A0A6Q2Y8M7;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=E3 SUMO-protein ligase RanBP2 {ECO:0000313|Ensembl:ENSELUP00000062305.1};
GN   Name=RANBP2 {ECO:0000313|Ensembl:ENSELUP00000062305.1};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000062305.1, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000062305.1, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000062305.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   Ensembl; ENSELUT00000053708.1; ENSELUP00000062305.1; ENSELUG00000007763.2.
DR   GeneTree; ENSGT00940000154389; -.
DR   Proteomes; UP000265140; LG16.
DR   Bgee; ENSELUG00000007763; Expressed in ovary and 15 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   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; 4.
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; 4.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00160; RanBD; 4.
DR   SMART; SM00028; TPR; 1.
DR   SMART; SM00547; ZnF_RBZ; 4.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 4.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 4.
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; 4.
DR   PROSITE; PS50199; ZF_RANBP2_2; 4.
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:UP000265140};
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          14..47
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1050..1186
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          1218..1247
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          1321..1350
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          1375..1404
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          1418..1447
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          1625..1761
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          1919..2056
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          2486..2621
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          2647..2803
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          954..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1183..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1490..1521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1894..1914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2091..2121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2137..2169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          692..719
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1026..1053
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2103..2117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2154..2168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2804 AA;  310683 MW;  B6552162A5EC7ED4 CRC64;
     IHVSAYLTIA ERDPKAHKLL GQLYEREGDI NKAVGCYKRS VDLNPAQKDL VLKVAELLVS
     KTERDSRAEF WVDKAAKLLP GNPAVFNLKE CLLNRQGQQG WNQLYDLLQA ELAVRPSDAH
     INVKLVQLFS SDGRLEEAVK HCLATEKRGL LRSNLDWYST VVRTLQEFLA QPSVLSNEKT
     SRCLHRELLL ARCSLLRLTL SGKGLQPSVE ALRSFDCAMQ GLRKAAPSVT DDLSEVYVEM
     RGHLYLHAGT LLLKMAQERE QQWRAVVDLA ALCYLLAYQV PRPKTKVCKG EQSQPLELLA
     SDRQSQAGHM LLNLNPNTHA FVREVVEAFG NRSGQGSLFE VLFGPQAPAG TSFIGNDDIR
     SINTQAPEIS DLIKWDNGSI QLHGGDLQQL CWLGLQWSFL AQRPALRDWL KQLFPRLTLE
     TSKLDTNAPE SICLLDLEVF LSGVVWCSHT QFQESAKISS TGQQHLHEPR CLPLPLLRLL
     STDRQRDWWD AVYSLIHKRA APGMSAKLRM TVQHGLSTLR GGEKHGLQPA LPIHWAQQLS
     STGLAVNSYY DQKDYIGRCV HYWKMVLPLL DKIKKKRSIP EPLDPMFIHF PSKVIQISSV
     KCFEEEAMIA FAVLLDIEGK TEEAIATLEA INNISSNWHL ARVRSEAFSV FFFSFQSNSV
     LIDLDLPCNS VRFPLVFNLS KEISPKTPPY WAEDQKSLLQ KLCQQVEALK NEVHDLRHNS
     SDSLMSPRQR IYGEGYGAEG MQEGYPPPQA FHGAPLTVAT TQAPSMYFNQ STAYNSGQYL
     LRTAANVTPT KAPVYGINRL PPQQHMYAYQ QPTNTPPLQS TPACIYTPQD QVFGAPLRFE
     SPATSLLSPY SEEYYGHTQP TTNPPLPEPG YFTKPSVVPV QQPKSVEGKP VDFGKISFGQ
     PIPAEPSKVP SFGAGVVAQS TPSAAFKFNS NFKSNDGDFT FKAKNSESLL GLLTSDMPSK
     SESPSEGKLL DPPSQGGIFT FGTKSTAGLS FGDAALTQDK PNLFGKIDQP FSFTNVTKPI
     FGLANRAEEE KGAESDNDST HVEEDEDGPH FEPIVPLPDK VDVKTGEEEE EEMFCNRAKL
     FRFDAETKEW KERGIGLVKI LKHNTSGKVR LLMRREQVLK ICANHYITPD MLLKPNAGSD
     KSWVWTAIDY ADEEPRTEQL AIRYKTSDEA LLFKMKFEEA QKIVPKSPKK QQDATDGKET
     FQPSAPQETS FAAQFARKDG EWDCDVCCIR NVSTAMQCVA CQSTNPNAPT EPDSKPATKT
     KGFTSGSASV GGFTFGFGAD SSKDSSCSGS FGKGFETTVE IQSKPSTVPF GSGFGAQFGK
     KPGQWECNTC LVINEASASS CVSCQTPNPS AKSTVEVAPT PKPTVSGFGT LFAKKDGQWD
     CDSCLVRNDA SATKCVSCQT PNPNASSTRS LGAMFAKQEG QWDCDTCLIR NEVSANQCIS
     CQTPNPNAKS TATAAPSSSS FSFSFGSRSA STQPAGTGFK SNLNSGSTFQ FGTSKDDRSS
     PASFKFETPP QSESSAPSAA GFSFTMPVPA GGFKFGIQEA AKETPPVDHV ENPLFTGKSS
     DFSFADLAKN SQGDFQFGQS DPNFKGFTRA GEQLFSSLQS NQRSEISADQ DEEDVYKTEE
     NDDIQFEPVV QMPEKVDLVT GEEDEQALYS QRVKLFRFDG ETSQWKERGV GVLKFLKNAT
     NGRLRVLMRR EQVLKVCANH WITTTMNLKP LAGSDKAWMW LANDFSDGDA RLEQLAAKFK
     TPELAEEFKL KFEECQRLLL DIPLQTPHKL VDTGRTAHLI QKAEEMKSGL KDLKSFLTDD
     KTKIKEDDSR ANITTASNTS GLIIKPHAES TGPTLEWDNY DLREEALDDS ADTSVYASPL
     ESSPIRKNLF RFGESTPGFN FSFQPVVSPA KSPAKLNKSG VSVDEEQDVT QEEERDGLYF
     EPVVPLPDLV EISTGEENEN VCFSHRAKLY RYDKDLNQWK ERGIGDLKIL QNYDTKRVRL
     VMRRDQVLKI CANHWVTSSM KLEPMKGAEK AWVWSAVDFA EIPEGNVEQL AVRFKLQDVA
     NSFRDIFEKA KAAQENDILV TPITQNDAPS QVTTTGPSVC GKAAVAILEE TTRERTDSSP
     EAFHTPDSRT ATPHTNLSKM IPPPKFLFGT DSLQKIFGNS PPSKEDGSSE SSKAKDSGRT
     SQPSPAFKIP DKGTSIYPFS ILLTLWFSLN CLFLNGNPHD VLMSLCSSVT APPQAEADDD
     DDDEVEVVYE RQPTADQAAL ARELLLPLTF FCYQNEPGYT SDDQTDDEDF ESAVKALLGK
     LYQDLPERAL DPEIEVVWEK RPTPEEEQRA RTLQLPPTFF CGVSSDSETE KDKLEDFESE
     LKTDVQSSTT DTPFSIQDEV QSSTAEADVP VLNTQKQFPE ESLTIQDPEV QSSTAEAPVP
     VQSKLNSCLS FSEAPSPFGF SALGAGGFSF ADLAQNTGGE FAFGKQDSSF SWANAGATLF
     GAAAPPKAEG EEEGSEEEDA NNVDIHFEPI VSLPEVETKS GEEDEEILFK ERTKLYRWDR
     DLGQWKERGV GDMKILFHPE KRFYRVLMRR EQVLKVCANH TISQSMELKP MNTSNQALVW
     TATDYAEGEG KVEQLAAKFK TAELAECFRK TFCECQSRIS QSEASSISSP QMSRVQEHSR
     DTNPQVYLVI SADDVPLGRV TIELFSHIVP KTAENFRVLC TGQKGFGLHN SVFHRIVPDF
     MCQGGDITKQ DGTGGRSIYG DKFEDENFDV RHTGPGLLSM ANRGRDTNNS QFFITLKKAE
     HLDFKHVAFG FVREGMDVVR EMGELGTKTG KPSKKIVITE CGQL
//
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