ID A0A3B3CTW6_ORYME Unreviewed; 2997 AA.
AC A0A3B3CTW6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=RANBP2-like and GRIP domain-containing protein 8 {ECO:0000313|Ensembl:ENSOMEP00000021036.1};
GN Name=RANBP2 {ECO:0000313|Ensembl:ENSOMEP00000021036.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000021036.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000021036.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSOMET00000030647.1; ENSOMEP00000021036.1; ENSOMEG00000022969.1.
DR GeneTree; ENSGT00940000154389; -.
DR OMA; TQCIACQ; -.
DR OrthoDB; 158765at2759; -.
DR Proteomes; UP000261560; Unplaced.
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; 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; 5.
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; 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; 4.
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; 5.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 1168..1304
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1329..1358
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1429..1458
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1497..1526
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1549..1579
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1589..1618
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1825..1961
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2121..2258
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2677..2812
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2840..2996
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 755..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2004..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2298..2325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2346..2373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2478..2602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2814..2834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 820..847
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1152..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2013..2028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2087..2106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2501..2535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2564..2602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2997 AA; 330262 MW; 710131534A3E6102 CRC64;
MRRSKVEVDR YVSSVLGSSP SPKEKPVKGF LFAKLYLEAK EYELAKRHVS EYLKVQERDP
KAHKFLGQLY ERDGELNKAV GCYKRSVDLN PTQRDLVLKV AELLVGKEEC DSRAEFWVDK
AAKLLPGNPT VFTLKERLLS RQGQQGWNQL FDLLQAELAA RPADPHVNVK LVQLFCQDGR
LDEAVKHCLA AEKRGLLRRS KEWYTVVLHT LQEYLAQPNT SSNEKLCRRL QKEVLLTHCN
LLRITLSETN VQPSLDAFRS FDGAMQTLNT AARRQSDDLL EIFVEMRGHL YLLAATLLLK
MAHERQQTWR AVTDLSAMCY LLAYQNPRPK PRVNKREQSP PLLLELLAND RQSQAGHMLL
SLTADPPTLI REVVEVFGNF KGQESLFELL WGPQASSSSS FIATDDIRSL GAVAPELSQL
TKYDTGSILL HGEDLQHLSW LGLQWTLQDQ RPPLRDWLQQ LYPRLTLETS KIDTNAPESI
CLLDLEVFLC GVVFTSHCQL QEKAKLSSGM KTQQELLEPR CLPLSLLRLL TTDRQREWWD
ATYNLIYNRA APGTSAKLRM IVQHGLNTLR AGEKHGLQPA LAIHWAQYLS QTGDGMNSYY
DQKEYIGRSV HYWRAVLPLL EKIKSRRSIP EPLEPLFMHF SSKNIQIPSV RSYEEEARIA
HAILLDIEGR TDEAITILEC INNLSSTWHL AQIYQRLSEE ATNGVEETQD RCITSLRKYR
TYLLRIYNAN ANEIDKLPVS MEEVVDLLND VNQQLGESGE DEEEEKEFER QIGPDHSSPA
HLQETSATIS HIKFSTPSPN KNIVSPSKRL ISPKTPPHWI EDQKNLLQIL CQKVEALTNE
VQDLKLNASG AAGSPHKLYG DSYRAEGLQE PFTPVQSYHG APLTVATTGP SLFYNQSPAY
NSQYLLRPAA NVTPTKAPVY GVNRLPPQQH VYGYQQPTHT PPLQTTPACM YPPQEQVFGA
PLRFESPATS LLSPYSEEYF GQSVSQQAPN PPLPEPGYFT KPSALPVQPP KSLEGASVDF
GKVPLSQPTP EVPRGPSFGA AAQSATPAAF KFNSNFKSND GDFTFSASQA KHSESLLGLL
TSDIPTTKDS APEKPPTQEH QTSIFSFGNK TSFSFIDPVQ NSASGGAFGK VDQPFKFGEI
SKPLFDIPKQ AESDNDSAHA DEDEDGPHFE PIVPLPDKVD VKTGEEEEEE MFCNRAKLYR
FDTETKEWKE RGIGNLKILK HNTKGKVRLL MRREQVLKIC ANHYITADML LKPNAGSDKS
WVWNAIDYAD EEPKTEQLAI RFKTVEEASL FKAKFEEAQK VALASPEKQP EKKSSSKDSD
SLAAQFALKE GEWECDVCCV RNKSSDLRCR ACQAPNPTSK AEVQPPKASA FTFKFGTDSS
KQSSSGSTFT GFGGFGSSAP SSFTFGIGSS KVADTAPKAF SFGSLDDKKS AQWECEKCST
KNETSADVCV SCKTSKTKKT VQSSPAAAAL PAAAAQPTAT VQPSAFTSDL SAKFSKKPGQ
WDCEVCDVRN ESTAKKCVAC NTSKTKETVA APVPPSMPPA PELTADSSKA GGQWDCKSCL
VRNEASATKC VCCSAPNDAL CLEAIFGKKQ GEWDCDACLV RNLATASKCI ACQTANPNAK
SDSSSSAPPF SFGSKSQPAG SGFPTSSGGG SPFQFGQSKE KSSALSPFKF ESFQAAPTST
TTSSSGFSFS KPIPAGGFKF GLQEPAKNPA SSSDPAPPGP ASSCLKSFAD KHKEKETPPT
PPDAKAEQDA NPLVSGKGNV SSFADLANSS GSDFQFGKKD PNFKGFSRAG EQIFSTPQAT
PTKTDAVSEQ EDDGMYKTEE NDDIQFEPVV QMPDKVDVIT GEEDEQVLYS QRVKLFRFDT
SSSQWKERGV GVLKFLKNSV NGRLRVLMRR EQVLKVCANH WITTTMNLKP LAGSDKAWMW
MANDFSDGDA KLEQLAVKFK TPELAEEFKA KFEECQRLLL DIPLQTPHKL VDTGRTAHLI
QKAEEMKSGL KDLKSFLTDD KTKIKDEDTQ ADSTASGEAS SLTIRPHGET TGPTLEWDNY
DLRGDALDDT ADSSVYASPL ASSPLRKNLF RFGESTSGFS FSFQPGISPS KSPAKLNQSR
ASVGTDDEQE VTQDEERDGQ YFEPVVPLPD LVEVSTGEEN EQAVFSHRAK LYRFDKDLGQ
WKERGIGDLK ILQNFDTKRV RLIMRRDQVL KLCANHWISE AMKLEPMKGA EKAWVWSAMD
FSEDGEGKIE QLAVRFKLQE TANTFKQAFE DSKVAQAKAE LMTPVVSRLA APKDATPPGF
PSSPVCGSAA IAVLEETTKE RTEPPPDAKP FAAAPQSPVN PSKTVVSPPK FVFGTDSLQK
IFGTLKSQPE ASTPAGKAKD PGSSVKSPLP APAFQMHTGS AEAAADGSRL EDDSEVEVLF
VKEPTAEQAA LARKLLLPLT FFCYKNEPGY TSDTETDDED FESAVKALNG KLYPDSPQAA
ASDSESFCQF VWEKRPTPEE EEKAKSLQLP PTFFCGLSTS DSDTDHDKPE DFETEVRKAQ
HELASESKKA EKRWSRPAAA PQGPSSVPAS SCPEAAAATT AAEEPTADQP TGSRSSSSPI
DLSTKKSSEP EPGSVADTST TASAAQDSTF GFNSLTGFSF ADLAKTTEGF AFGSKDSDFS
WANAGAMVFK PAAPCEPKTK TDDGSDEEEA PTNVDIHFEP IVSLPEVETK SGEEDEEILF
KERAKLYRWD RDSSMWKERG IGDLKILFHP NKRFYRILMR REQVLRVCAN HTIIQGMELK
PLNTSTNALV WTATDYADGE GVVEQLAAKF KTPEIAETFK KTFCECQSRM SQDDGDASCA
SSPQMSRVQE HSRETNPQVF LKVAVDGKPL GSITIELFSH IVPKTAENFR ALCTGEKGFG
FQNSIFHRII PDFMCQGGDI TNNNGTGGKS IYGSSFEDEN FDVRHTGPGI LSMANRGRDT
NNSQFFITLK KAEHLDFKHV AFGWVRDGMD VVQQMGEMGT KAGIPSKKLV ITECGQL
//
