ID A0A3P8SZI7_AMPPE Unreviewed; 3068 AA.
AC A0A3P8SZI7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=RAN binding protein 2 {ECO:0000313|Ensembl:ENSAPEP00000017467.1};
GN Name=RANBP2 {ECO:0000313|Ensembl:ENSAPEP00000017467.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000017467.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000017467.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000017467.1}
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 STRING; 161767.ENSAPEP00000017467; -.
DR Ensembl; ENSAPET00000017963.1; ENSAPEP00000017467.1; ENSAPEG00000012495.1.
DR GeneTree; ENSGT00940000154389; -.
DR OMA; TQCIACQ; -.
DR Proteomes; UP000265080; Chromosome 12.
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; cd14684; RanBD1_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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000265080};
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 1187..1323
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1351..1380
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1458..1487
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1523..1552
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1577..1606
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1616..1645
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1856..1992
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2152..2289
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2748..2883
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2911..3067
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 756..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2115..2149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2331..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2375..2408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2433..2456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2540..2577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2592..2678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2721..2749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 824..851
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 783..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2342..2356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2375..2389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2433..2451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3068 AA; 337937 MW; 0563552383325E7F CRC64;
MRRSKAEVDR YVSSVQSSSP SLKEKPVKGF LFAKLYFEAK EYELAKRHVS EYLKVQERDP
KAHKFLGQLY EREGDINKAV GCYKRSVDLN PAQRDLVLKV AELLVSKEEC DSRAEFWVEK
AAKLLPGNPA VFNLKERLLS RQGQQGWNRL FDLLQAELAA RPGDAHVNVK LVQLFCQDGR
LDEAVKHCLT AEKRGLLRHS LDWYTVVVHT LQEYLAQPSI SSNEKMCRRL QRELLLAHCS
LLRITLSESS VQPSLDALRG FDQAMQTLSS IAGHHTDDLG EVFVEMRGHL YLHSATLLLK
LAQDRQHTWR AVIDLAALCY LLAYQVPRPK PKVTKRDQSA PYLLELLAND RQSQSGHMLF
NLSTDSSALI REVVEAFGNR SGQDSLFELL WGPQASAGSS FIANDDIHSI TSMAPELSQL
AKWDTGSILL HSGDLQHLSW LGLQWTLLTQ RPALREWLQQ LFPRLTLETS KLDTNAPESI
CLLDLEVFLY GVVFCSHCQL QETAKISSGV NQQQQQQLYE PRCLPLPLLR LLTTDRQREW
WDAIYSLIHK RAAPGMSAKL RMIVQHGLNT LRAREKHGLQ PALAIHWAQC LSQTGDGVNS
YYDQKEYIGR SVHYWKIVLP LLEKIKNRRS IPEPLEPLFI HFPSKDIQIS SVKGYEEEAR
IAYAVLLDIE GRTEEAIATL ETINNMSSIW HLAQIYQRLS EEASNGVEET QDRCITFLRK
FRTYLSKIYS ANADDIEKLP VSMEEVVDRL NDVNQQLGES GEAMDEEDEK EEEGRRGPAH
SSPAHPTETS ATISHIKFST PSPNKSVISP SKRLISPKTP PHWVEDQKSL LQMLCQQVEA
LKNEVHDLRH NSSGNAGSPH KMYGESYGAE GLQEPFTPVQ SYHGAPLTVA TTGPSVFYNQ
STAYNSQYLL RTAANVTPTK GPMYSVNRMP PQQHMYAYQP PTHTPPLQTA PACIYPPQEQ
VFGAPLRFES PATNLLSPYS EEYYGQSVTQ QTTNPPLPEP GYFTKPSVVP VQPPKSVEGK
PMDFGKLSFS QQAPAEVPRV PSFGAGAVAQ STPSTAFKFN SNFKSNDGDF TFSASQAKHS
ESLLGLLTSD IPAKTDAVSE KQAAQEQPPS QTGIFTFGNK NITSFSFVDS AQTTASGSLF
GKVEQPFKFG DITKPAFEVA KPVAEQERAA ESDNDSTHIE EDEDGPHFEP IVPLPDKVDV
KTGEEEEEEM FCNRAKLYRF DTETKEWKER GIGNVKILKH STKGKVRLLM RREQVLKICA
NHYITADMLL KPNAGSDKSW VWNAIDYADE EPKPEQLAIR FKTVDEASLF KAKFEEAQKI
VLKSPEEHNQ QERKEESLKE SESLAAQFAL KEGEWECAVC CVRNASTDMR CLACQSPNPK
SSSKPDIQPA GETKASPFTF KFGTDSSKPS SSGSMFTGFG AFGASVPSSF TFGISSSKPA
DTGTSAFGCD FGAQFAKKPG QWNCETCSAR NEASAGSCVS CKALKTSTVT TATAQTTPAA
DAPVVQPSIS TVDTGFGAQF SKKPGQWDCD VCEIRNEASV NKCVACKSPN PAAKSTEGAP
VASNLSAESG LGAFAKKDGQ WDCNTCLVRN DASAAECVSC HAPNENPSLE AMFAKKDGEW
DCDICLVRND ASANKCAACQ TPNPNAKSTS NTAPSPSSFS FVFGTKSSSS QSAGTGFTMP
FVSGSTFQFG ENKDKNSAAS FKFEASQSGS STAASSGFSF SMPNPAGGFK FGIQEPAQES
PSNDNQTPPG PASSFLKSIA DKHKEEKSFS APSVGQTDQD QNPLVAGKTN TFSFADLAKS
SGGDFQFGEK DPDFKGFSRA GEQVFSSFQA TPTKAEASNE LEDDDMYKTE ESDDIQFEPV
VQMPEKVDLV TGEEDEQVLY SQRVKLFRFD SNTSQWKERG VGTLKFLKNN SNGRLRVLMR
REQVLKVCAN HWITTTMNLK PLAGSDKAWI WMANDFSDGD AKLEQLAAKF KSPELAEEFK
EKFEECQRLL LDIPLQTPHK LVDTGRTAHL IQKAEEMKSG LKDLKSFLTD EKTKIKDDDT
QGDITTSSDV SSLVIKPHGE TTGPTLEWDN YDLREEALDD TANSSVYASP LASSPLRKNL
FRFGESTGGF SFSFQPGISP AKSPSKLNQS RASVGTDDEQ DVSQDEERDG QYFEPVVPLP
DLVDISTGEE NEQVVFSHRA KLYRYDKELT QWKERGIGDL KILQNYETKR VRLIMRRDQV
LKICANHWIT AAMKLEPMKG AEKAWVWSAM DFAEEGKGNI EQLAVRFKLQ DTANTFKEVF
EEAKIAQDKK ELMNPVTSRV PAPQDGGTAG SATIAATVCG KAAIAVLEET TKERTELSPD
TRPCAAGSQS PVNPTKAVVS PPKFVFGTDS LQKIFGTPKS PSESDGSASV LKARDSGRHA
TASPAAPAFK IPDKGLDFRL FKDNPMAFWT STSTTQFEPQ GPPQAEGNSA GSDEDSEVEV
VYVREPTAEQ AALARKLLLP LTFFCYQNEP GYTSDDQTDD EDFESAVAAL NGKLYPDPPE
KKAAACADEP DCQVVWEKKP TPEEEEKAKR LQLPPTFFCG LSTTDSDPDH DKPEDFETEV
RKAQEVLVAQ LNQAEQASSS PAEAAAEPTP GLSSSSVEAA GSTSARDEQT SDQPAETQSE
AHSSSSPIDL STKKSSEPES NTETDAAAST ATTTSQDSTF GFNSLGGFSF ADLAKNTEGF
AFGTNDSNFS WANAGATVFG SVGPSAPKNT ADEEGSDEEE ASNNVDIHFE PIVSLPEVET
KSGEEDEEIL FKERAKLYRW DRDLGQWKER GIGDLKILFH PTKHFYRILM RREQVLRVCA
NHTISPAMEL KPMNASANAL LWTATDYSDG DGVVEQLAAK FKTPEIAETF KKTFCECQSR
VGQSGDDASC ISSPQMSRVQ EHSRETNPQV FLTVAADGQP LGTVTIELFS HIVPKTAENF
RALCTGEKGF GLKDSIFHRV IPDFMCQGGD ITNSDGTGGK SIYGSQFEDE NFDVRHTGPG
ILSMANRGRD TNNSQFFITL KKAEHLDFKH VAFGWVRDGM EVVQQMGELG TKGGLPSKKF
VITDCGQL
//
