ID A0A6J2U249_DROLE Unreviewed; 2931 AA.
AC A0A6J2U249;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE SubName: Full=Microtubule-associated protein futsch isoform X8 {ECO:0000313|RefSeq:XP_030381217.1};
GN Name=LOC115629049 {ECO:0000313|RefSeq:XP_030381217.1};
OS Drosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Scaptodrosophila.
OX NCBI_TaxID=7225 {ECO:0000313|Proteomes:UP000504634, ECO:0000313|RefSeq:XP_030381217.1};
RN [1] {ECO:0000313|RefSeq:XP_030381217.1}
RP IDENTIFICATION.
RC STRAIN=11010-0011.00 {ECO:0000313|RefSeq:XP_030381217.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_030381217.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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 RefSeq; XP_030381217.1; XM_030525357.1.
DR GeneID; 115629049; -.
DR Proteomes; UP000504634; Unplaced.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:1990450; F:linear polyubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR CDD; cd19815; Bbox1_HOIP; 1.
DR CDD; cd20337; BRcat_RBR_HOIP; 1.
DR CDD; cd16631; mRING-HC-C4C4_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047543; Bbox1_RNF31-like.
DR InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047542; Rcat_RBR_RNF31-like.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR032065; RNF31-UBA.
DR InterPro; IPR041031; RNF31_C.
DR InterPro; IPR047541; RNF31_RBR_mRING-HC-like.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE LUBEL; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF16678; UBA_HOIP; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000504634};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 2549..2779
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2553..2602
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1784..1973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1990..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2040..2118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2251..2362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..55
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..316
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..409
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..501
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..552
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..700
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..863
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1551
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1933
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2004
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2092
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2291..2331
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2931 AA; 325308 MW; B6D46BB39603BDE5 CRC64;
MTTQQLLNKN VRTMPKWVTE ANERIGPKPP PTPPNGAATT NGTTPKAPAL PPKTKNQPEP
DYEVIEFSNQ QYSNEPMKTT VIRTKTPENK LKCTLCGSQN PWVTCGECSG QLFCASCDDM
FHKHPKRKNH VRKAVEQGTP PIPPKAQAGG APPVAPPRRG KRGLLTPFLG RKEQTQTTGT
PPLPPPSPTP SQKSSSWRGL MMNSRPLPDP PKPTPSEGGG SSRSGTPKSV FDNIQRPPSV
QLEKIKSKAS ATLDRMAILQ QRYRQHKAQQ ELGGSRSDVA SDQLLPNGGT FEHWSNISPS
PSHFRSGSMS SGLNSSHFDL SDDSHNFHNS LLFQQQQRQA AGAQRRQMST SVFNLNSLNR
RPPTEMQSNG AWLANQPMQQ AQSMAQLNCA GCQTRQQPGW PQQPRQQPHM HQHPDDWSQF
GSQQQFNHSN LSLNMGPGYL PQQHQHYPPP VFMTQRGIMP NMYPQGYPVM HPGVMGMPPV
AASRAASRPR YAASPTPSRK SLSMRRKRSS YVDDELTDDE DSDQDDRRSM VSNRSGMTSA
SRAHQHHQRQ RRLSSASQFI NNGNDDIDSE QRHGPRRRDR RGSIAKSVQS EWLPERRDSS
AGGGTLKRQT EPQKPSRIYS DLESEGSAAR ALVQAKIQQK LKETEPHKAK KTEAKPKREM
KDENTQAAAV VQKVPHRENT TAPAPAGSSE SEEEYEEVVE EVSQSESETE QSKPAPELIP
TQATNGPENA AEVEADGDDL GPPPSTPDHE WECEFCTFVN ESNIKICAIC CKTPSKPPEK
PKSKTTPTAA KVEPKPATTA AIQVSATPKP EVKLVRKSSM KSSKPIEKPS STTSTVNNHK
ATTSTSSTNT SAKAAAKPAT TATGESASAL AKGFIHKDSV ENIWNTLDES IQAQAEQVLK
QAQKVSTGCG GTPPRELPTA EEAREAREMG TSPPPQSIST QTYDALPFRR ESVPAQTEEP
TAVPQERFRT PEPPKMERRP YYRSSSQLQQ ENDRYRSSND LRYNNEGYGA LEHYNASQWT
KRPNFISDLK TLQHQTSSPF DLPHEPFAYK HEPARDPETE LHIILKELEL YKFTVEELEA
ALKYCGPETH PIQWLRENWH KLVSTVQSLA TKYGQERAEN TIGTVSQNEA REALRSSSGN
VWQAVADCIQ QRQQKFRKLS SKGNFLRDDI VNALTAHQDI QDFLNTHALD CLQPPQAAGE
SPAIANPFDA PYIDDIDHSP SKSAYATPSP YQLEDSTLKN LEILIGNMEQ NQAKQNQEVL
RSIETMLETF KGKPEQDYET DPEVMRILTK SPISAPKAPL LVEDRSTDDV KNFVWQHIQE
IVPNLVQQVE QELMERPEGQ QTDEVPEVPV VKVPTPPPVD PSIYIMEEVI KPNLREASIR
EELPPNFIYA TEIANFKLEF DRGSETTHQP EWEPDDLNDA DNIVYMSYLA PKEVAAESKE
SPQKLPQAET LEDQSPNKAA AETTTSQIES ENGTKTIKDI NTPEVLTTES PAAITTETMK
ASLQSEIIAG EKTKSNDIPT DNHAVQEDDK PSTSREANRR NKRSQLPRKG RTRDQSQKPT
NRTKLSKGIT DKKKESNTDN AEKPGESSTN DVESLQTDEP KDTPRQTEIN ESAQTKSDET
ANNEIVELQT DSQVETQAVL NETETDTLAK IVQHTPTGEV PLVKVEPVQE VQVGDAVEAV
PEIVQHIPVV EAPLIKAEPL PEVQVGDGVE AVPAQIKPLQ EPQKTEPIES NSVPNEITEN
SEVLPPHTDS VDIVTEEIKM IEAEAQSRAD EPALDSQEQI FIEDEVPASE VRPTANNVPE
PITDSQLASN EVSEIQEEET PTSVAAVERK RSPKRFSKIP VRTQSTNSLR SESKVNKQVP
TTSGTQEHNE NADTTAEETA AEETTQTQHE DRSLETIQSN AKPITSMVEP VPSISTPAAI
SPVESEEVFE DAAEFSSTEE VRAQDEVTSE AELYSLDSDE QTTEQRDNTR SPESEVLLVL
NSAEVAQEST IAKSTSSATV NSHSSHSDST KMVLKEFIPS GDPSKQNLSE LVEDTQRLIK
QMREEISMDE FESTDDDYSE DYSDEYDEGE EEEWYDSEGD EEGDYDDEDG TTYDEQTPFI
EDASSGAARL ENGEEEGTEI EDILEETENE DDEEETGQAP HETVMTTSIA TSTNHEPVVH
ELTEIVSPTV LDAVITAMIP TASETIDGVP TTQVMETAET VANSSTLPAV EVINMVEPNA
LPIVPEPVIA DSESRPAEMP ADIVLEAQQP EEQTVDESNA LPITSPPPIA DSESRPMELP
TETVLEEPKK VTPTTTNNKQ KTNKKANNTE GSSTSKSSTT VNKTTKSTAS KIPKPTNEPN
TTLVNKKVPL RSKSFSGPPT PMGISSVKRI QQEYLQKQGL SSTGPTHSRV PTFVPKKTIS
DAINKFNKPT TDGPSTSSAA AAAVNALFKT RTQPRIPKKK YHETCFSDDD YETSTAEEDT
SDDLASAPTK AELLQRKLSI PVFRAYPSVQ EQVIEDPAVL ARKYVDQDLV SNIAEAQIAA
TLVNMKFQED VALWAAKECS DLDQAIAMLQ QECELCMNMY PMNQIVSMLK CTHKCCKQCA
KSYFTVQITD RSINDCSCPY CKLPELSSES LHEDDHLEYF SNLDIFLKNI LDSDVHELFQ
RKLRDRTLLQ DPNFKWCIQC SSGFFARPKQ KRLICPDCGS VTCAQCRKPW EKQHEGSSCE
AYLEWKRVND PELQAQGVQE HLAQHGIDCP KCKFRYSLAR GGCMHFTCTQ CKFEFCYGCA
RPFMMGAKCN VSSYCAKLGL HAHHPRNCLF YLRDKIPMQL QFLLKEQNVS FDTVAIELRD
EPSSSATARA SARCPIPLQK ETPQGLVDTV CNSEVPEKHA GMCRTHYVEY LAAKVAKAGI
DPLPIFDLTD CVQELRRRGI ALPERGPWDT DEIYKNMCSE VIKKNIPLKS A
//
