KCMF1_DROME
ID KCMF1_DROME Reviewed; 599 AA.
AC Q95RX5; Q0KI99;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase Kcmf1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305|PubMed:27552662};
GN Name=Kcmf1 {ECO:0000303|PubMed:27552662, ECO:0000312|FlyBase:FBgn0037655};
GN ORFNames=CG11984 {ECO:0000312|EMBL:AAF54323.3};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL28614.1, ECO:0000312|EMBL:AAN71238.1, ECO:0000312|EMBL:AAN71257.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ABC86284.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABC86284.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH POE.
RX PubMed=27552662; DOI=10.1371/journal.pbio.1002539;
RA Ashton-Beaucage D., Lemieux C., Udell C.M., Sahmi M., Rochette S.,
RA Therrien M.;
RT "The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the Function of
RT the N-end Rule ligase POE/UBR4 in Drosophila.";
RL PLoS Biol. 14:E1002539-E1002539(2016).
CC -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC ubiquitination. Involved in the negative regulation of the Ras/MAPK
CC signaling pathway in the wing by acting with the E2 enzyme Unc6 and the
CC putative E3 ligases poe and Ufd4 to mediate the ubiquitination and
CC proteasomal degradation of rl/MAPK. {ECO:0000269|PubMed:27552662,
CC ECO:0000305|PubMed:27552662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305|PubMed:27552662};
CC -!- SUBUNIT: Interacts with poe. {ECO:0000269|PubMed:27552662}.
CC -!- SIMILARITY: Belongs to the KCMF1 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF54323.3; -; Genomic_DNA.
DR EMBL; AE014297; AAF54324.3; -; Genomic_DNA.
DR EMBL; AE014297; AAF54325.3; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94857.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94858.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94859.1; -; Genomic_DNA.
DR EMBL; AY061066; AAL28614.1; -; mRNA.
DR EMBL; BT001502; AAN71257.1; -; mRNA.
DR EMBL; BT001483; AAN71238.1; -; mRNA.
DR EMBL; BT024222; ABC86284.1; -; mRNA.
DR RefSeq; NP_001163560.1; NM_001170089.1.
DR RefSeq; NP_001163561.1; NM_001170090.1.
DR RefSeq; NP_001163562.1; NM_001170091.1.
DR RefSeq; NP_649861.3; NM_141604.3.
DR RefSeq; NP_731305.2; NM_169252.2.
DR RefSeq; NP_731306.2; NM_169253.2.
DR AlphaFoldDB; Q95RX5; -.
DR SMR; Q95RX5; -.
DR IntAct; Q95RX5; 6.
DR STRING; 7227.FBpp0289967; -.
DR PaxDb; Q95RX5; -.
DR PRIDE; Q95RX5; -.
DR DNASU; 41082; -.
DR EnsemblMetazoa; FBtr0300743; FBpp0289967; FBgn0037655.
DR EnsemblMetazoa; FBtr0300744; FBpp0289968; FBgn0037655.
DR EnsemblMetazoa; FBtr0300745; FBpp0289969; FBgn0037655.
DR EnsemblMetazoa; FBtr0300746; FBpp0289970; FBgn0037655.
DR EnsemblMetazoa; FBtr0300747; FBpp0289971; FBgn0037655.
DR EnsemblMetazoa; FBtr0300748; FBpp0289972; FBgn0037655.
DR GeneID; 41082; -.
DR KEGG; dme:Dmel_CG11984; -.
DR UCSC; CG11984-RA; d. melanogaster.
DR UCSC; CG11984-RB; d. melanogaster.
DR CTD; 56888; -.
DR FlyBase; FBgn0037655; Kcmf1.
DR VEuPathDB; VectorBase:FBgn0037655; -.
DR eggNOG; KOG1280; Eukaryota.
DR GeneTree; ENSGT00510000047171; -.
DR HOGENOM; CLU_032080_2_0_1; -.
DR InParanoid; Q95RX5; -.
DR OMA; FMQPTFT; -.
DR OrthoDB; 785378at2759; -.
DR PhylomeDB; Q95RX5; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q95RX5; -.
DR BioGRID-ORCS; 41082; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 41082; -.
DR PRO; PR:Q95RX5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037655; Expressed in egg cell and 24 other tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IGI:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR039858; KCMF1.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12268:SF13; PTHR12268:SF13; 1.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..599
FT /note="E3 ubiquitin-protein ligase Kcmf1"
FT /id="PRO_0000442702"
FT ZN_FING 4..60
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 78..101
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 155..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 599 AA; 62398 MW; 0E8416FFFA785334 CRC64;
MSRHEGVSCD SCLKSNFNGR RYKCLICYDY DLCADCYEDG VTSTRHLVEH PMQCILTRSD
IELYFGGEML ASDQPQSFTC PYCKKMGFSD ATLLEHVSAE HTETSLEVVC PVCAGLPGGE
PNLVTDDFAG HLTLEHRQGP RELISFLDEP SAIRHGGGVR RIPGRTLGGP RTRRSNMHFS
SSSGLSALSP SGRESVDPIA ELLSQLSGVR RGGPPTSQLQ QLQMQMQLDR QQVTASRQID
RLPRRAHPIV STSNSNAAMA EVISGGAGGS GGSGAVGSGS GGGSGATAPP NLRTTEWPVT
ASFSTSASNH SQTQSSLAAN SLNAREAIGT SSSAGSNVLG ISVGVGGTAN GNGGAGSSGV
ATGAGGAGQG GGQGGAAAGE SFLLAQFMQP TFTEAEWAVV ESMRADRSMF VQSLMLSMLC
TEALDLNASD ESLAKSDNVN KGQQQQQEDA EAEAQAETLL NNNADVEQQQ QQQQLQPAMV
RQVNQMQQTS PEDFVCDEYR YKNKKANTTQ TSGTGGLGGA GATAAPGGGA SGAGTKPTAD
RGIERRSGRP PPGEMATGSQ QPQQQQQSTA NPAASQQKYK QNASAATAAG NTNQIPDTR
