KCMF1_MOUSE
ID KCMF1_MOUSE Reviewed; 381 AA.
AC Q80UY2; Q9WUM2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=E3 ubiquitin-protein ligase KCMF1;
DE EC=2.3.2.27;
DE AltName: Full=Differentially expressed in branching tubulogenesis 91;
DE Short=Debt-91;
DE AltName: Full=RING-type E3 ubiquitin transferase KCMF1 {ECO:0000305};
GN Name=Kcmf1; Synonyms=Debt91;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12810064; DOI=10.1016/s0006-291x(03)00875-1;
RA Li Z., Stuart R.O., Eraly S.A., Gittes G., Beier D.R., Nigam S.K.;
RT "Debt91, a putative zinc finger protein differentially expressed during
RT epithelial morphogenesis.";
RL Biochem. Biophys. Res. Commun. 306:623-628(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC ubiquitination. {ECO:0000250}.
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;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80UY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UY2-2; Sequence=VSP_035227;
CC -!- TISSUE SPECIFICITY: Testis, liver, kidney, heart and skeletal muscle.
CC {ECO:0000269|PubMed:12810064}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development, with
CC much higher expression after day 15, when many organs including the
CC kidney are undergoing extensive branching morphogenesis.
CC {ECO:0000269|PubMed:12810064}.
CC -!- INDUCTION: Up-regulated during growth factor-induced branching
CC tubulogenesis. {ECO:0000269|PubMed:12810064}.
CC -!- SIMILARITY: Belongs to the KCMF1 family. {ECO:0000305}.
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DR EMBL; AF143859; AAD31040.1; -; mRNA.
DR EMBL; AK142436; BAE25063.1; -; mRNA.
DR EMBL; BC043330; AAH43330.1; -; mRNA.
DR CCDS; CCDS39518.1; -. [Q80UY2-1]
DR RefSeq; NP_062689.2; NM_019715.2. [Q80UY2-1]
DR AlphaFoldDB; Q80UY2; -.
DR SMR; Q80UY2; -.
DR BioGRID; 216636; 1.
DR IntAct; Q80UY2; 1.
DR STRING; 10090.ENSMUSP00000064410; -.
DR iPTMnet; Q80UY2; -.
DR PhosphoSitePlus; Q80UY2; -.
DR SwissPalm; Q80UY2; -.
DR EPD; Q80UY2; -.
DR jPOST; Q80UY2; -.
DR MaxQB; Q80UY2; -.
DR PaxDb; Q80UY2; -.
DR PeptideAtlas; Q80UY2; -.
DR PRIDE; Q80UY2; -.
DR ProteomicsDB; 263490; -. [Q80UY2-1]
DR ProteomicsDB; 263491; -. [Q80UY2-2]
DR Antibodypedia; 31781; 143 antibodies from 18 providers.
DR DNASU; 74287; -.
DR Ensembl; ENSMUST00000068697; ENSMUSP00000064410; ENSMUSG00000055239. [Q80UY2-1]
DR GeneID; 74287; -.
DR KEGG; mmu:74287; -.
DR UCSC; uc009cjd.1; mouse. [Q80UY2-1]
DR CTD; 56888; -.
DR MGI; MGI:1921537; Kcmf1.
DR VEuPathDB; HostDB:ENSMUSG00000055239; -.
DR eggNOG; KOG1280; Eukaryota.
DR GeneTree; ENSGT00510000047171; -.
DR HOGENOM; CLU_032080_1_1_1; -.
DR InParanoid; Q80UY2; -.
DR OMA; TTRHLTD; -.
DR OrthoDB; 1107794at2759; -.
DR PhylomeDB; Q80UY2; -.
DR TreeFam; TF318128; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 74287; 19 hits in 72 CRISPR screens.
DR ChiTaRS; Kcmf1; mouse.
DR PRO; PR:Q80UY2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80UY2; protein.
DR Bgee; ENSMUSG00000055239; Expressed in spermatid and 235 other tissues.
DR ExpressionAtlas; Q80UY2; baseline and differential.
DR Genevisible; Q80UY2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
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; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
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; IPR013087; Znf_C2H2_type.
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; SM00355; ZnF_C2H2; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT CHAIN 2..381
FT /note="E3 ubiquitin-protein ligase KCMF1"
FT /id="PRO_0000349220"
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 154..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..259
FT /evidence="ECO:0000255"
FT COMPBIAS 169..193
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12810064"
FT /id="VSP_035227"
SQ SEQUENCE 381 AA; 41791 MW; 4A15FC5CF60CF246 CRC64;
MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD
FDLYYGGEAF SVEQPQSFTC PYCGKMGYTE TSLQEHVTSE HAETSTEVIC PICAALPGGD
PNHVTDDFAA HLTLEHRAPR DLDESSGVRH VRRMFHPGRG LGGPRARRSN MHFTSSSTGG
LSSSQSSYSP SSREAMDPIA ELLSQLSGVR RSAGGQLNSS GPSASQLQQL QMQLQLERQH
AQAARQQLET ARNASRRTNT SSVTTTITQA TATANTANTE NSPQALHNSQ FLLTRLNDPK
MSEAERQSME SERADRSLFV QELLLSTLVR EESSSSDEDD RGEMADFGAM GCVDIMPLDV
ALENLNLKES NKGNEPPPPP L
