FBX43_MOUSE
ID FBX43_MOUSE Reviewed; 640 AA.
AC Q8CDI2; Q4G0C8; Q8R0R1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=F-box only protein 43;
DE AltName: Full=Endogenous meiotic inhibitor 2;
GN Name=Fbxo43; Synonyms=Emi2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and Eye;
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 [3]
RP TISSUE SPECIFICITY, INTERACTION WITH CDC20, AND FUNCTION.
RX PubMed=16456547; DOI=10.1038/sj.emboj.7600953;
RA Shoji S., Yoshida N., Amanai M., Ohgishi M., Fukui T., Fujimoto S.,
RA Nakano Y., Kajikawa E., Perry A.C.F.;
RT "Mammalian Emi2 mediates cytostatic arrest and transduces the signal for
RT meiotic exit via Cdc20.";
RL EMBO J. 25:834-845(2006).
CC -!- FUNCTION: Required to establish and maintain the arrest of oocytes at
CC the second meiotic metaphase until fertilization. Probably acts by
CC inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin
CC ligase. Probably recognizes and binds to some phosphorylated proteins
CC and promotes their ubiquitination and degradation.
CC {ECO:0000269|PubMed:16456547}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with CDC20 (Probable). {ECO:0000250,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q8CDI2; Q9JJ66: Cdc20; NbExp=2; IntAct=EBI-8060482, EBI-2551389;
CC -!- TISSUE SPECIFICITY: Present in testis and ovary (at protein level).
CC Expression is high in immature oocytes, and diminishes after oocyte
CC activation. {ECO:0000269|PubMed:16456547}.
CC -!- PTM: Phosphorylated on Thr-176 and Ser-275 in response to calcium,
CC which is a prerequisite for ubiquitination and proteasomal degradation.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated in response to calcium, which promotes proteasomal
CC degradation. {ECO:0000250}.
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DR EMBL; AK030012; BAC26733.1; -; mRNA.
DR EMBL; BC026503; AAH26503.1; -; mRNA.
DR EMBL; BC098484; AAH98484.1; -; mRNA.
DR PDB; 2RT9; NMR; -; A=565-616.
DR PDB; 5DMS; X-ray; 1.90 A; B/D=169-177.
DR PDB; 5DMV; X-ray; 2.50 A; D=146-177.
DR PDBsum; 2RT9; -.
DR PDBsum; 5DMS; -.
DR PDBsum; 5DMV; -.
DR AlphaFoldDB; Q8CDI2; -.
DR BMRB; Q8CDI2; -.
DR SMR; Q8CDI2; -.
DR IntAct; Q8CDI2; 1.
DR MINT; Q8CDI2; -.
DR STRING; 10090.ENSMUSP00000054125; -.
DR iPTMnet; Q8CDI2; -.
DR PhosphoSitePlus; Q8CDI2; -.
DR PaxDb; Q8CDI2; -.
DR PRIDE; Q8CDI2; -.
DR ProteomicsDB; 272968; -.
DR MGI; MGI:1926053; Fbxo43.
DR eggNOG; ENOG502QRSQ; Eukaryota.
DR InParanoid; Q8CDI2; -.
DR PhylomeDB; Q8CDI2; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; Fbxo43; mouse.
DR PRO; PR:Q8CDI2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CDI2; protein.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140013; P:meiotic nuclear division; IMP:MGI.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IMP:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IGI:MGI.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IBA:GO_Central.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044064; ZF_ZBR.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 1.
DR PROSITE; PS51872; ZF_ZBR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Meiosis; Metal-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..640
FT /note="F-box only protein 43"
FT /id="PRO_0000247234"
FT DOMAIN 423..480
FT /note="F-box"
FT ZN_FING 568..616
FT /note="ZBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT REGION 328..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4G163"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G163"
FT CONFLICT 332
FT /note="G -> GS (in Ref. 2; AAH98484)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="Q -> R (in Ref. 2; AAH98484)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="R -> P (in Ref. 1; BAC26733)"
FT /evidence="ECO:0000305"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:2RT9"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:2RT9"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:2RT9"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:2RT9"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:2RT9"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:2RT9"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:2RT9"
SQ SEQUENCE 640 AA; 71171 MW; D23850243AC73E52 CRC64;
MDSSAVTVKG LSLIDFCSTS SFKYRGHHEL SESCSLNKKE EEPMLTCEHP ETPSLGSPNS
AVSPSQIMKS VSLRKEKDKS PELCETPKLR RKKCTLRRRL DFSFPLLKGD SDSQSRSLES
NISQGVSLEK HLPGSTSGFP KEDNFSPLVT STIKTEDVVS NSQNSRLHFS QHKTSTIEDS
KDNCGLFEVE CLSPIEGNDF KDSITHFSDS SLSVSDENTC PELLGSCGSQ TTYGADVTTS
VTPVSSLIAK IKFNGNQTLD SSGEVRDSLF TPEDSGFCSL SWDKSEDFLS DQEGSFQELL
QKHRVTPKVG DQVKKPKHFG RLRRLSTLQE QGQSEDEMQT VHPNSDSGVL ESLQGSEEKR
GNLALSFKDL SNTPALQLVQ ELFMKSKRKR SQQEDDQEFF EDRDEGKIAR LQRVLAGLIG
KKMGIEQLDI LTELQYRNLK HILAMVLESL TSESLYSAWN VSRNWREIVA QDKKANRRRK
LYIIQLRASA QGAAVLRVQD AATRLCLLSR LALRSVQAQA QAPSGEQVPT LSPWGDVLTP
VASSSLTHLR SKQEQYVKVA RTLFTDEALK PCPRCQSPAK YQPHKKRGLC SRLACGFDFC
VLCLCAYHGS EDCRRGSAKA RGSKDVLPGS AQSKRNLKRL
