FBX43_RAT
ID FBX43_RAT Reviewed; 664 AA.
AC Q66H04;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=F-box only protein 43;
DE AltName: Full=Endogenous meiotic inhibitor 2;
GN Name=Fbxo43; Synonyms=Emi2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC Interacts with CDC20 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on Thr-190 and Ser-289 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; BC082107; AAH82107.2; -; mRNA.
DR RefSeq; NP_001012117.2; NM_001012117.1.
DR RefSeq; XP_006241597.1; XM_006241535.3.
DR AlphaFoldDB; Q66H04; -.
DR BMRB; Q66H04; -.
DR STRING; 10116.ENSRNOP00000014333; -.
DR iPTMnet; Q66H04; -.
DR PhosphoSitePlus; Q66H04; -.
DR PaxDb; Q66H04; -.
DR Ensembl; ENSRNOT00000014333; ENSRNOP00000014333; ENSRNOG00000010459.
DR GeneID; 315034; -.
DR KEGG; rno:315034; -.
DR UCSC; RGD:1310225; rat.
DR CTD; 286151; -.
DR RGD; 1310225; Fbxo43.
DR eggNOG; ENOG502QRSQ; Eukaryota.
DR GeneTree; ENSGT00530000063692; -.
DR HOGENOM; CLU_029091_0_0_1; -.
DR InParanoid; Q66H04; -.
DR OMA; WKVSKNW; -.
DR OrthoDB; 521317at2759; -.
DR PhylomeDB; Q66H04; -.
DR TreeFam; TF101170; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q66H04; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000010459; Expressed in testis.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; ISO:RGD.
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 2: Evidence at transcript level;
KW Meiosis; Metal-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..664
FT /note="F-box only protein 43"
FT /id="PRO_0000247235"
FT DOMAIN 445..502
FT /note="F-box"
FT ZN_FING 592..640
FT /note="ZBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 614
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT BINDING 637
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01220"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4G163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G163"
SQ SEQUENCE 664 AA; 73228 MW; AE73B4502F03C0E2 CRC64;
MPQKHSASHR AGSNMGSSAV TVRCPSLPDF GPTSSFKHRG PHELSETCSF SKKEKDPMLT
CEHLETPRLG FPNPAVSPSP RKKSVSLRKE KEESPELCET PKLRRKKCTL RRRLDLTLTL
LKGDSDSQSS SLESNISHSL SLEKRLRDST SGFPKEDNFS PLVTSTVKTE DAISSSQNSR
LHFSQHKTST IDDSKDDCGL FEVECLSPIE GNDFKDSVTH FSDSGLSASD ENTCPELLGS
SGSQTTYGAD VTTSVTPVSS LIAKIKFHGS QTLASSAEVR DSLSTPEDSG FCSLSWDKSE
DFLSDQEGSF QELQKHRGTP TVGDLVRQPK HPGRLRRLPT LQEQGSQSET DDEMQVAHPS
AGVRVGTASG VLESQQGSEE KSGDLTLSFK DLSNTPALQL VCELFMKSKR KRFEQADDQE
FSEEREEGKI ARLQHVLAGL IGKKMGIERL DILTELQYRN LKHILAMVLD SLTAESLYSA
WNVSRNWRGI VAQDKRANRR RKLFIAQLKA KAQGAAVLRV QDAATRLRLL SRLALRSVQA
QAQAPNGQNE QAPAQSPWGE VLTPVASSSL THLRSKQEQY LKVARTLFTD EALKPCPRCQ
SPAKYQPHKK RGLCSRLACG FDFCVLCLCA YHGSEDCRRG SAKGRGSRDV LPGSAQSKRN
LKRL
