ID CAF4_YEAS7 Reviewed; 645 AA.
AC A6ZZZ8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=CCR4-associated factor 4;
GN Name=CAF4; ORFNames=SCY_3408;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Involved in mitochondrial fission. Has a partially redundant
CC function to MDV1 in acting as an adapter protein, binding to FIS1 on
CC the mitochondrial outer membrane and recruiting the dynamin-like GTPase
CC DNM1 to form mitochondrial fission complexes. Plays a key role in
CC determining the polarized localization of those DNM1 clusters that are
CC not immediately involved in the mitochondrial fission process (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DNM1, FIS1 and MDV1, components of the
CC mitochondrial fission machinery. Interacts via its WD repeats with
CC DNM1. Interacts with CCR4 and NOT1, components of the CCR4-NOT complex.
CC It is however not a component of the 1.0 MDa CCR4-NOT core complex, but
CC appears to be part of a less characterized, 1.9 MDa CCR4-NOT complex.
CC Interacts with DBF2, another likely component of the 1.9 MDa complex.
CC Interacts with SRB9 and SRB10, components of the SRB8-11 complex (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Uniformly distributed on the cytoplasmic face of
CC the mitochondrial outer membrane. This localization is dependent on
CC FIS1. Reorganizes to punctate structures on mitochondria, corresponding
CC to mitochondrial constriction sites, at a late step in mitochondrial
CC division (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN59941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFW02000152; EDN59941.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A6ZZZ8; -.
DR SMR; A6ZZZ8; -.
DR HOGENOM; CLU_012350_1_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000266; P:mitochondrial fission; IEA:InterPro.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 6.10.250.1070; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR021653; Caf4.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19857:SF8; ANGIO-ASSOCIATED MIGRATORY CELL PROTEIN; 1.
DR PANTHER; PTHR19857; MITOCHONDRIAL DIVISION PROTEIN 1-RELATED; 1.
DR Pfam; PF11615; Caf4; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Coiled coil; Membrane; Mitochondrion; Mitochondrion outer membrane; Repeat;
KW WD repeat.
FT CHAIN 1..645
FT /note="CCR4-associated factor 4"
FT /id="PRO_0000330093"
FT REPEAT 319..359
FT /note="WD 1"
FT REPEAT 362..402
FT /note="WD 2"
FT REPEAT 424..463
FT /note="WD 3"
FT REPEAT 481..528
FT /note="WD 4"
FT REPEAT 529..568
FT /note="WD 5"
FT REPEAT 570..605
FT /note="WD 6"
FT REPEAT 616..645
FT /note="WD 7"
FT REGION 1..274
FT /note="Required for interaction with FIS1 and MDV1"
FT /evidence="ECO:0000250"
FT REGION 74..126
FT /note="Sufficient for interaction with FIS1"
FT /evidence="ECO:0000250"
FT REGION 242..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..253
FT /evidence="ECO:0000255"
FT COMPBIAS 242..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 73150 MW; 73F1DA5C660217DD CRC64;
MGSGDTRGES SLVAKPIEII LNKLPHAILA QQQFQKYITS PIYRYLSKLL LFREVAWPES
TKDTQKGQVG IFSFQNNYAD SATTFRILAH LDEQRYPLPN GAAEKNLPSL FEGFKATVSI
IQQRLLLDNV DGATNSDKEK YVQLPDINTG FVNKTYSRID LTHLLEDVET NVENLSINKT
LEMDELTRLD SMINELESRK LKILERVKHI DSKSTNLEND VTLIKDRINF IEEYSLEADR
EQSLRKQMEE ERSSEASSFT QNEEAISSLY DVESKDTRLK DFYKMPHEKS HDKNRQMHII
SETYSRNSTA FRMTIPHGEH GNSITALDFD TPWGTLCSSS YQDRIVKVWD LNHGIQVGEL
PGHLATVNCM QIDKKNYNML ITGSKDATLK LWDLNLSREL YLDHSPLKEK TEEIVTPCIH
NFELHKDEIT ALSFDSEALV SGSRDKKIFH WDLTTGKCIQ QLDLIFTPTH SDIKMPARSL
NNGTCLLGTE APMIGALQCY NSALATGTKD GLVRLWDLRV GKPVRLLEGH TDGITSLKFD
SEKLVTGSMD NSVRIWDLRT SSILDVIAYD LPVSSLDFDG KLITVGANEG GVNVFNMERD
EHWMTPEPPH SLDGDELSRR IAIVKYKDGF LINGHNDGDI NVWTL
//
