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CAF4_YEAS7
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   03-AUG-2022, entry version 60.
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   PRIDE; A6ZZZ8; -.
DR   EnsemblFungi; EDN59941; EDN59941; SCY_3408.
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   Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF11615; Caf4; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 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
 
 
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