CAF4_YEAST
ID CAF4_YEAST Reviewed; 643 AA.
AC P36130; D6VX99;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=CCR4-associated factor 4;
GN Name=CAF4; OrderedLocusNames=YKR036C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 94-95.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INTERACTION WITH CCR4; DBF2; NOT1; SRB9 AND SRB10, AND SUBUNIT.
RX PubMed=11113136; DOI=10.1074/jbc.m009112200;
RA Liu H.-Y., Chiang Y.-C., Pan J., Chen J., Salvadore C., Audino D.C.,
RA Badarinarayana V., Palaniswamy V., Anderson B., Denis C.L.;
RT "Characterization of CAF4 and CAF16 reveals a functional connection between
RT the CCR4-NOT complex and a subset of SRB proteins of the RNA polymerase II
RT holoenzyme.";
RL J. Biol. Chem. 276:7541-7548(2001).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP FUNCTION IN MITOCHONDRIAL FISSION, INTERACTION WITH DNM1; FIS1 AND MDV1,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16009724; DOI=10.1083/jcb.200503148;
RA Griffin E.E., Graumann J., Chan D.C.;
RT "The WD40 protein Caf4p is a component of the mitochondrial fission
RT machinery and recruits Dnm1p to mitochondria.";
RL J. Cell Biol. 170:237-248(2005).
RN [9]
RP FUNCTION IN MITOCHONDRIAL FISSION.
RX PubMed=16835275; DOI=10.1242/jcs.03026;
RA Schauss A.C., Bewersdorf J., Jakobs S.;
RT "Fis1p and Caf4p, but not Mdv1p, determine the polar localization of Dnm1p
RT clusters on the mitochondrial surface.";
RL J. Cell Sci. 119:3098-3106(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 65-124, INTERACTION WITH FIS1,
RP MUTAGENESIS OF 85-PHE-ARG-86; LEU-88; LEU-110; PHE-111 AND PHE-114, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17998537; DOI=10.1073/pnas.0706441104;
RA Zhang Y., Chan D.C.;
RT "Structural basis for recruitment of mitochondrial fission complexes by
RT Fis1.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18526-18530(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.
CC {ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16835275}.
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.
CC {ECO:0000269|PubMed:11113136, ECO:0000269|PubMed:16009724,
CC ECO:0000269|PubMed:17998537}.
CC -!- INTERACTION:
CC P36130; P40515: FIS1; NbExp=4; IntAct=EBI-26394, EBI-25059;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:17998537}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16009724,
CC ECO:0000269|PubMed:17998537}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:17998537}.
CC Note=Uniformly distributed on the cytoplasmic face of the mitochondrial
CC outer membrane. This localization is dependent on FIS1. Reorganizes to
CC punctate structures on mitochondria, corresponding to mitochondrial
CC constriction sites, at a late step in mitochondrial division.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z28261; CAA82110.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006944; DAA09189.2; -; Genomic_DNA.
DR PIR; S38108; S38108.
DR RefSeq; NP_012962.3; NM_001179826.2.
DR PDB; 2PQR; X-ray; 1.88 A; C/D=65-124.
DR PDBsum; 2PQR; -.
DR AlphaFoldDB; P36130; -.
DR SMR; P36130; -.
DR BioGRID; 34167; 124.
DR DIP; DIP-5945N; -.
DR IntAct; P36130; 30.
DR MINT; P36130; -.
DR STRING; 4932.YKR036C; -.
DR iPTMnet; P36130; -.
DR MaxQB; P36130; -.
DR PaxDb; P36130; -.
DR PRIDE; P36130; -.
DR EnsemblFungi; YKR036C_mRNA; YKR036C; YKR036C.
DR GeneID; 853908; -.
DR KEGG; sce:YKR036C; -.
DR SGD; S000001744; CAF4.
DR VEuPathDB; FungiDB:YKR036C; -.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00940000176613; -.
DR HOGENOM; CLU_012350_1_0_1; -.
DR InParanoid; P36130; -.
DR OMA; GVRMWDM; -.
DR BioCyc; YEAST:G3O-32008-MON; -.
DR EvolutionaryTrace; P36130; -.
DR PRO; PR:P36130; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36130; protein.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0000266; P:mitochondrial fission; IMP:SGD.
DR GO; GO:0016559; P:peroxisome fission; IGI:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..643
FT /note="CCR4-associated factor 4"
FT /id="PRO_0000051478"
FT REPEAT 317..357
FT /note="WD 1"
FT REPEAT 360..400
FT /note="WD 2"
FT REPEAT 422..461
FT /note="WD 3"
FT REPEAT 479..526
FT /note="WD 4"
FT REPEAT 527..566
FT /note="WD 5"
FT REPEAT 568..603
FT /note="WD 6"
FT REPEAT 614..643
FT /note="WD 7"
FT REGION 1..274
FT /note="Required for interaction with FIS1 and MDV1"
FT /evidence="ECO:0000269|PubMed:16009724"
FT REGION 74..126
FT /note="Sufficient for interaction with FIS1"
FT REGION 243..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..255
FT /evidence="ECO:0000255"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 85..86
FT /note="FR->AA: Abolishes interaction with FIS1."
FT /evidence="ECO:0000269|PubMed:17998537"
FT MUTAGEN 88
FT /note="L->A: Abolishes interaction with FIS1."
FT /evidence="ECO:0000269|PubMed:17998537"
FT MUTAGEN 110
FT /note="L->A: Abolishes interaction with FIS1."
FT /evidence="ECO:0000269|PubMed:17998537"
FT MUTAGEN 111
FT /note="F->A: Abolishes interaction with FIS1."
FT /evidence="ECO:0000269|PubMed:17998537"
FT MUTAGEN 114
FT /note="F->A: Abolishes interaction with FIS1."
FT /evidence="ECO:0000269|PubMed:17998537"
FT CONFLICT 94..95
FT /note="QR -> HG (in Ref. 1; CAA82110)"
FT /evidence="ECO:0000305"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2PQR"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2PQR"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2PQR"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2PQR"
SQ SEQUENCE 643 AA; 72832 MW; 2C6B472CCC2340D3 CRC64;
MGSGDTRGES SLVAKPIEII LNKLPHAILA QQQFQKYITS PIYRYLSKLL LFREVAWPES
TKDTQKGQVG IFSFQNNYAD SATTFRILAH LDEQRYPLPN GAAEKNLPSL FEGFKATVSI
IQQRLLLDNV DGATNSDKEK YVQLPDINTG FVNKTYSRID LTHLLEDVET NVENLSINKT
LEMDELTRLD SMINELESRK LKILERVKHI DSKSTNLEND VTLIKDRINF IEEYNLEADR
EQSLRKQMEE ERSSEASSFT QNEEAISSLC DVESKDTRLK DFYKMPHEKS HDKNRQIISE
TYSRNTTAFR MTIPHGEHGN SITALDFDTP WGTLCSSSYQ DRIVKVWDLN HGIQVGELPG
HLATVNCMQI DKKNYNMLIT GSKDATLKLW DLNLSREIYL DHSPLKEKTE EIVTPCIHNF
ELHKDEITAL SFDSEALVSG SRDKKIFHWD LTTGKCIQQL DLIFTPTHSD IKMPARSLNN
GACLLGTEAP MIGALQCYNS ALATGTKDGI VRLWDLRVGK PVRLLEGHTD GITSLKFDSE
KLVTGSMDNS VRIWDLRTSS ILDVIAYDLP VSSLDFDGKL ITVGANEGGV NVFNMERDEH
WMTPEPPHSL DGDELSRRIA IVKYKDGFLI NGHNDGDINV WTL
