ID   SAP4_YEAST              Reviewed;         818 AA.
AC   P53036; D6VVA5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=SIT4-associating protein SAP4;
GN   Name=SAP4; OrderedLocusNames=YGL229C;
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 [GENOMIC DNA].
RX   PubMed=8649382; DOI=10.1128/mcb.16.6.2744;
RA   Luke M.M., della Seta F., di Como C.J., Sugimoto H., Kobayashi R.,
RA   Arndt K.T.;
RT   "The SAPs, a new family of proteins, associate and function positively with
RT   the SIT4 phosphatase.";
RL   Mol. Cell. Biol. 16:2744-2755(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
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   [4]
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).
CC   -!- FUNCTION: Associates with the SIT4 phosphatase in a cell cycle
CC       dependent manner. May be directly or indirectly involved in SIT4-
CC       dependent functions in budding and in normal G1 cyclin expression (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Hyperphosphorylated in the absence of SIT4. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
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DR   EMBL; U50562; AAC49305.1; -; Genomic_DNA.
DR   EMBL; Z72751; CAA96947.1; -; Genomic_DNA.
DR   EMBL; Z72750; CAA96946.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07889.1; -; Genomic_DNA.
DR   PIR; S64251; S64251.
DR   RefSeq; NP_011285.1; NM_001181095.1.
DR   AlphaFoldDB; P53036; -.
DR   BioGRID; 33010; 73.
DR   DIP; DIP-1604N; -.
DR   IntAct; P53036; 16.
DR   MINT; P53036; -.
DR   STRING; 4932.YGL229C; -.
DR   iPTMnet; P53036; -.
DR   MaxQB; P53036; -.
DR   PaxDb; P53036; -.
DR   PRIDE; P53036; -.
DR   EnsemblFungi; YGL229C_mRNA; YGL229C; YGL229C.
DR   GeneID; 852622; -.
DR   KEGG; sce:YGL229C; -.
DR   SGD; S000003198; SAP4.
DR   VEuPathDB; FungiDB:YGL229C; -.
DR   eggNOG; KOG2073; Eukaryota.
DR   GeneTree; ENSGT00390000009899; -.
DR   HOGENOM; CLU_003676_2_1_1; -.
DR   InParanoid; P53036; -.
DR   BioCyc; YEAST:G3O-30703-MON; -.
DR   PRO; PR:P53036; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53036; protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR   InterPro; IPR007587; SAPS.
DR   PANTHER; PTHR12634; PTHR12634; 4.
DR   Pfam; PF04499; SAPS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Reference proteome.
FT   CHAIN           1..818
FT                   /note="SIT4-associating protein SAP4"
FT                   /id="PRO_0000097585"
FT   REGION          33..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   818 AA;  94729 MW;  FB6E4FC06E4DD3FB CRC64;
     MSLWPFGETL SHSGIDSILE EYYLIFRSLE GNETSSTDDK KNEPSMESES EFGTESRDRS
     DLNQSFIDRI LLETALLDEL NGAANDRLVD FICLGYFYDD RSQQVRHMDY LVDMLMAYLK
     DIDRTGYRTP FLLENSFHQT GEYEDQDDED PMLYVNIISS IFCSKSAPIV EALVQNTPFL
     SSLFEVFQFE NIEAENCPIL AVFLKINETL LFEQTSSYLE FFKSQPNIVD KFLYHIEVSP
     LVEFLIKIML TDQVESPTNI IDFLYHQDLI PKCLNLLENS KYSPGIQNSS GELLKALISI
     STNFKLDTLW IGPNRLTRQL ASPQYVDQLI NIILFQRGHA MGVAVSIIIE LIRKNNSDYD
     EVDLLSTTIV DNPPSQRDPV YLGHLLYELT MHMEDFYALL IKLENDDDDD HDTASKALPS
     VKHHLLENQL HESFRPLGFE RVKITELISE MLHCSNMGLM NSKRGEKIAR TRDKCRDTLD
     QNSLEKAMKN LNINDNTITS NTLEDKCNNN DSNDSNDNQK QKKNIKKKFH DNELYSTFDT
     SDDNIDDDDD MSFEIPYVSE TQNLKIRKNP TIGDLFKIKL HDLGFFPKFL QLFLRYPWNN
     FWHNIVFDII QQIFNGRMDF SYNSFLVYSL FDFKKSTRFI PKPLYGSNQK LPVKDFHIIS
     DFILQGHKDS FEFYEKEKTN LGYMGQLVLI AEEIAKYSKI YKTDLIAPDI YAFLQDEVWM
     SYSSDILNET RTMCSIILGG GQFCAESDEN TNQDFLEKAD MSKPAHPSTM DENEIVHEED
     VKLHDKVAEL IDELGQLTEL DIHDKIKDVI VDHHSDLN