DSS4_YEAST
ID DSS4_YEAST Reviewed; 143 AA.
AC P32601; D6W427; Q12299; Q3S1N1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein DSS4;
GN Name=DSS4; OrderedLocusNames=YPR017C; ORFNames=LPZ16C, YP9531.11C;
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=8429886; DOI=10.1038/361460a0;
RA Moya M., Roberts D., Novick P.;
RT "DSS4-1 is a dominant suppressor of sec4-8 that encodes a nucleotide
RT exchange protein that aids Sec4p function.";
RL Nature 361:460-463(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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: Guanine-nucleotide-releasing protein that acts on SEC4. Might
CC play a general role in vesicular transport.
CC -!- MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DSS4/MSS4 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01132}.
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DR EMBL; X70495; CAA49903.1; -; Genomic_DNA.
DR EMBL; S54550; AAA13721.1; -; Genomic_DNA.
DR EMBL; U31900; AAA97595.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95013.1; -; Genomic_DNA.
DR EMBL; Z49919; CAA90162.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11443.1; -; Genomic_DNA.
DR PIR; S57551; S57551.
DR RefSeq; NP_015342.1; NM_001184114.1.
DR AlphaFoldDB; P32601; -.
DR BioGRID; 36194; 94.
DR DIP; DIP-1423N; -.
DR IntAct; P32601; 17.
DR MINT; P32601; -.
DR STRING; 4932.YPR017C; -.
DR MaxQB; P32601; -.
DR PaxDb; P32601; -.
DR PRIDE; P32601; -.
DR EnsemblFungi; YPR017C_mRNA; YPR017C; YPR017C.
DR GeneID; 856128; -.
DR KEGG; sce:YPR017C; -.
DR SGD; S000006221; DSS4.
DR VEuPathDB; FungiDB:YPR017C; -.
DR eggNOG; KOG4113; Eukaryota.
DR HOGENOM; CLU_124782_0_0_1; -.
DR InParanoid; P32601; -.
DR OMA; ECDKGPL; -.
DR BioCyc; YEAST:G3O-34177-MON; -.
DR PRO; PR:P32601; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32601; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:SGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00246; RabGEF; 1.
DR Gene3D; 2.170.150.10; -; 1.
DR InterPro; IPR007515; Mss4.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR011323; Mss4/transl-control_tumour.
DR PANTHER; PTHR13276; PTHR13276; 1.
DR Pfam; PF04421; Mss4; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51796; MSS4; 1.
PE 1: Evidence at protein level;
KW Guanine-nucleotide releasing factor; Metal-binding; Protein transport;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..143
FT /note="Protein DSS4"
FT /id="PRO_0000174180"
FT DOMAIN 1..131
FT /note="MSS4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT VARIANT 108
FT /note="D -> G (in DSS4-1; a dominant suppressor of SEC4-8)"
FT CONFLICT 136
FT /note="S -> T (in Ref. 1; CAA49903/AAA13721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 143 AA; 16126 MW; 1D7B6D3443D93AE2 CRC64;
MSKATCSFEG CHSAVITIND DNIINLPEQV HSEFKLLENR TMRDATPSES NFLVVPDVWD
FDNVGVSREI PSSILGDLSD KSDFVFEYGN SSWKIKKCLK YLICADCDKG PIGIICKVQD
QTKNEERVLH LLSLRSLQIM GRN
