DSL1_YEAST
ID DSL1_YEAST Reviewed; 754 AA.
AC P53847; D6W0T5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein transport protein DSL1;
DE AltName: Full=Dependent on SLY1-20 protein 1;
GN Name=DSL1; OrderedLocusNames=YNL258C; ORFNames=N0842;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 725-GLN--ASP-754.
RX PubMed=11493604; DOI=10.1074/jbc.m105833200;
RA Andag U., Neumann T., Schmitt H.D.;
RT "The coatomer-interacting protein Dsl1p is required for Golgi-to-
RT endoplasmic reticulum retrieval in yeast.";
RL J. Biol. Chem. 276:39150-39160(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TIP20 AND RET2.
RX PubMed=11739780; DOI=10.1091/mbc.12.12.3783;
RA Reilly B.A., Kraynack B.A., VanRheenen S.M., Waters M.G.;
RT "Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires
RT Dsl1p, a component of the ER target site that interacts with a COPI coat
RT subunit.";
RL Mol. Biol. Cell 12:3783-3796(2001).
RN [6]
RP FUNCTION.
RX PubMed=11260526; DOI=10.1034/j.1600-0854.2001.020307.x;
RA VanRheenen S.M., Reilly B.A., Chamberlain S.J., Waters M.G.;
RT "Dsl1p, an essential protein required for membrane traffic at the
RT endoplasmic reticulum/Golgi interface in yeast.";
RL Traffic 2:212-231(2001).
RN [7]
RP MUTAGENESIS OF TRP-413; TRP-425 AND TRP-455, AND INTERACTION WITH RET1 AND
RP RET2.
RX PubMed=14504276; DOI=10.1074/jbc.m308740200;
RA Andag U., Schmitt H.D.;
RT "Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval
RT system in yeast, uses the same sequence motif to interact with different
RT subunits of the COPI vesicle coat.";
RL J. Biol. Chem. 278:51722-51734(2003).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for protein transport between the Golgi and the
CC endoplasmic reticulum. May tether coatomer-coated retrograde transport
CC vesicles to the ER membrane through interaction with coatomer as well
CC as the SNARE complex. May contribute to the stabilization of the SNARE
CC complex. {ECO:0000269|PubMed:11260526, ECO:0000269|PubMed:11493604,
CC ECO:0000269|PubMed:11739780}.
CC -!- SUBUNIT: Component of a peripheral membrane protein complex consisting
CC of DSL1, SEC39/DSL3 and TIP20. Bound to a SNARE complex consisting of
CC UFE1, USE1, SEC20 and SEC22 or YKT6 through direct interaction of TIP20
CC with SEC20. Binds the coatomer complex through direct interaction with
CC RET2/COPD and RET1/COPA. Binds TIP20 and SEC39/DSL3.
CC -!- INTERACTION:
CC P53847; Q12745: SEC39; NbExp=14; IntAct=EBI-29249, EBI-31898;
CC P53847; P33891: TIP20; NbExp=14; IntAct=EBI-29249, EBI-19396;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11493604, ECO:0000269|PubMed:11739780}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11493604,
CC ECO:0000269|PubMed:11739780}.
CC -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X96722; CAA65486.1; -; Genomic_DNA.
DR EMBL; Z71534; CAA96165.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10301.1; -; Genomic_DNA.
DR PIR; S63231; S63231.
DR RefSeq; NP_014141.1; NM_001183096.1.
DR PDB; 3ETU; X-ray; 2.40 A; A=1-361.
DR PDB; 3ETV; X-ray; 1.94 A; A=37-339.
DR PDB; 5FJW; X-ray; 2.80 A; L/M/N/O/P/Q/R/S=411-419.
DR PDB; 5FJZ; X-ray; 1.90 A; P/Q/R/S=411-419.
DR PDBsum; 3ETU; -.
DR PDBsum; 3ETV; -.
DR PDBsum; 5FJW; -.
DR PDBsum; 5FJZ; -.
DR AlphaFoldDB; P53847; -.
DR SMR; P53847; -.
DR BioGRID; 35581; 76.
DR ComplexPortal; CPX-1786; Dsl1 tethering complex.
DR DIP; DIP-4274N; -.
DR IntAct; P53847; 9.
DR STRING; 4932.YNL258C; -.
DR iPTMnet; P53847; -.
DR MaxQB; P53847; -.
DR PaxDb; P53847; -.
DR PRIDE; P53847; -.
DR EnsemblFungi; YNL258C_mRNA; YNL258C; YNL258C.
DR GeneID; 855463; -.
DR KEGG; sce:YNL258C; -.
DR SGD; S000005202; DSL1.
DR VEuPathDB; FungiDB:YNL258C; -.
DR eggNOG; ENOG502QR7Q; Eukaryota.
DR HOGENOM; CLU_357169_0_0_1; -.
DR InParanoid; P53847; -.
DR OMA; NHLKDIM; -.
DR BioCyc; YEAST:G3O-33254-MON; -.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR EvolutionaryTrace; P53847; -.
DR PRO; PR:P53847; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53847; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0070939; C:Dsl1/NZR complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990423; C:RZZ complex; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0032581; P:ER-dependent peroxisome organization; IMP:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:ComplexPortal.
DR Gene3D; 1.10.357.150; -; 1.
DR Gene3D; 1.20.58.2230; -; 1.
DR InterPro; IPR021876; Dsl1_C.
DR InterPro; IPR021875; Dsl1_N_dom.
DR InterPro; IPR038442; Dsl1_N_sf.
DR InterPro; IPR046362; Zw10/DSL1_C_sf.
DR Pfam; PF11989; Dsl1_C; 1.
DR Pfam; PF11988; Dsl1_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..754
FT /note="Protein transport protein DSL1"
FT /id="PRO_0000203383"
FT REGION 1..200
FT /note="Interaction with TIP20"
FT /evidence="ECO:0000269|PubMed:11739780"
FT REGION 406..459
FT /note="Interaction with RET2"
FT REGION 406..440
FT /note="Interaction with RET1"
FT /evidence="ECO:0000269|PubMed:14504276"
FT REGION 425..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 413
FT /note="W->A: Viable and reduced interaction with RET2,
FT strong Golgi-ER retrograde transport defect. Loss of
FT interaction with RET2; when associated with A-455. Lethal
FT and loss of interactions with RET1 and RET2; when
FT associated with A-425."
FT /evidence="ECO:0000269|PubMed:14504276"
FT MUTAGEN 425
FT /note="W->A: Loss of interaction with RET1; when associated
FT with A-413."
FT /evidence="ECO:0000269|PubMed:14504276"
FT MUTAGEN 455
FT /note="W->A: Viable and no effect. Lethal and loss of
FT interaction with RET2 and reduced interaction with RET1;
FT when associated with A-413."
FT /evidence="ECO:0000269|PubMed:14504276"
FT MUTAGEN 725..754
FT /note="Missing: In dsl1-22; strong Golgi-ER retrograde
FT transport defect."
FT /evidence="ECO:0000269|PubMed:11493604"
FT HELIX 45..73
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 102..129
FT /evidence="ECO:0007829|PDB:3ETV"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3ETV"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3ETV"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:3ETV"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3ETV"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:3ETV"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3ETV"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:3ETV"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 266..290
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:3ETV"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 302..321
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:3ETU"
SQ SEQUENCE 754 AA; 88072 MW; 51EDB17F2C55A917 CRC64;
MESLFPNKGE IIRELLKDPL ILKNDSKRSN GSELELDSSD LLQREAILAN ELNILDNLKT
FLNLIKEVKT NLNILELENC YYSLQSLRKK MRNNAAYLKQ SFNFQQSIST YVDTLHLELV
STLYKILTNG FWKITENSIQ FTPTVEWGKD KVHIEYDTFM DFVAQQYFPK GSLDNQAWFI
LDMTSADSQE QVRAKLNTIM KEYMNLSRIV SMIKNSIFIS GKEISYENEK NILVFSKSSS
HGQHCVSTVL TSFEAVCDFM LDGLAFRDRK TLSYELGPLF NTEFTKFVKN NASIILESLD
SPLKNLVSVI NNKLTRLVAK SEVTNWTHSG KEIQDLLMNK QLYYNLLLDK VLESHISEIR
SIFEDPKKSW QNLEVVELTT SNTNTMSEKI GKNDSDVQNE KELHNAVSKD DDWNWEVEDD
DADAWGDEID VNIDDEEEKT NQEKEKEPEE EENAWDEAWA IDENIDDASL ENGKEHLKAH
DVGSLDKDHI EVTQLPKLFL AISQNFKSSF ADSHVDEQYF AYKYNLLQTS YMAMCTANFS
HNWCQLYVDM RYLIERDEKL YRIKELTRNL LETKLNMKYR IVCQLIRHQL TEFRENERNP
SWDATIEKLL PYILKEIVRP LQKIRGEEGS RYLLSFLNFL YNDCVTKEIL KWQIISEVNS
ENLGELVSLL VNNTDIQLLA KEPSYKKMRE KFATMGKFLP LHLKEIMEMF YNGDFYLFAT
DELIQWIELL FADTPLRRNA IDDIYEIRGT ALDD
