SLY1_YEAST
ID SLY1_YEAST Reviewed; 666 AA.
AC P22213; D6VSH2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein SLY1;
DE AltName: Full=Suppressor of loss of YPT1 protein 1;
GN Name=SLY1; OrderedLocusNames=YDR189W; ORFNames=YD9346.01, YD9395.22;
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=1990290; DOI=10.1128/mcb.11.2.872-885.1991;
RA Dascher C., Ossig R., Gallwitz D., Schmitt H.D.;
RT "Identification and structure of four yeast genes (SLY) that are able to
RT suppress the functional loss of YPT1, a member of the RAS superfamily.";
RL Mol. Cell. Biol. 11:872-885(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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).
RN [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH SED5.
RX PubMed=12426383; DOI=10.1093/emboj/cdf608;
RA Bracher A., Weissenhorn W.;
RT "Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p.";
RL EMBO J. 21:6114-6124(2002).
CC -!- FUNCTION: Able to suppress the functional loss of YPT1. SLY1 is
CC essential for cell viability. May interact indirectly, or directly with
CC YPT1.
CC -!- SUBUNIT: Interacts with SED5. {ECO:0000269|PubMed:12426383}.
CC -!- INTERACTION:
CC P22213; Q01590: SED5; NbExp=5; IntAct=EBI-17387, EBI-16930;
CC P22213; P41834: UFE1; NbExp=4; IntAct=EBI-17387, EBI-20016;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC -!- MISCELLANEOUS: Present with 5780 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; X54323; CAA38221.1; -; Genomic_DNA.
DR EMBL; Z48784; CAA88703.1; -; Genomic_DNA.
DR EMBL; Z46727; CAA86695.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12032.1; -; Genomic_DNA.
DR PIR; A39610; A39610.
DR RefSeq; NP_010475.1; NM_001180497.1.
DR PDB; 1MQS; X-ray; 3.00 A; A=1-666.
DR PDBsum; 1MQS; -.
DR AlphaFoldDB; P22213; -.
DR SMR; P22213; -.
DR BioGRID; 32242; 331.
DR DIP; DIP-2940N; -.
DR IntAct; P22213; 13.
DR MINT; P22213; -.
DR STRING; 4932.YDR189W; -.
DR iPTMnet; P22213; -.
DR MaxQB; P22213; -.
DR PaxDb; P22213; -.
DR PRIDE; P22213; -.
DR EnsemblFungi; YDR189W_mRNA; YDR189W; YDR189W.
DR GeneID; 851770; -.
DR KEGG; sce:YDR189W; -.
DR SGD; S000002597; SLY1.
DR VEuPathDB; FungiDB:YDR189W; -.
DR eggNOG; KOG1301; Eukaryota.
DR GeneTree; ENSGT00550000074845; -.
DR HOGENOM; CLU_016216_3_1_1; -.
DR InParanoid; P22213; -.
DR OMA; DRQLDNF; -.
DR BioCyc; YEAST:G3O-29777-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR EvolutionaryTrace; P22213; -.
DR PRO; PR:P22213; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P22213; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0019905; F:syntaxin binding; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0035543; P:positive regulation of SNARE complex assembly; IMP:SGD.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IMP:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..666
FT /note="Protein SLY1"
FT /id="PRO_0000206299"
FT REPEAT 106..142
FT /note="1"
FT REPEAT 220..257
FT /note="2"
FT REPEAT 436..474
FT /note="3"
FT REPEAT 478..514
FT /note="4"
FT REGION 106..514
FT /note="4 X approximate repeats"
FT VARIANT 532
FT /note="E -> K (in SLY1-20 mutant)"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1MQS"
FT TURN 27..33
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:1MQS"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 191..210
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 223..240
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 336..360
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 388..412
FT /evidence="ECO:0007829|PDB:1MQS"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 447..460
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 467..478
FT /evidence="ECO:0007829|PDB:1MQS"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 486..503
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 529..533
FT /evidence="ECO:0007829|PDB:1MQS"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 543..548
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 557..566
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 573..579
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 616..626
FT /evidence="ECO:0007829|PDB:1MQS"
FT STRAND 635..643
FT /evidence="ECO:0007829|PDB:1MQS"
FT HELIX 646..659
FT /evidence="ECO:0007829|PDB:1MQS"
SQ SEQUENCE 666 AA; 74679 MW; 79B0A1C4FB45042F CRC64;
MAVEEIASRK DISLRDMQIS AILKMLFLNK DLNNNDNITT ITDDIFNQQE IIWKVLILDI
KSTATISSVL RVNDLLKAGI TVHSLIKQDR SPLPDVPAIY FVSPTKENID IIVNDLKSDK
YSEFYINFTS SLPRNLLEDL AQQVSITGKS DKIKQVYDQY LDFIVTEPEL FSLEISNAYL
TLNDPKTTEE EITGLCANIA DGLFNTVLTI NSIPIIRAAK GGPAEIIAEK LGTKLRDFVI
NTNSSSTSTL QGNDSLERGV LIILDRNIDF ASMFSHSWIY QCMVFDIFKL SRNTVTIPLE
SKENGTDNTT AKPLATKKYD IEPNDFFWME NSHLPFPEAA ENVEAALNTY KEEAAEITRK
TGVTNISDLD PNSNNDTVQI QEVVKKLPEL TAKKNTIDTH MNIFAALLSQ LESKSLDTFF
EVEQDPGSTK TRSRFLDILK DGKTNNLEDK LRSFIVLYLT STTGLPKDFV QNVENYFKEN
DYDINALKYV YKLREFMQLS NMSLQNKSLE DGSDSAFKPS NLTLSGIYGL TEGKLQGGVG
SLISGIKKLL PEKKTIPITN VVDAIMDPLN SSQKNLETTD SYLYIDPKIT RGSHTRKPKR
QSYNKSLVFV VGGGNYLEYQ NLQEWAHSQL HNPKKVMYGS TAITTPAEFL NEISRLGASN
SSNNDA
