SND1_YEAST
ID SND1_YEAST Reviewed; 877 AA.
AC Q04007; D6VSH0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=SRP-independent targeting protein 1 {ECO:0000303|PubMed:27905431};
GN Name=SND1 {ECO:0000303|PubMed:27905431};
GN OrderedLocusNames=YDR186C {ECO:0000312|SGD:S000002594};
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=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 [2]
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 [3]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692 AND SER-706, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-334, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692; SER-706 AND SER-841, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-310; SER-311;
RP SER-692; SER-694 AND SER-706, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-668 AND LYS-670, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ENV10.
RX PubMed=27905431; DOI=10.1038/nature20169;
RA Aviram N., Ast T., Costa E.A., Arakel E.C., Chuartzman S.G., Jan C.H.,
RA Hassdenteufel S., Dudek J., Jung M., Schorr S., Zimmermann R.,
RA Schwappach B., Weissman J.S., Schuldiner M.;
RT "The SND proteins constitute an alternative targeting route to the
RT endoplasmic reticulum.";
RL Nature 540:134-138(2016).
CC -!- FUNCTION: Functions in the SND pathway, a SRP (signal recognition
CC particle) and GET (guided entry of tail-anchored proteins) independent
CC pathway for targeting a broad range of substrate proteins to the
CC endoplasmic reticulum. SND functions in parallel to GET in targeting
CC proteins with downstream hydrophobic motifs.
CC {ECO:0000269|PubMed:27905431}.
CC -!- SUBUNIT: Interacts with ENV10/SND2. {ECO:0000269|PubMed:27905431}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:27905431}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z46727; CAA86693.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12030.1; -; Genomic_DNA.
DR PIR; S49783; S49783.
DR RefSeq; NP_010472.3; NM_001180494.3.
DR AlphaFoldDB; Q04007; -.
DR BioGRID; 32240; 241.
DR DIP; DIP-6821N; -.
DR IntAct; Q04007; 8.
DR MINT; Q04007; -.
DR STRING; 4932.YDR186C; -.
DR TCDB; 9.A.64.1.1; the srp-independent targeting (snd) family.
DR iPTMnet; Q04007; -.
DR MaxQB; Q04007; -.
DR PaxDb; Q04007; -.
DR PRIDE; Q04007; -.
DR EnsemblFungi; YDR186C_mRNA; YDR186C; YDR186C.
DR GeneID; 851767; -.
DR KEGG; sce:YDR186C; -.
DR SGD; S000002594; SND1.
DR VEuPathDB; FungiDB:YDR186C; -.
DR eggNOG; ENOG502QRGG; Eukaryota.
DR HOGENOM; CLU_018066_0_0_1; -.
DR InParanoid; Q04007; -.
DR OMA; NIYIHDG; -.
DR BioCyc; YEAST:G3O-29775-MON; -.
DR PRO; PR:Q04007; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04007; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..877
FT /note="SRP-independent targeting protein 1"
FT /id="PRO_0000253835"
FT REGION 369..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 412..441
FT /evidence="ECO:0000255"
FT COMPBIAS 369..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..501
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 668
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 877 AA; 98331 MW; B9DF8982537DC9D3 CRC64;
MDTVGTDAAA ASINERRFAQ STSPKVSVKS QDSLFLITYS NMQQTVVQAS LADRYPSLKK
LNILLYIDIP TIDYYNDEMT HNKLSRLNKR FKLHRLRNSI AQSFSNTSTA EDNDKFWEEL
KSLISSRSTP ENKFDLNVLV SSSGSLRYVE TIRFLVEKLF NSFKDLYVQK KLNLCFQINV
SPTSLKWFST FLNAELLNLK IINWQNIGSF TKTIQNSKSL PFKEYYTKLN EKFTGSNQSN
GSMQDQTVLD SIVIVTNSTG VKALLTLLSD HPLTSLISQE SIKALHEYSD AVNEDKGDDQ
SNTSLKRNSS SLLNFQNSVL TSNKDKSVRI RSLSINRKSN RAHMFKTNES ITTIPSTSIN
NLIGQESNLR KQPSGTALHL QSHLHPHSRS QSYSSSNMSR SPSPFPYGKT PSNDELVYDE
LNNQINEVQD RAKNEEIVLY NNNNYDDYTK ERGEQEQDRT SYADEYGFNY DDEEGGNEDN
YDDDEDDDDD DDDDDESDDE GLSFYAPSIL SRSGSSTDVL SSGIDSMAKN SKETRGRFRS
LSLMDPALQK PFNQKFPNSQ QPDSAGASSP KRSTSSNHFT NVYVHDGDFD GTDTINNKKN
LSSATLIKRK SLMNRNLAPS ISNGLIPPEF ISRISTPSTS ASSSNSSLND MSTVSNAFSK
LLNDTSKKQK FLNSPIPQHT QQASPLLMRN NSNSNLLFEK NLINKSFEEL RRQPSVNLFS
TLMNGNMEKN GLALNFKSRT PTDALMANSI KNSNNSSHRL LNLEEEDQIM SGSLPKERED
DNDSTNSTIV PNHPDNDNYN DNDNDNNTGI NSNNFNLNLY DDNDSAGFTD VTTEGVKYSN
SNSTVTKPVY KKAVTLDLYG EDDMDNMGGW VLGGNAR
