SNL1_YEAST
ID SNL1_YEAST Reviewed; 159 AA.
AC P40548; D6VVR3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=HSP70 co-chaperone SNL1;
DE AltName: Full=Suppressor of NUP116-C lethal;
GN Name=SNL1; OrderedLocusNames=YIL016W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND NUCLEAR PORE ASSEMBLY.
RX PubMed=9450961; DOI=10.1091/mbc.9.2.355;
RA Ho A.K., Raczniak G.A., Ives E.B., Wente S.R.;
RT "The integral membrane protein snl1p is genetically linked to yeast nuclear
RT pore complex function.";
RL Mol. Biol. Cell 9:355-373(1998).
RN [5]
RP FUNCTION, INTERACTION WITH SSA1; SSA4 AND SSB1, HSP70 CO-CHAPERONE
RP ACTIVITY, AND MUTAGENESIS OF GLU-112 AND ARG-141.
RX PubMed=12105220; DOI=10.1074/jbc.m204624200;
RA Sondermann H., Ho A.K., Listenberger L.L., Siegers K., Moarefi I.,
RA Wente S.R., Hartl F.-U., Young J.C.;
RT "Prediction of novel Bag-1 homologs based on structure/function analysis
RT identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 277:33220-33227(2002).
RN [6]
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: Stimulator of ATPase activity of molecular chaperones of the
CC HSP70 family (principally of the SSA class). Stimulation is important
CC for HSP70-substrate complex dissociation after folding of newly
CC synthesized or refolded proteins. SNL1 is probably involved in nuclear
CC pore biogenesis and in particular the folding or refolding of misfolded
CC NUP116, GLE2 and NIC96. {ECO:0000269|PubMed:12105220,
CC ECO:0000269|PubMed:9450961}.
CC -!- SUBUNIT: Interacts with the HSP70 family members SSA1, SSA4, and SSB1.
CC These interactions are strongly reduced by ADP and ATP.
CC {ECO:0000269|PubMed:12105220}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9450961}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:9450961}. Nucleus membrane
CC {ECO:0000269|PubMed:9450961}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:9450961}.
CC -!- MISCELLANEOUS: Present with 3346 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z46881; CAA86976.1; -; Genomic_DNA.
DR EMBL; AY558552; AAS56878.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08529.1; -; Genomic_DNA.
DR PIR; S49966; S49966.
DR RefSeq; NP_012248.1; NM_001179366.1.
DR AlphaFoldDB; P40548; -.
DR SMR; P40548; -.
DR BioGRID; 34972; 201.
DR DIP; DIP-5636N; -.
DR IntAct; P40548; 41.
DR MINT; P40548; -.
DR STRING; 4932.YIL016W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR MaxQB; P40548; -.
DR PaxDb; P40548; -.
DR PRIDE; P40548; -.
DR EnsemblFungi; YIL016W_mRNA; YIL016W; YIL016W.
DR GeneID; 854796; -.
DR KEGG; sce:YIL016W; -.
DR SGD; S000001278; SNL1.
DR VEuPathDB; FungiDB:YIL016W; -.
DR eggNOG; ENOG502S72Q; Eukaryota.
DR HOGENOM; CLU_112518_0_0_1; -.
DR InParanoid; P40548; -.
DR OMA; RESHIDT; -.
DR BioCyc; YEAST:G3O-31292-MON; -.
DR PRO; PR:P40548; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40548; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0006999; P:nuclear pore organization; IGI:SGD.
DR GO; GO:0006457; P:protein folding; IPI:SGD.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR Pfam; PF02179; BAG; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
PE 1: Evidence at protein level;
KW Chaperone; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..159
FT /note="HSP70 co-chaperone SNL1"
FT /id="PRO_0000088881"
FT TOPO_DOM 1..12
FT /note="Perinuclear space"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..159
FT /note="Cytoplasmic"
FT DOMAIN 73..159
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 112
FT /note="E->A: Strongly reduces interaction with HSP70 family
FT members."
FT /evidence="ECO:0000269|PubMed:12105220"
FT MUTAGEN 141
FT /note="R->A: Strongly reduces interaction with HSP70 family
FT members."
FT /evidence="ECO:0000269|PubMed:12105220"
SQ SEQUENCE 159 AA; 18306 MW; 05524B473D3E888E CRC64;
MSHNAMEHWK SKLSKTSTST YVLLAVIAVV FLVTIRRPNG SKGKSSKKRA SKKNKKGKNQ
FEKAPVPLTL EEQIDNVSLR YGNELEGRSK DLINRFDVED EKDIYERNYC NEMLLKLLIE
LDSIDLINVD ESLRRPLKEK RKGVIKEIQA MLKSLDSLK
