P36016 (LHS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heat shock protein 70 homolog LHS1
EC=3.6.1.3

Gene names

Name:	LHS1
Ordered Locus Names:	YKL073W
ORF Names:	YKL355

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	881 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Chaperone required for protein translocation and folding in the endoplasmic reticulum. Ref.7
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with the heat shock protein 70 (HSP70) KAR2, and this stimulates nucleotide exchange on KAR2. KAR2 in turn acts to stimulate the ATPase activity of LHS1. Ref.7
Subcellular location	Endoplasmic reticulum lumen.
Induction	By the unfolded protein response (UPR). Ref.5
Post-translational modification	N-glycosylated.
Miscellaneous	Present with 137 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC posttranslational protein targeting to membrane, translocation Inferred from mutant phenotype Ref.4PubMed 8887673. Source: SGD response to unfolded protein Inferred from genetic interaction Ref.4PubMed 8887673. Source: SGD
Cellular_component	endoplasmic reticulum lumen Inferred from direct assay Ref.4PubMed 8887673. Source: SGD
Molecular_function	ATP binding Inferred from direct assay PubMed 19759005. Source: SGD ATPase activity Inferred from electronic annotation. Source: EC adenyl-nucleotide exchange factor activity Inferred from direct assay Ref.7. Source: SGD unfolded protein binding Inferred from genetic interaction Ref.4PubMed 8887673. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 881	861	Heat shock protein 70 homolog LHS1		PRO_0000013556
Regions
	Motif	878 – 881	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	128	1	N-linked (GlcNAc...) Potential
	Glycosylation	458	1	N-linked (GlcNAc...) Potential
	Glycosylation	474	1	N-linked (GlcNAc...) Potential
	Glycosylation	481	1	N-linked (GlcNAc...) Potential
	Glycosylation	489	1	N-linked (GlcNAc...) Potential
	Glycosylation	527	1	N-linked (GlcNAc...) Potential
	Glycosylation	844	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	239	1	G → D in allele LHS1-1; constitutive ATPase activity. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P36016 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: ACED092CA3A34785	FASTA	881	99,572
	10 20 30 40 50 60 MRNVLRLLFL TAFVAIGSLA AVLGVDYGQQ NIKAIVVSPQ APLELVLTPE AKRKEISGLS 70 80 90 100 110 120 IKRLPGYGKD DPNGIERIYG SAVGSLATRF PQNTLLHLKP LLGKSLEDET TVTLYSKQHP 130 140 150 160 170 180 GLEMVSTNRS TIAFLVDNVE YPLEELVAMN VQEIANRANS LLKDRDARTE DFVNKMSFTI 190 200 210 220 230 240 PDFFDQHQRK ALLDASSITT GIEETYLVSE GMSVAVNFVL KQRQFPPGEQ QHYIVYDMGS 250 260 270 280 290 300 GSIKASMFSI LQPEDTTQPV TIEFEGYGYN PHLGGAKFTM DIGSLIENKF LETHPAIRTD 310 320 330 340 350 360 ELHANPKALA KINQAAEKAK LILSANSEAS INIESLINDI DFRTSITRQE FEEFIADSLL 370 380 390 400 410 420 DIVKPINDAV TKQFGGYGTN LPEINGVILA GGSSRIPIVQ DQLIKLVSEE KVLRNVNADE 430 440 450 460 470 480 SAVNGVVMRG IKLSNSFKTK PLNVVDRSVN TYSFKLSNES ELYDVFTRGS AYPNKTSILT 490 500 510 520 530 540 NTTDSIPNNF TIDLFENGKL FETITVNSGA IKNSYSSDKC SSGVAYNITF DLSSDRLFSI 550 560 570 580 590 600 QEVNCICQSE NDIGNSKQIK NKGSRLAFTS EDVEIKRLSP SERSRLHEHI KLLDKQDKER 610 620 630 640 650 660 FQFQENLNVL ESNLYDARNL LMDDEVMQNG PKSQVEELSE MVKVYLDWLE DASFDTDPED 670 680 690 700 710 720 IVSRIREIGI LKKKIELYMD SAKEPLNSQQ FKGMLEEGHK LLQAIETHKN TVEEFLSQFE 730 740 750 760 770 780 TEFADTIDNV REEFKKIKQP AYVSKALSTW EETLTSFKNS ISEIEKFLAK NLFGEDLREH 790 800 810 820 830 840 LFEIKLQFDM YRTKLEEKLR LIKSGDESRL NEIKKLHLRN FRLQKRKEEK LKRKLEQEKS 850 860 870 880 RNNNETESTV INSADDKTTI VNDKTTESNP SSEEDILHDE L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of a 20.7 kb region of yeast chromosome XI includes the NUP100 gene, an open reading frame (ORF) possibly representing a nucleoside diphosphate kinase gene, tRNAs for His, Val and Trp in addition to seven ORFs with weak or no significant similarity to known proteins." Rasmussen S.W. Yeast 10:S69-S74(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors." Craven R.A., Egerton M., Stirling C.J. EMBO J. 15:2640-2650(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation." Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., Walter P. Cell 101:249-258(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION.
[7]	"Coordinated activation of Hsp70 chaperones." Steel G.J., Fullerton D.M., Tyson J.R., Stirling C.J. Science 303:98-101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KAR2, MUTAGENESIS OF GLY-239.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75780 Genomic DNA. Translation: CAA53401.1. Z28073 Genomic DNA. Translation: CAA81910.1. BK006944 Genomic DNA. Translation: DAA09083.1.
PIR	S37895.
RefSeq	NP_012850.1. NM_001179639.1.
3D structure databases
ProteinModelPortal	P36016.
SMR	P36016. Positions 19-671.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6520N.
IntAct	P36016. 5 interactions.
MINT	MINT-684320.
STRING	4932.YKL073W.
Proteomic databases
PaxDb	P36016.
PeptideAtlas	P36016.
PRIDE	P36016.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL073W; YKL073W; YKL073W.
GeneID	853789.
KEGG	sce:YKL073W.
Organism-specific databases
CYGD	YKL073w.
SGD	S000001556. LHS1.
Phylogenomic databases
eggNOG	COG0443.
GeneTree	ENSGT00700000105728.
HOGENOM	HOG000111144.
KO	K09486.
OMA	DESCALG.
OrthoDB	EOG4H1F3X.
Gene expression databases
Genevestigator	P36016.
GermOnline	YKL073W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR013126. Hsp_70_fam. [Graphical view]
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00297. HSP70_1. False negative. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974918.

Entry information

Entry name

LHS1_YEAST

Accession

Primary (citable) accession number: P36016
Secondary accession number(s): D6VXL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program