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HSP71_CANAL
ID   HSP71_CANAL             Reviewed;         656 AA.
AC   P41797; A0A1D8PFP4; Q5AKZ7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Heat shock protein SSA1;
GN   Name=SSA1; Synonyms=HSP70; OrderedLocusNames=CAALFM_C113480WA;
GN   ORFNames=CaO19.12447, CaO19.4980;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7558317; DOI=10.1128/iai.63.10.4039-4045.1995;
RA   La Valle R., Bromuro C., Ranucci L., Muller H.M., Crisanti A., Cassone A.;
RT   "Molecular cloning and expression of a 70-kilodalton heat shock protein of
RT   Candida albicans.";
RL   Infect. Immun. 63:4039-4045(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-244.
RX   PubMed=7744244; DOI=10.1111/j.1574-6968.1995.tb07506.x;
RA   Eroles P., Sentandreu M., Elorza M.V., Sentandreu R.;
RT   "Cloning of a DNA fragment encoding part of a 70-kDa heat shock protein of
RT   Candida albicans.";
RL   FEMS Microbiol. Lett. 128:95-100(1995).
RN   [6]
RP   FUNCTION, INTERACTION WITH HUMAN HTN3, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12761219; DOI=10.1074/jbc.m300680200;
RA   Li X.S., Reddy M.S., Baev D., Edgerton M.;
RT   "Candida albicans Ssa1/2p is the cell envelope binding protein for human
RT   salivary histatin 5.";
RL   J. Biol. Chem. 278:28553-28561(2003).
CC   -!- FUNCTION: May play a role in the transport of polypeptides both across
CC       the mitochondrial membranes and into the endoplasmic reticulum.
CC       {ECO:0000250, ECO:0000269|PubMed:12761219}.
CC   -!- SUBUNIT: Binds human HTN3/histatin-5, a peptide from saliva, and
CC       mediates its fungicidal activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12761219}.
CC       Secreted, cell wall {ECO:0000269|PubMed:12761219}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; S78163; AAB34280.1; -; mRNA.
DR   EMBL; CP017623; AOW26952.1; -; Genomic_DNA.
DR   EMBL; Z30210; CAA82929.1; -; mRNA.
DR   PIR; S51712; S51712.
DR   RefSeq; XP_722186.1; XM_717093.2.
DR   AlphaFoldDB; P41797; -.
DR   SMR; P41797; -.
DR   BioGRID; 1219167; 9.
DR   STRING; 237561.P41797; -.
DR   COMPLUYEAST-2DPAGE; P41797; -.
DR   PRIDE; P41797; -.
DR   GeneID; 3636229; -.
DR   KEGG; cal:CAALFM_C113480WA; -.
DR   CGD; CAL0000184706; HSP70.
DR   VEuPathDB; FungiDB:C1_13480W_A; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   HOGENOM; CLU_005965_3_0_1; -.
DR   InParanoid; P41797; -.
DR   OMA; VVVQFKG; -.
DR   OrthoDB; 288077at2759; -.
DR   Reactome; R-HSA-6803157; Antimicrobial peptides.
DR   PRO; PR:P41797; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR   GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR   GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IDA:CGD.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IDA:CGD.
DR   GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0044409; P:entry into host; IMP:CGD.
DR   GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009636; P:response to toxic substance; IMP:CGD.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell wall; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Secreted; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..656
FT                   /note="Heat shock protein SSA1"
FT                   /id="PRO_0000078364"
FT   REGION          608..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        176
FT                   /note="A -> G (in Ref. 5; AAB34280)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   656 AA;  70324 MW;  562BA08EDDFE2EFD CRC64;
     MSKAVGIDLG TTYSCVAHFA NDRVEIIAND QGNRTTPSFV AFTDTERLIG DAAKNQAAMN
     PANTVFDAKR LIGRKFDDPE VINDAKHFPF KVIDKAGKPV IQVEYKGETK TFSPEEISSM
     VLTKMKEIAE GYLGSTVKDA VVTVPAYFND SQRQATKDAG TIAGLNVLRI INEPTAAAIA
     YGLDKKGSRG EHNVLIFDLG GGTFDVSLLA IDEGIFEVKA TAGDTHLGGE DFDNRLVNFF
     IQEFKRKNKK DISTNQRALR RLRTACERAK RTLSSSAQTS IEIDSLYEGI DFYTSITRAR
     FEELCADLFR STLDPVGKVL ADAKIDKSQV EEIVLVGGST RIPKIQKLVS DFFNGKELNK
     SINPDEAVAY GAAVQAAILT GDTSSKTQDI LLLDVAPLSL GIETAGGIMT KLIPRNSTIP
     TKKSETFSTY ADNQPGVLIQ VFEGERAKTK DNNLLGKFEL SGIPPAPRGV PQIEVTFDID
     ANGILNVSAL EKGTGKTQKI TITNDKGRLS KEEIDKMVSE AEKFKEEDEK EAARVQAKNQ
     LESYAYSLKN TINDGEMKDK IGADDKEKLT KAIDETISWL DASQAASTEE YEDKRKELES
     VANPIISGAY GAAGGAPGGA GGFPGAGGFP GGAPGAGGPG GATGGESSGP TVEEVD
 
 
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