ID A0A087W2A1_ECHMU Unreviewed; 649 AA.
AC A0A087W2A1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Heat Shock protein family member hsp 3 {ECO:0000313|EMBL:CDI98630.1};
GN ORFNames=EmuJ_000249600 {ECO:0000313|EMBL:CDI98630.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDI98630.1};
RN [1] {ECO:0000313|EMBL:CDI98630.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDI98630.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; LN902844; CDI98630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087W2A1; -.
DR STRING; 6211.A0A087W2A1; -.
DR OMA; AYTKNQD; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_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:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000313|EMBL:CDI98630.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..649
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001831757"
FT COILED 277..304
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 649 AA; 71633 MW; 057200107D188019 CRC64;
MGLSTYVGTF LLCILTLSHC KSGKEEYGTV IGIDLGTTYS CVGVFKNGRV EIIANDQGNR
ITPSYVAFSG DGERLIGDAA KNQLTSNPKN TLFDAKRLIG RDYDDKDVQG DIKRYPFKVI
NKNNKPYMKV QVGSEEKGFA PEEVSAMVLS KMKEIAEAYL GTEVTHAVVT VPAYFNDAQR
QATKDAGAIA GLTVLRIINE PTAAAIAYGL DKKDTEKNIL VFDLGGGTFD VSLLTIDNGV
FEVVATSGDT HLGGEDFDQR LIDYFVKLYK KKEGKDITKD DRAVQKLRRE VEKAKRTLST
EHSTMIEIDN LFEGKDFSEP LTRARFEELN NDLFRSTLKP VMKVMEDSGL KKEDIDDIVL
VGGSTRIPKI QQLVKEFFNG KEPSRGINPD EAVAYGAAVQ AGVISGVEDT GDIVLLDVCP
LTMGIETVGG VMTKLIPRNT VIPTKKSQIF STAADNQPTV TIQVFEGERP MTKDNHFLGK
FDLTGIPPAP RGLPQIEVTF EIDVNGILRV SAEDKGTGKK SNIVINKETN RLTPEEIERM
IQDAEKFSDQ DKQVKERVEV RNDLESLAYS IKNQVKDKEK MGGKLSDDEI KTIEDAADEA
IKWMENNPQA ETSDYKKQKA NLESVVQPIV SKLYEGAAPP TESTPKEEL
//
