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Q24895

- GRP78_ECHMU

UniProt

Q24895 - GRP78_ECHMU

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Protein
78 kDa glucose-regulated protein
Gene
GRP78
Organism
Echinococcus multilocularis (Fox tapeworm)
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at transcript leveli

Functioni

Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER By similarity.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
78 kDa glucose-regulated protein
Short name:
GRP-78
Gene namesi
Name:GRP78
OrganismiEchinococcus multilocularis (Fox tapeworm)
Taxonomic identifieri6211 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesCestodaEucestodaCyclophyllideaTaeniidaeEchinococcus

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Chaini21 – 64962978 kDa glucose-regulated protein
PRO_0000013574Add
BLAST

Proteomic databases

PRIDEiQ24895.

Structurei

3D structure databases

ProteinModelPortaliQ24895.
SMRiQ24895. Positions 28-569.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi646 – 6494Prevents secretion from ER

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q24895-1 [UniParc]FASTAAdd to Basket

« Hide

MGLSTYVGTF LLCILTLSHC KSGKEEYGTV IGIDLGTTYS CVGVFKNGRV    50
EIIANDQGNR ITPSYVAFSG DGERLIGDAA KNQLTSNPKN TLFDAKRLIG 100
RDYDDKDVQG DIKRYPFKVI NKNNKPYMKV QVGSEEKGFA PEEVSAMVLS 150
KMKEIAEAYL GTEVTHAVVT VPAYFNDAQR QATKDAGAIA GLTVLRIINE 200
PTAAAIAYGL DKKDTEKNIL VFDLGGGTFD VSLLTIDNGV FEVVATSGDT 250
HLGGEDFDQR LIDYFVKLYK KKEGKDITKD DRAVQKLRRE VEKAKRTLST 300
EHSTMIEIDN LFEGKDFSEP LTRARFEELN NDLFRSTLKP VMKVMEDSGL 350
KKEDIDDIVL VGGSTRIPKI QQLVKEFFNV KEPSRGINPD EAVAYGAAVQ 400
AGVISGVEDT GDIVLLDVCP LTMGIETVGG VMTKLIPRNT VIPTKKSQIF 450
STAADNQPTV TIQVFEGERP MTKDNHFLGK FDLTGIPPAP RGLPQIEVTF 500
EIDVNGILRV SAEDKGTGKK SNIVINKETN RLTPEEIERM IQDAEKFSDQ 550
DKQVKERVEV RNDLESLAYS IKNQVKDKEK MGGKLSDDEI KTIEDAADEA 600
IKWMENNPQA ETSDYKKQKA NLESVVQPIV SKLYEGAAPP TESTPKEEL 649
Length:649
Mass (Da):71,675
Last modified:November 1, 1996 - v1
Checksum:i057E7D617D1D8418
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63604 mRNA. Translation: AAC37258.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63604 mRNA. Translation: AAC37258.1 .

3D structure databases

ProteinModelPortali Q24895.
SMRi Q24895. Positions 28-569.
ModBasei Search...

Proteomic databases

PRIDEi Q24895.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and characterization of an Echinococcus multilocularis and Echinococcus granulosus stress protein homologous to the mammalian 78 kDa glucose regulated protein."
    Muhlschlegel F., Frosch P., Castro A., Apfel H., Muller A., Frosch M.
    Mol. Biochem. Parasitol. 74:245-250(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiGRP78_ECHMU
AccessioniPrimary (citable) accession number: Q24895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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