Q24895 (GRP78_ECHMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
78 kDa glucose-regulated protein
Short name=GRP-78

Gene names

Name:

GRP78

Organism

Echinococcus multilocularis

Taxonomic identifier

6211 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Platyhelminthes › Cestoda › Eucestoda › Cyclophyllidea › Taeniidae › Echinococcus

Protein attributes

Sequence length	649 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
Gene Ontology (GO)
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
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 – 649	629	78 kDa glucose-regulated protein		PRO_0000013574
Regions
	Motif	646 – 649	4	Prevents secretion from ER

Sequences

	Sequence		Length	Mass (Da)
	Q24895 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 057E7D617D1D8418	FASTA	649	71,675
	10 20 30 40 50 60 MGLSTYVGTF LLCILTLSHC KSGKEEYGTV IGIDLGTTYS CVGVFKNGRV EIIANDQGNR 70 80 90 100 110 120 ITPSYVAFSG DGERLIGDAA KNQLTSNPKN TLFDAKRLIG RDYDDKDVQG DIKRYPFKVI 130 140 150 160 170 180 NKNNKPYMKV QVGSEEKGFA PEEVSAMVLS KMKEIAEAYL GTEVTHAVVT VPAYFNDAQR 190 200 210 220 230 240 QATKDAGAIA GLTVLRIINE PTAAAIAYGL DKKDTEKNIL VFDLGGGTFD VSLLTIDNGV 250 260 270 280 290 300 FEVVATSGDT HLGGEDFDQR LIDYFVKLYK KKEGKDITKD DRAVQKLRRE VEKAKRTLST 310 320 330 340 350 360 EHSTMIEIDN LFEGKDFSEP LTRARFEELN NDLFRSTLKP VMKVMEDSGL KKEDIDDIVL 370 380 390 400 410 420 VGGSTRIPKI QQLVKEFFNV KEPSRGINPD EAVAYGAAVQ AGVISGVEDT GDIVLLDVCP 430 440 450 460 470 480 LTMGIETVGG VMTKLIPRNT VIPTKKSQIF STAADNQPTV TIQVFEGERP MTKDNHFLGK 490 500 510 520 530 540 FDLTGIPPAP RGLPQIEVTF EIDVNGILRV SAEDKGTGKK SNIVINKETN RLTPEEIERM 550 560 570 580 590 600 IQDAEKFSDQ DKQVKERVEV RNDLESLAYS IKNQVKDKEK MGGKLSDDEI KTIEDAADEA 610 620 630 640 IKWMENNPQA ETSDYKKQKA NLESVVQPIV SKLYEGAAPP TESTPKEEL

References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63604 mRNA. Translation: AAC37258.1.
3D structure databases
ProteinModelPortal	Q24895.
SMR	Q24895. Positions 28-569.
ModBase	Search...
Proteomic databases
PRIDE	Q24895.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. 1 hit. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GRP78_ECHMU

Accession

Primary (citable) accession number: Q24895

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)