Q90593 (GRP78_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
Short name=BiP

Gene names

Name:	HSPA5
Synonyms:	GRP78

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	652 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	Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER By similarity.
Subcellular location	Endoplasmic reticulum lumen.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER overload response Inferred from electronic annotation. Source: Compara activation of signaling protein activity involved in unfolded protein response Inferred from electronic annotation. Source: Compara cellular response to glucose starvation Inferred from electronic annotation. Source: Compara cerebellar Purkinje cell layer development Inferred from electronic annotation. Source: Compara cerebellum structural organization Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of protein ubiquitination Inferred from electronic annotation. Source: Compara proteolysis involved in cellular protein catabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum chaperone complex Inferred from electronic annotation. Source: Compara endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: Compara integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara midbody Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara signalosome Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from electronic annotation. Source: Compara ribosome binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KCNMA1	Q8AYS8	3	EBI-1635886,EBI-1635766

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 652	636	78 kDa glucose-regulated protein		PRO_0000013570
Regions
	Motif	649 – 652	4	Prevents secretion from ER By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q90593 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4E4BB58A3EEFAF6F	FASTA	652	72,019
	10 20 30 40 50 60 MRHLLLALLL LGGARADDEE KKEDVGTVVG IDLGTTYSCV GVFKNGRVEI IANDQGNRIT 70 80 90 100 110 120 PSYVAFTPEG ERLIGDAAKN QLTSNPENTV FDAKRLIGRT WNDPSVQQDI KYLPFKVVEK 130 140 150 160 170 180 KAKPHIQVDV GGGQTKTFAP EEISAMVLTK MKETAEAYLG KKVTHAVVTV PAYFNDAQRQ 190 200 210 220 230 240 ATKDAGTIAG LNVMRIINEP TAAAIAYGLD KREGEKNILV FDLGGGTFDV SLLTIDNGVF 250 260 270 280 290 300 EVVATNGDTH LGGEDFDQRV MEHFIKLYKK KTGKDVRKDN RAVQKLRREV EKAKRALSSQ 310 320 330 340 350 360 HQARIEIESF FEGEDFSETL TRAKFEELNM DLFRSTMKPV QKVLEDSDLK KSDIDEIVLV 370 380 390 400 410 420 GGSTRIPKIQ QLVKEFFNGK EPSRGINPDE AVAYGAAVQA GVLSGDQDTG DLVLLDVCPL 430 440 450 460 470 480 TLGIETVGGV MTKLIPRNTV VPTKKSQIFS TASDNQPTVT IKVYEGERPL TKDNHLLGTF 490 500 510 520 530 540 DLTGIPPAPR GVPQIEVTFE IDVNGILRVT AEDKGTGNKN KITITNDQNR LTPEEIERMV 550 560 570 580 590 600 NDAEKFAEED KKLKERIDAR NELESYAYSL KNQIGDKEKL GGKLSSEDKE TIEKAVEEKI 610 620 630 640 650 EWLESHQDAD IEDFKSKKKE LEEVVQPIVS KLYGSAGPPP TGEEEAAEKD EL

References

[1]

"78-kilodalton glucose-regulated protein is induced in Rous sarcoma virus-transformed cells independently of glucose deprivation." Stoeckle M.Y., Sugano S., Hampe A., Vashishtha A., Pellman D., Hanafusa H. Mol. Cell. Biol. 8:2675-2680(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27260 mRNA. Translation: AAA48785.1.
IPI	IPI00590375.
PIR	I50242.
RefSeq	NP_990822.1. NM_205491.1.
UniGene	Gga.4219.
3D structure databases
ProteinModelPortal	Q90593.
SMR	Q90593. Positions 26-568.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q90593. 1 interaction.
STRING	9031.ENSGALP00000001474.
Proteomic databases
PaxDb	Q90593.
PRIDE	Q90593.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000001476; ENSGALP00000001474; ENSGALG00000001000.
GeneID	396487.
KEGG	gga:396487.
Organism-specific databases
CTD	3309.
Phylogenomic databases
eggNOG	COG0443.
GeneTree	ENSGT00550000074467.
HOGENOM	HOG000228135.
HOVERGEN	HBG051845.
InParanoid	Q90593.
KO	K09490.
OMA	VIAKLYQ.
OrthoDB	EOG444KJV.
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...
Other
NextBio	20816526.

Entry information

Entry name

GRP78_CHICK

Accession

Primary (citable) accession number: Q90593

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program