P59769 (GRP78_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Immunoglobulin heavy chain-binding protein homolog
Short name=BiP

Gene names

Name:	bipA
Synonyms:	bip

Organism

Aspergillus awamori (Black koji mold)

Taxonomic identifier

105351 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	672 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.
Induction	By heat shock and tunicamycin. Not induced by carbon source starvation. Ref.1
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Gene Ontology (GO)
Biological_process	response to unfolded protein Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	endoplasmic reticulum lumen Non-traceable author statement Ref.2Ref.1. Source: UniProtKB
Molecular_function	ATP binding Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 38	38	Potential
	Chain	39 – 672	634	78 kDa glucose-regulated protein homolog		PRO_0000013577
Regions
	Motif	669 – 672	4	Prevents secretion from ER By similarity
Experimental info
	Sequence conflict	316	1	R → G in CAA73106. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P59769 [UniParc]. Last modified July 11, 2003. Version 1. Checksum: C701807FCE08C175	FASTA	672	73,459
	10 20 30 40 50 60 MARISHQGAA KPFTAWTTIF YLLLVFIAPL AFFGTAHAQD ETSPQESYGT VIGIDLGTTY 70 80 90 100 110 120 SCVGVMQNGK VEILVNDQGN RITPSYVAFT DEERLVGDAA KNQYAANPRR TIFDIKRLIG 130 140 150 160 170 180 RKFDDKDVQK DAKHFPYKVV NKDGKPHVKV DVNQTPKTLT PEEVSAMVLG KMKEIAEGYL 190 200 210 220 230 240 GKKVTHAVVT VPAYFNDAQR QATKDAGTIA GLNVLRVVNE PTAAAIAYGL DKTGDERQVI 250 260 270 280 290 300 VYDLGGGTFD VSLLSIDNGV FEVLATAGDT HLGGEDFDQR VMDHFVKLYN KKNNVDVTKD 310 320 330 340 350 360 LKAMGKLKRE VEKAKRTLSS QMSTRIEIEA FHNGEDFSET LTRAKFEELN MDLFKKTLKP 370 380 390 400 410 420 VEQVLKDAKV KKSEVDDIVL VGGSTRIPKV QALLEEFFGG KKASKGINPD EAVAFGAAVQ 430 440 450 460 470 480 GGVLSGEEGT GDVVLMDVNP LTLGIETTGG VMTKLIPRNT VIPTRKSQIF STAADNQPTV 490 500 510 520 530 540 LIQVYEGERS LTKDNNLLGK FELTGIPPAP RGVPQIEVSF DLDANGILKV HASDKGTGKA 550 560 570 580 590 600 ESITITNDKG RLSQEEIDRM VAEAEEFAEE DKAIKAKIEA RNTLENYAFS LKNQVNDENG 610 620 630 640 650 660 LGGQIDEDDK QTILDAVKEV TEWLEDNAAT ATTEDFEEQK EQLSNVAYPI TSKLYGSAPA 670 DEDDEPSGHD EL

References

[1]

"The ER chaperone encoding bipA gene of black Aspergilli is induced by heat shock and unfolded proteins." van Gemeren I.A., Punt P.J., Drint-Kuyvenhoven A., Broekhuijsen M.P., van't Hoog A., Beijersbergen A., Verrips C.T., van den Hondel C.A.M.J.J. Gene 198:43-52(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: ATCC 11358 / K-6615 / CBS 115.52.

[2]

"Characterization of the bip gene of Aspergillus awamori encoding a protein with an HDEL retention signal homologous to the mammalian BiP involved in polypeptide secretion." Hijarrubia M.J., Casqueiro J., Gutierrez S., Fernandez F.J., Martin J.F. Curr. Genet. 32:139-146(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 22342 / NRRL 3112.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08867 Genomic DNA. Translation: CAA70090.1. Y12504 Genomic DNA. Translation: CAA73106.1.
PIR	T43723.
3D structure databases
ProteinModelPortal	P59769.
SMR	P59769. Positions 49-589.
ModBase	Search...
Proteomic databases
PRIDE	P59769.
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_ASPAW

Accession

Primary (citable) accession number: P59769
Secondary accession number(s): O13280, O14453

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2003
Last sequence update:	July 11, 2003
Last modified:	April 3, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program