Q91883 (GRP78_XENLA) 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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	658 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.
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
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 – 19	19	Potential
	Chain	20 – 658	639	78 kDa glucose-regulated protein		PRO_0000013571
Regions
	Motif	655 – 658	4	Prevents secretion from ER By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q91883 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 43E1468F532E80CF	FASTA	658	72,635
	10 20 30 40 50 60 MVTMKLFALV LLVSASVFAS DDDDKKDDIG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG 70 80 90 100 110 120 NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKYLPFK 130 140 150 160 170 180 VIEKKTKPYI EVDIGDQMKT FAPEEISAMV LVKMKETAEA YLGRKVTHAV VTVPAYFNDA 190 200 210 220 230 240 QRQATKDAGT IAGLNVMRII NEPTAAAIAY GLDKKEGEKN ILVFDLGGGT FDVSLLTIDN 250 260 270 280 290 300 GVFEVVATNG DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR ADKRAVQKLR REVEKAKRAL 310 320 330 340 350 360 SAQHQSRIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLDDS DLKKSDIDEI 370 380 390 400 410 420 VLVGGSTRIP KIQQLVKELF NGKEPSRGIN PDEAVAYGAA VQAGVLSGDQ DTGDLVLLDV 430 440 450 460 470 480 CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ IFSTASDNQP TVTIKVYEGE RPLTKDNHLL 490 500 510 520 530 540 GTFDLTGIPP APRGVPQIEV TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE 550 560 570 580 590 600 RMVTDAEKFA EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETIEKAVE 610 620 630 640 650 EKIEWLESHQ DADIEDFKAK KKELEEIVQP IVGKLYGGAG APPPEGAEGA EETEKDEL

References

[1]	"Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP." Beggah A., Mathews P., Beguin P., Geering K. J. Biol. Chem. 271:20895-20902(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62807 mRNA. Translation: AAB08760.1.
RefSeq	NP_001081462.1. NM_001087993.1.
UniGene	Xl.3204.
3D structure databases
ProteinModelPortal	Q91883.
SMR	Q91883. Positions 30-571.
ModBase	Search...
Proteomic databases
PRIDE	Q91883.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397850.
KEGG	xla:397850.
Phylogenomic databases
HOVERGEN	HBG051845.
KO	K09490.
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_XENLA

Accession

Primary (citable) accession number: Q91883

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program