P36604 (GRP78_SCHPO) 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:	bip1
Synonyms:	bip
ORF Names:	SPAC22A12.15c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
Subcellular location	Endoplasmic reticulum lumen.
Post-translational modification	Partially N-glycosylated.
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
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' posttranslational protein folding Inferred from direct assay PubMed 9860839. Source: PomBase ER-associated ubiquitin-dependent protein catabolic process Inferred from sequence orthology. Source: PomBase cellular response to unfolded protein Inferred from sequence orthology. Source: PomBase
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 16823372. Source: PomBase endoplasmic reticulum lumen Inferred from direct assay Ref.1. Source: PomBase nuclear membrane Inferred from direct assay Ref.1. Source: PomBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from sequence orthology. Source: PomBase unfolded protein binding Inferred from sequence orthology. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 663	639	78 kDa glucose-regulated protein homolog		PRO_0000013585
Regions
	Motif	660 – 663	4	Prevents secretion from ER
Amino acid modifications
	Glycosylation	29	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	173	1	A → S in CAA45762. Ref.1
	Sequence conflict	301 – 302	2	KR → NG in CAA45762. Ref.1
	Sequence conflict	336 – 345	10	NMDLFKKTLK → KHGSLQEDFE in CAA45762. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36604 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 9DB80112E6C35742	FASTA	663	73,227
	10 20 30 40 50 60 MKKFQLFSIL SYFVALFLLP MAFASGDDNS TESYGTVIGI DLGTTYSCVA VMKNGRVEII 70 80 90 100 110 120 ANDQGNRITP SYVAFTEDER LVGEAAKNQA PSNPENTIFD IKRLIGRKFD EKTMAKDIKS 130 140 150 160 170 180 FPFHIVNDKN RPLVEVNVGG KKKKFTPEEI SAMILSKMKQ TAEAYLGKPV THAVVTVPAY 190 200 210 220 230 240 FNDAQRQATK DAGTIAGLNV IRIVNEPTAA AIAYGLDKTD TEKHIVVYDL GGGTFDVSLL 250 260 270 280 290 300 SIDNGVFEVL ATSGDTHLGG EDFDNRVINY LARTYNRKNN VDVTKDLKAM GKLKREVEKA 310 320 330 340 350 360 KRTLSSQKSV RIEIESFFNG QDFSETLSRA KFEEINMDLF KKTLKPVEQV LKDSNLKKSE 370 380 390 400 410 420 IDDIVLVGGS TRIPKVQELL ESFFGKKASK GINPDEAVAY GAAVQAGVLS GEEGSDNIVL 430 440 450 460 470 480 LDVIPLTLGI ETTGGVMTKL IGRNTPIPTR KSQIFSTAVD NQNTVLIQVY EGERTLTKDN 490 500 510 520 530 540 NLLGKFDLRG IPPAPRGVPQ IEVTFEVDAN GVLTVSAVDK SGKGKPEKLV IKNDKGRLSE 550 560 570 580 590 600 EDIERMVKEA EEFAEEDKIL KERIEARNTL ENYAYSLKGQ FDDDEQLGGK VDPEDKQAVL 610 620 630 640 650 660 DAVEDVAEWL EIHGEDASKE EFEDQRQKLD AVVHPITQKL YSEGAGDADE EDDDYFDDEA DEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the BiP gene and identification of an ER retention signal in Schizosaccharomyces pombe." Pidoux A.L., Armstrong J. EMBO J. 11:1583-1591(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X64416 Genomic DNA. Translation: CAA45762.1. CU329670 Genomic DNA. Translation: CAB16585.1.
PIR	S20877. T38155.
RefSeq	NP_593245.1. NM_001018642.2.
3D structure databases
ProteinModelPortal	P36604.
SMR	P36604. Positions 35-575.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	278306. 8 interactions.
IntAct	P36604. 2 interactions.
MINT	MINT-4688922.
STRING	4896.SPAC22A12.15c-1.
Proteomic databases
PaxDb	P36604.
PRIDE	P36604.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC22A12.15c.1; SPAC22A12.15c.1:pep; SPAC22A12.15c.
GeneID	2541815.
KEGG	spo:SPAC22A12.15c.
Organism-specific databases
PomBase	SPAC22A12.15c.
Phylogenomic databases
eggNOG	COG0443.
HOGENOM	HOG000228135.
KO	K09490.
OMA	CWIALLF.
OrthoDB	EOG728916.
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	20802903.
PRO	P36604.

Entry information

Entry name

GRP78_SCHPO

Accession

Primary (citable) accession number: P36604
Secondary accession number(s): O13906

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	December 15, 1998
Last modified:	February 19, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program