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Protein

Endoplasmic reticulum chaperone BiP

Gene

KAR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.1 Publication

Miscellaneous

Present with 337000 molecules/cell in log phase SD medium.1 Publication

Enzyme regulationi

The chaperone activity is regulated by ATP-induced allosteric coupling of the nucleotide-binding (NBD) and substrate-binding (SBD) domains. In the ADP-bound and nucleotide-free (apo) states, the two domains have little interaction. In contrast, in the ATP-bound state the two domains are tightly coupled, which results in drastically accelerated kinetics in both binding and release of polypeptide substrates. J domain-containing co-chaperones stimulate the ATPase activity and are required for efficient substrate recognition by HSPA5/BiP.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei117ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi58 – 61ATPBy similarity4
Nucleotide bindingi247 – 249ATPBy similarity3
Nucleotide bindingi313 – 320ATPBy similarity8
Nucleotide bindingi384 – 387ATPBy similarity4

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • unfolded protein binding Source: SGD

GO - Biological processi

  • fungal-type cell wall beta-glucan biosynthetic process Source: SGD
  • karyogamy involved in conjugation with cellular fusion Source: SGD
  • posttranslational protein targeting to membrane, translocation Source: SGD
  • response to unfolded protein Source: SGD
  • SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
  • ubiquitin-dependent ERAD pathway Source: SGD

Keywordsi

Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31501-MONOMER
ReactomeiR-SCE-3371453 Regulation of HSF1-mediated heat shock response
R-SCE-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-SCE-3371568 Attenuation phase
R-SCE-3371571 HSF1-dependent transactivation
R-SCE-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-SCE-6798695 Neutrophil degranulation
R-SCE-8876725 Protein methylation

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum chaperone BiPCurated
Alternative name(s):
78 kDa glucose-regulated protein homolog1 Publication
Short name:
GRP-781 Publication
Immunoglobulin heavy chain-binding protein homologCurated
Short name:
BiPCurated
Gene namesi
Name:KAR2
Synonyms:GRP781 Publication, SSD1
Ordered Locus Names:YJL034W
ORF Names:J1248
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL034W
SGDiS000003571 KAR2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 42Sequence analysisAdd BLAST42
ChainiPRO_000001358743 – 682Endoplasmic reticulum chaperone BiPAdd BLAST640

Proteomic databases

MaxQBiP16474
PaxDbiP16474
PRIDEiP16474

2D gel databases

SWISS-2DPAGEiP16474

PTM databases

iPTMnetiP16474

Interactioni

Subunit structurei

Interacts with EPS1, PDI1 and YOS9.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi33726, 637 interactors
DIPiDIP-2392N
IntActiP16474, 160 interactors
MINTiP16474
STRINGi4932.YJL034W

Structurei

Secondary structure

1682
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 57Combined sources5
Beta strandi59 – 67Combined sources9
Beta strandi72 – 74Combined sources3
Beta strandi82 – 85Combined sources4
Beta strandi88 – 90Combined sources3
Beta strandi95 – 98Combined sources4
Helixi99 – 103Combined sources5
Helixi105 – 107Combined sources3
Helixi109 – 111Combined sources3
Helixi116 – 118Combined sources3
Turni119 – 121Combined sources3
Helixi127 – 133Combined sources7
Beta strandi137 – 143Combined sources7
Beta strandi146 – 160Combined sources15
Helixi162 – 181Combined sources20
Beta strandi187 – 192Combined sources6
Helixi198 – 210Combined sources13
Beta strandi214 – 220Combined sources7
Helixi221 – 228Combined sources8
Turni229 – 232Combined sources4
Beta strandi238 – 245Combined sources8
Beta strandi250 – 258Combined sources9
Beta strandi261 – 270Combined sources10
Helixi275 – 294Combined sources20
Helixi298 – 300Combined sources3
Helixi302 – 318Combined sources17
Turni319 – 321Combined sources3
Beta strandi323 – 333Combined sources11
Beta strandi336 – 343Combined sources8
Helixi344 – 357Combined sources14
Helixi359 – 369Combined sources11
Helixi373 – 375Combined sources3
Beta strandi378 – 383Combined sources6
Helixi384 – 387Combined sources4
Helixi389 – 398Combined sources10
Turni399 – 401Combined sources3
Turni410 – 412Combined sources3
Helixi413 – 425Combined sources13
Beta strandi444 – 448Combined sources5
Turni449 – 451Combined sources3
Beta strandi452 – 457Combined sources6
Beta strandi462 – 471Combined sources10
Beta strandi481 – 489Combined sources9
Helixi493 – 495Combined sources3
Beta strandi496 – 504Combined sources9
Beta strandi517 – 523Combined sources7
Beta strandi527 – 535Combined sources9
Turni536 – 538Combined sources3
Beta strandi541 – 547Combined sources7
Helixi555 – 567Combined sources13
Helixi569 – 580Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H0XX-ray1.92A438-586[»]
3QFPX-ray2.26A43-426[»]
3QFUX-ray1.80A43-426[»]
3QMLX-ray2.31A/B43-426[»]
ProteinModelPortaliP16474
SMRiP16474
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16474

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni146 – 300Nucleotide-binding (NBD)By similarityAdd BLAST155
Regioni420 – 520Substrate-binding (SBD)By similarityAdd BLAST101

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi679 – 682Prevents secretion from ER4

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00910000144045
HOGENOMiHOG000228135
InParanoidiP16474
KOiK09490
OMAiCVGVMQK
OrthoDBiEOG092C1VPN

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00014 ER_TARGET, 1 hit
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFFNRLSAGK LLVPLSVVLY ALFVVILPLQ NSFHSSNVLV RGADDVENYG
60 70 80 90 100
TVIGIDLGTT YSCVAVMKNG KTEILANEQG NRITPSYVAF TDDERLIGDA
110 120 130 140 150
AKNQVAANPQ NTIFDIKRLI GLKYNDRSVQ KDIKHLPFNV VNKDGKPAVE
160 170 180 190 200
VSVKGEKKVF TPEEISGMIL GKMKQIAEDY LGTKVTHAVV TVPAYFNDAQ
210 220 230 240 250
RQATKDAGTI AGLNVLRIVN EPTAAAIAYG LDKSDKEHQI IVYDLGGGTF
260 270 280 290 300
DVSLLSIENG VFEVQATSGD THLGGEDFDY KIVRQLIKAF KKKHGIDVSD
310 320 330 340 350
NNKALAKLKR EAEKAKRALS SQMSTRIEID SFVDGIDLSE TLTRAKFEEL
360 370 380 390 400
NLDLFKKTLK PVEKVLQDSG LEKKDVDDIV LVGGSTRIPK VQQLLESYFD
410 420 430 440 450
GKKASKGINP DEAVAYGAAV QAGVLSGEEG VEDIVLLDVN ALTLGIETTG
460 470 480 490 500
GVMTPLIKRN TAIPTKKSQI FSTAVDNQPT VMIKVYEGER AMSKDNNLLG
510 520 530 540 550
KFELTGIPPA PRGVPQIEVT FALDANGILK VSATDKGTGK SESITITNDK
560 570 580 590 600
GRLTQEEIDR MVEEAEKFAS EDASIKAKVE SRNKLENYAH SLKNQVNGDL
610 620 630 640 650
GEKLEEEDKE TLLDAANDVL EWLDDNFETA IAEDFDEKFE SLSKVAYPIT
660 670 680
SKLYGGADGS GAADYDDEDE DDDGDYFEHD EL
Length:682
Mass (Da):74,468
Last modified:August 1, 1990 - v1
Checksum:iA107BD03DF3F30D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25064 Genomic DNA Translation: AAA34714.1
M25394 Genomic DNA Translation: AAA34713.1
M31006 Genomic DNA Translation: AAA34454.1
Z49309 Genomic DNA Translation: CAA89325.1
BK006943 Genomic DNA Translation: DAA08765.1
PIRiA32366 HHBYK2
RefSeqiNP_012500.3, NM_001181468.3

Genome annotation databases

EnsemblFungiiYJL034W; YJL034W; YJL034W
GeneIDi853418
KEGGisce:YJL034W

Similar proteinsi

Entry informationi

Entry nameiBIP_YEAST
AccessioniPrimary (citable) accession number: P16474
Secondary accession number(s): D6VWE9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 23, 2018
This is version 193 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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