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Protein

Hypoxia up-regulated protein 1

Gene

Hyou1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • response to hypoxia Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxia up-regulated protein 1
Alternative name(s):
150 kDa oxygen-regulated protein
Short name:
ORP-150
Gene namesi
Name:Hyou1
Synonyms:Orp150
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621146. Hyou1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
  • smooth endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32322 PublicationsAdd
BLAST
Chaini33 – 999967Hypoxia up-regulated protein 1PRO_0000013539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence analysis
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence analysis
Modified residuei567 – 5671PhosphoserineBy similarity
Glycosylationi596 – 5961N-linked (GlcNAc...)Sequence analysis
Glycosylationi830 – 8301N-linked (GlcNAc...)Sequence analysis
Glycosylationi862 – 8621N-linked (GlcNAc...)Sequence analysis
Glycosylationi869 – 8691N-linked (GlcNAc...)Sequence analysis
Modified residuei883 – 8831N6-acetyllysineBy similarity
Glycosylationi922 – 9221N-linked (GlcNAc...)Sequence analysis
Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ63617.
PRIDEiQ63617.

2D gel databases

World-2DPAGE0004:Q63617.

PTM databases

iPTMnetiQ63617.
UniCarbKBiQ63617.

Expressioni

Tissue specificityi

Selectively expressed by cultured astrocytes but not endothelial cells, microglia or neurons.

Inductioni

By oxygen deprivation.

Interactioni

Subunit structurei

Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.

Protein-protein interaction databases

BioGridi251367. 4 interactions.
IntActiQ63617. 2 interactions.
MINTiMINT-4579866.
STRINGi10116.ENSRNOP00000039172.

Structurei

3D structure databases

ProteinModelPortaliQ63617.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi996 – 9994Prevents secretion from ERSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi603 – 6064Poly-Glu

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0104. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000007865.
HOVERGENiHBG106402.
InParanoidiQ63617.
KOiK09486.
PhylomeDBiQ63617.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 2 hits.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q63617-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATVRRQRP RRLLCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV
60 70 80 90 100
KPGVPMEIVL NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF
110 120 130 140 150
QHLLGKQADN PHVALYRSRF PEHELNVDPQ RQTVRFQISP QLQFSPEEVL
160 170 180 190 200
GMVLNYSRSL AEDFAEQPIK DAVITVPAFF NQAERRAVLQ AARMAGLKVL
210 220 230 240 250
QLINDNTATA LSYGVFRRKD INSTAQNIMF YDMGSGSTVC TIVTYQTVKT
260 270 280 290 300
KEAGTQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR
310 320 330 340 350
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE
360 370 380 390 400
LCADLFDRVP GPVQQALQSA EMSLDQIEQV ILVGGPTRVP KVQEVLLKPV
410 420 430 440 450
GKEELGKNIN ADEAAAMGAV YQAAALSKAF KVKPFVVRDA VIYPILVEFT
460 470 480 490 500
REVEEEPGLR SLKHNKRVLF SRMGPYPQRK VITFNRYSHD FNFHINYGDL
510 520 530 540 550
GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK AHFNLDESGV
560 570 580 590 600
LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA
610 620 630 640 650
VQEEEESPAE GSKDEPAEQG ELKEEAEAPM EDTSQPPPSE PKGDAAREGE
660 670 680 690 700
TPDEKESGDK SEAQKPNEKG QAGPEGVPPA PEEEKKQKPA RKQKMVEEIG
710 720 730 740 750
VELAVLDLPD LPEDELAHSV QKLEDLTLRD LEKQEREKAA NSLEAFIFET
760 770 780 790 800
QDKLYQPEYQ EVSTEEQREE ISGKLSATST WLEDEGFGAT TVMLKDKLAE
810 820 830 840 850
LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR LIPEMDQIFT
860 870 880 890 900
DVEMTTLEKV INDTWTWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
910 920 930 940 950
EVQYLLNKAK FTKPRPRPKD KNGTRTEPPL NASAGDQEEK VIPPTGQTEE
960 970 980 990
AKAILEPDKE GLGTEAADSE PLELGGPGAE SEQAEQTAGQ KRPLKNDEL
Length:999
Mass (Da):111,289
Last modified:November 1, 1996 - v1
Checksum:iF93D53169C5A5EBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41853 mRNA. Translation: AAB05672.1.
RefSeqiNP_620222.2. NM_138867.2.
UniGeneiRn.10542.

Genome annotation databases

GeneIDi192235.
KEGGirno:192235.
UCSCiRGD:621146. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41853 mRNA. Translation: AAB05672.1.
RefSeqiNP_620222.2. NM_138867.2.
UniGeneiRn.10542.

3D structure databases

ProteinModelPortaliQ63617.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251367. 4 interactions.
IntActiQ63617. 2 interactions.
MINTiMINT-4579866.
STRINGi10116.ENSRNOP00000039172.

PTM databases

iPTMnetiQ63617.
UniCarbKBiQ63617.

2D gel databases

World-2DPAGE0004:Q63617.

Proteomic databases

PaxDbiQ63617.
PRIDEiQ63617.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi192235.
KEGGirno:192235.
UCSCiRGD:621146. rat.

Organism-specific databases

CTDi10525.
RGDi621146. Hyou1.

Phylogenomic databases

eggNOGiKOG0104. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000007865.
HOVERGENiHBG106402.
InParanoidiQ63617.
KOiK09486.
PhylomeDBiQ63617.

Miscellaneous databases

NextBioi622852.
PROiQ63617.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 2 hits.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150."
    Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T., Matsumoto M., Yura T., Yanagi H.
    Biochem. Biophys. Res. Commun. 230:94-99(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-63.
    Tissue: Astrocyte.
  2. "Purification and characterization of a novel stress protein, the 150-kDa oxygen-regulated protein (ORP150), from cultured rat astrocytes and its expression in ischemic mouse brain."
    Kuwabara K., Matsumoto M., Ikeda J., Hori O., Ogawa S., Maeda Y., Kitagawa K., Imuta N., Kinoshita T., Stern D.M., Yanagi H., Kamada T.
    J. Biol. Chem. 271:5025-5032(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-47, CHARACTERIZATION.
    Strain: Sprague-Dawley.
    Tissue: Astrocyte.
  3. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
    Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
    Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.

Entry informationi

Entry nameiHYOU1_RAT
AccessioniPrimary (citable) accession number: Q63617
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.