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Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150)

 HYOU1_RAT               Reviewed;         999 AA.
Q63617;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 137.
RecName: Full=Hypoxia up-regulated protein 1;
AltName: Full=150 kDa oxygen-regulated protein;
Short=ORP-150;
Flags: Precursor;
Name=Hyou1; Synonyms=Orp150;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-63.
TISSUE=Astrocyte;
PubMed=9020069; DOI=10.1006/bbrc.1996.5890;
Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T.,
Matsumoto M., Yura T., Yanagi H.;
"Cloning and expression of cDNA encoding the human 150 kDa oxygen-
regulated protein, ORP150.";
Biochem. Biophys. Res. Commun. 230:94-99(1997).
[2]
PROTEIN SEQUENCE OF 33-47, AND CHARACTERIZATION.
STRAIN=Sprague-Dawley; TISSUE=Astrocyte;
PubMed=8617779; DOI=10.1074/jbc.271.9.5025;
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.;
"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.";
J. Biol. Chem. 271:5025-5032(1996).
[3]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-862;
ASN-869 AND ASN-931, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24090084; DOI=10.1021/pr400783j;
Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
Graham M.E., Packer N.H., Cordwell S.J.;
"Site-specific glycan-peptide analysis for determination of N-
glycoproteome heterogeneity.";
J. Proteome Res. 12:5791-5800(2013).
-!- FUNCTION: 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).
{ECO:0000250}.
-!- SUBUNIT: 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.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
-!- TISSUE SPECIFICITY: Selectively expressed by cultured astrocytes
but not endothelial cells, microglia or neurons.
-!- INDUCTION: By oxygen deprivation.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; U41853; AAB05672.1; -; mRNA.
RefSeq; NP_620222.2; NM_138867.2.
UniGene; Rn.10542; -.
ProteinModelPortal; Q63617; -.
SMR; Q63617; -.
BioGrid; 251367; 4.
IntAct; Q63617; 3.
STRING; 10116.ENSRNOP00000039172; -.
iPTMnet; Q63617; -.
PhosphoSitePlus; Q63617; -.
UniCarbKB; Q63617; -.
World-2DPAGE; 0004:Q63617; -.
PaxDb; Q63617; -.
PRIDE; Q63617; -.
GeneID; 192235; -.
KEGG; rno:192235; -.
UCSC; RGD:621146; rat.
CTD; 10525; -.
RGD; 621146; Hyou1.
eggNOG; KOG0104; Eukaryota.
eggNOG; COG0443; LUCA.
HOGENOM; HOG000007865; -.
HOVERGEN; HBG106402; -.
InParanoid; Q63617; -.
KO; K09486; -.
PhylomeDB; Q63617; -.
PRO; PR:Q63617; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Chaperone; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
Nucleotide-binding; Phosphoprotein; Reference proteome; Signal.
SIGNAL 1 32 {ECO:0000269|PubMed:8617779,
ECO:0000269|PubMed:9020069}.
CHAIN 33 999 Hypoxia up-regulated protein 1.
/FTId=PRO_0000013539.
MOTIF 996 999 Prevents secretion from ER.
{ECO:0000255}.
COMPBIAS 603 606 Poly-Glu.
MOD_RES 567 567 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y4L1}.
MOD_RES 883 883 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JKR6}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 596 596 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 830 830 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 862 862 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 869 869 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 922 922 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 931 931 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
SEQUENCE 999 AA; 111289 MW; F93D53169C5A5EBD CRC64;
MAATVRRQRP RRLLCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF QHLLGKQADN PHVALYRSRF
PEHELNVDPQ RQTVRFQISP QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPAFF
NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INSTAQNIMF YDMGSGSTVC
TIVTYQTVKT KEAGTQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFDRVP
GPVQQALQSA EMSLDQIEQV ILVGGPTRVP KVQEVLLKPV GKEELGKNIN ADEAAAMGAV
YQAAALSKAF KVKPFVVRDA VIYPILVEFT REVEEEPGLR SLKHNKRVLF SRMGPYPQRK
VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK
AHFNLDESGV LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA
VQEEEESPAE GSKDEPAEQG ELKEEAEAPM EDTSQPPPSE PKGDAAREGE TPDEKESGDK
SEAQKPNEKG QAGPEGVPPA PEEEKKQKPA RKQKMVEEIG VELAVLDLPD LPEDELAHSV
QKLEDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSATST
WLEDEGFGAT TVMLKDKLAE LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR
LIPEMDQIFT DVEMTTLEKV INDTWTWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
EVQYLLNKAK FTKPRPRPKD KNGTRTEPPL NASAGDQEEK VIPPTGQTEE AKAILEPDKE
GLGTEAADSE PLELGGPGAE SEQAEQTAGQ KRPLKNDEL


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