HYOU1_RAT
ID HYOU1_RAT Reviewed; 999 AA.
AC Q63617;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Hypoxia up-regulated protein 1;
DE AltName: Full=150 kDa oxygen-regulated protein;
DE Short=ORP-150;
DE Flags: Precursor;
GN Name=Hyou1; Synonyms=Orp150;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-63.
RC TISSUE=Astrocyte;
RX PubMed=9020069; DOI=10.1006/bbrc.1996.5890;
RA Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T., Matsumoto M.,
RA Yura T., Yanagi H.;
RT "Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated
RT protein, ORP150.";
RL Biochem. Biophys. Res. Commun. 230:94-99(1997).
RN [2]
RP PROTEIN SEQUENCE OF 33-47, AND CHARACTERIZATION.
RC STRAIN=Sprague-Dawley; TISSUE=Astrocyte;
RX PubMed=8617779; DOI=10.1074/jbc.271.9.5025;
RA Kuwabara K., Matsumoto M., Ikeda J., Hori O., Ogawa S., Maeda Y.,
RA Kitagawa K., Imuta N., Kinoshita T., Stern D.M., Yanagi H., Kamada T.;
RT "Purification and characterization of a novel stress protein, the 150-kDa
RT oxygen-regulated protein (ORP150), from cultured rat astrocytes and its
RT expression in ischemic mouse brain.";
RL J. Biol. Chem. 271:5025-5032(1996).
RN [3]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-862; ASN-869
RP AND ASN-931, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms
CC triggered by oxygen deprivation. May play a role as a molecular
CC chaperone and participate in protein folding (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- TISSUE SPECIFICITY: Selectively expressed by cultured astrocytes but
CC not endothelial cells, microglia or neurons.
CC -!- INDUCTION: By oxygen deprivation.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U41853; AAB05672.1; -; mRNA.
DR RefSeq; NP_620222.2; NM_138867.2.
DR AlphaFoldDB; Q63617; -.
DR SMR; Q63617; -.
DR BioGRID; 251367; 9.
DR IntAct; Q63617; 4.
DR MINT; Q63617; -.
DR STRING; 10116.ENSRNOP00000039172; -.
DR GlyGen; Q63617; 9 sites, 7 N-linked glycans (5 sites).
DR iPTMnet; Q63617; -.
DR PhosphoSitePlus; Q63617; -.
DR World-2DPAGE; 0004:Q63617; -.
DR jPOST; Q63617; -.
DR PaxDb; Q63617; -.
DR PRIDE; Q63617; -.
DR GeneID; 192235; -.
DR KEGG; rno:192235; -.
DR UCSC; RGD:621146; rat.
DR CTD; 10525; -.
DR RGD; 621146; Hyou1.
DR eggNOG; KOG0104; Eukaryota.
DR InParanoid; Q63617; -.
DR PhylomeDB; Q63617; -.
DR PRO; PR:Q63617; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:8617779,
FT ECO:0000269|PubMed:9020069"
FT CHAIN 33..999
FT /note="Hypoxia up-regulated protein 1"
FT /id="PRO_0000013539"
FT REGION 564..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 996..999
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 573..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4L1"
FT MOD_RES 883
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKR6"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
SQ 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
