HYOU1_CRIGR
ID HYOU1_CRIGR Reviewed; 999 AA.
AC Q60432;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Hypoxia up-regulated protein 1;
DE AltName: Full=150 kDa oxygen-regulated protein;
DE Short=ORP-150;
DE AltName: Full=170 kDa glucose-regulated protein;
DE Short=GRP-170;
DE Flags: Precursor;
GN Name=HYOU1; Synonyms=GRP170, ORP150;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=8603749; DOI=10.1016/0014-5793(96)00011-7;
RA Chen X., Easton D., Oh H.J., Lee-Yoon D.S., Liu X., Subjeck J.;
RT "The 170 kDa glucose regulated stress protein is a large HSP70-, HSP110-
RT like protein of the endoplasmic reticulum.";
RL FEBS Lett. 380:68-72(1996).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:8603749}.
CC -!- INDUCTION: By anoxia. {ECO:0000269|PubMed:8603749}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U34206; AAB00689.1; -; mRNA.
DR PIR; S68689; S68689.
DR RefSeq; NP_001233670.1; NM_001246741.1.
DR AlphaFoldDB; Q60432; -.
DR SMR; Q60432; -.
DR STRING; 10029.NP_001233670.1; -.
DR GeneID; 100689308; -.
DR KEGG; cge:100689308; -.
DR CTD; 10525; -.
DR eggNOG; KOG0104; Eukaryota.
DR OrthoDB; 708294at2759; -.
DR PRO; PR:Q60432; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; 2.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Phosphoprotein; Signal; Stress response.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..999
FT /note="Hypoxia up-regulated protein 1"
FT /id="PRO_0000013537"
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 644..669
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 COMPBIAS 985..999
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:0000255"
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:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
SQ SEQUENCE 999 AA; 111271 MW; FC6A73AE6E84A412 CRC64;
MAATVRRQRP RRLLCWTLVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF QHLLGKQADN PHVALYRDRF
PEHELNIDPQ RQTVRFQISP QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPAFF
NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INSTAQNVMF YDMGSGTTVC
TIVTYQTVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RRGQKAKDVR
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVESEE LCADLFERVP
GPVQQALQSA EMSLDEIEQV ILVGGATRVP KVQEVLLKAV GKEELGKNIN ADEAAAMGAV
YQAAALSKAF KVKPFVVRDA VIYPILVEFT REVEEEPGVR SLKHNKRVLF SRMGPYPQGK
VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGESLKK YPDYESKGIK
AHFNLDESGV LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA
VQEEEESPTE GSKDEPGEQG DLKEETEAPV EDTSQPPPPE PKGDAAPEGE KPDEKESGGK
SEAQKPEEKG QSGPEGVPPA PEEEKKQKPA RKQKMVEEIG VELAVLDLPD LPEDELARSV
KKLEDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSATST
WLEDEGFGAT TVMLKEKLAE LKKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR
LIPEMDQIFT EVEMTTLEKV INDTWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
EVQYLLNKAK FTKPRPRPKD KNGTRTEPPL NATAGDQEEK VIPPAGQPEE AKPILEPDKE
ETTTEPTDSE PLELGGPGAE SEPKEQTAGQ KRSSKNDEL
