HYOU1_MOUSE
ID HYOU1_MOUSE Reviewed; 999 AA.
AC Q9JKR6; Q3TAL1; Q3TZD0; Q3U1U2; Q64139; Q80X75;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Hypoxia up-regulated protein 1;
DE Short=GRP-170;
DE AltName: Full=140 kDa Ca(2+)-binding protein;
DE Short=CBP-140;
DE Flags: Precursor;
GN Name=Hyou1; Synonyms=Grp170;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen X., Easton D.P., Subjeck J.R.;
RT "The 170 kDa glucose regulated protein of mouse.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Placenta, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 347-999, AND SUBCELLULAR LOCATION.
RX PubMed=7641295; DOI=10.1247/csf.20.133;
RA Naved A.F., Ozawa M., Yu S., Miyauchi T., Muramatsu H., Muramatsu T.;
RT "CBP-140, a novel endoplasmic reticulum resident Ca(2+)-binding protein
RT with a carboxy-terminal NDEL sequence showed partial homology with 70-kDa
RT heat shock protein (hsp70).";
RL Cell Struct. Funct. 20:133-141(1995).
RN [5]
RP PROTEIN SEQUENCE OF 439-451.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-883, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(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 {ECO:0000269|PubMed:7641295}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF228709; AAF65544.1; -; mRNA.
DR EMBL; AK171769; BAE42657.1; -; mRNA.
DR EMBL; AK145857; BAE26702.1; -; mRNA.
DR EMBL; AK155721; BAE33401.1; -; mRNA.
DR EMBL; AK157949; BAE34279.1; -; mRNA.
DR EMBL; BC050107; AAH50107.1; -; mRNA.
DR EMBL; S78797; AAB35051.1; -; mRNA.
DR CCDS; CCDS23107.1; -.
DR RefSeq; NP_067370.3; NM_021395.4.
DR RefSeq; XP_006510022.1; XM_006509959.2.
DR RefSeq; XP_006510023.1; XM_006509960.2.
DR RefSeq; XP_006510024.1; XM_006509961.2.
DR AlphaFoldDB; Q9JKR6; -.
DR SMR; Q9JKR6; -.
DR BioGRID; 198427; 28.
DR CORUM; Q9JKR6; -.
DR IntAct; Q9JKR6; 2.
DR MINT; Q9JKR6; -.
DR STRING; 10090.ENSMUSP00000068594; -.
DR GlyConnect; 2376; 18 N-Linked glycans (6 sites).
DR GlyGen; Q9JKR6; 9 sites, 18 N-linked glycans (6 sites).
DR iPTMnet; Q9JKR6; -.
DR PhosphoSitePlus; Q9JKR6; -.
DR SwissPalm; Q9JKR6; -.
DR REPRODUCTION-2DPAGE; IPI00123342; -.
DR REPRODUCTION-2DPAGE; Q3TZD0; -.
DR REPRODUCTION-2DPAGE; Q64139; -.
DR REPRODUCTION-2DPAGE; Q9JKR6; -.
DR CPTAC; non-CPTAC-3714; -.
DR EPD; Q9JKR6; -.
DR jPOST; Q9JKR6; -.
DR MaxQB; Q9JKR6; -.
DR PaxDb; Q9JKR6; -.
DR PeptideAtlas; Q9JKR6; -.
DR PRIDE; Q9JKR6; -.
DR ProteomicsDB; 273064; -.
DR Antibodypedia; 32575; 518 antibodies from 38 providers.
DR DNASU; 12282; -.
DR Ensembl; ENSMUST00000066601; ENSMUSP00000068594; ENSMUSG00000032115.
DR Ensembl; ENSMUST00000160902; ENSMUSP00000125594; ENSMUSG00000032115.
DR Ensembl; ENSMUST00000161318; ENSMUSP00000123700; ENSMUSG00000032115.
DR GeneID; 12282; -.
DR KEGG; mmu:12282; -.
DR UCSC; uc009pdf.2; mouse.
DR CTD; 10525; -.
DR MGI; MGI:108030; Hyou1.
DR VEuPathDB; HostDB:ENSMUSG00000032115; -.
DR eggNOG; KOG0104; Eukaryota.
DR GeneTree; ENSGT00940000157686; -.
DR HOGENOM; CLU_005965_5_0_1; -.
DR InParanoid; Q9JKR6; -.
DR OMA; VHEITME; -.
DR OrthoDB; 708294at2759; -.
DR PhylomeDB; Q9JKR6; -.
DR TreeFam; TF105048; -.
DR BioGRID-ORCS; 12282; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Hyou1; mouse.
DR PRO; PR:Q9JKR6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JKR6; protein.
DR Bgee; ENSMUSG00000032115; Expressed in spermatocyte and 241 other tissues.
DR ExpressionAtlas; Q9JKR6; baseline and differential.
DR Genevisible; Q9JKR6; MM.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
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:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0002931; P:response to ischemia; IDA:ParkinsonsUK-UCL.
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; Stress response.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..999
FT /note="Hypoxia up-regulated protein 1"
FT /id="PRO_5000057827"
FT REGION 567..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:0007744|PubMed:23806337"
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:0000269|PubMed:19349973"
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"
FT CONFLICT 137
FT /note="Q -> L (in Ref. 3; AAH50107)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="N -> D (in Ref. 3; AAH50107)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="T -> A (in Ref. 2; BAE34279)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="Q -> R (in Ref. 2; BAE42657)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="R -> G (in Ref. 4; AAB35051)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="K -> R (in Ref. 3; AAH50107)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="E -> K (in Ref. 3; AAH50107)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="Missing (in Ref. 4; AAB35051)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="P -> L (in Ref. 4; AAB35051)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="D -> N (in Ref. 4; AAB35051)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="Q -> R (in Ref. 3; AAH50107)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="E -> K (in Ref. 3; AAH50107)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="S -> P (in Ref. 3; AAH50107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 111181 MW; 2951482D1EE2EF36 CRC64;
MAATVRRQRP RRLLCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF QHLLGKQADN PHVALYRSRF
PEHELIVDPQ RQTVRFQISP QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPAFF
NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INSTAQNVMF YDMGSGSTVC
TIVTYQTVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFDRVP
GPVQQALQSA EMSLDQIEQV ILVGGATRVP KVQEVLLKAV GKEELGKNIN ADEAAAMGAV
YQAAALSKAF KVKPFVVRDA VIYPILVEFT REVEEEPGLR SLKHNKRVLF SRMGPYPQRK
VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK
AHFNLDESGV LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA
VQEEEESPAE GSKDEPAEQG ELKEEAEPPA EETSQPPPSE PKGDAAREGE KPDEKESGDK
PEAQKPNEKG QAGPEGAAPA PEEDKKPKPA RKQKMVEEIG VELAVLDLPD LPEDELARSV
QKLEELTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSATST
WLEDEGFGAT TVMLKDKLAE LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR
LIPEMDQVFT EVEMTTLEKV INDTWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASAGDQEEK VIPPAGQTEE AKPILEPDKE
ETGTEPADSE PLELGGPGAG PEQEEQSAGQ KRPSKNDEL
