ID   HYOU1_XENTR             Reviewed;         643 AA.
AC   Q0VA61;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Hypoxia up-regulated protein 1;
DE   Flags: Precursor; Fragment;
GN   Name=hyou1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BC121233; AAI21234.1; ALT_TERM; mRNA.
DR   RefSeq; NP_001263614.1; NM_001276685.2.
DR   RefSeq; NP_001263615.1; NM_001276686.1.
DR   AlphaFoldDB; Q0VA61; -.
DR   SMR; Q0VA61; -.
DR   STRING; 8364.ENSXETP00000022209; -.
DR   PaxDb; Q0VA61; -.
DR   PRIDE; Q0VA61; -.
DR   GeneID; 779444; -.
DR   KEGG; xtr:779444; -.
DR   CTD; 10525; -.
DR   Xenbase; XB-GENE-921821; hyou1.
DR   eggNOG; KOG0104; Eukaryota.
DR   InParanoid; Q0VA61; -.
DR   OrthoDB; 708294at2759; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
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   GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central.
DR   GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Endoplasmic reticulum; Nucleotide-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..643
FT                   /note="Hypoxia up-regulated protein 1"
FT                   /id="PRO_0000379423"
FT   REGION          565..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         643
SQ   SEQUENCE   643 AA;  72301 MW;  C18F59C40E71BB01 CRC64;
     MRPLVCVFTM FLLALLSSNT ESVAVMSVDM GSEWMKIAIV KPGVPMEIVL NKESRRKTPV
     AIALKENERL FGDSALGMAV KNPKVTFRYF QDLLGKRADN PHVKAFEARF PEYQLVKDEH
     RETVLFKLSE ELTYSPEELL GMMLNYSRSL AEEFAEQPVK DVVITVPAFF NQAERRAVLQ
     AAQLSDLKVL QLINDNTAVA LNYGVFRRKD INATAQNIMF YEMGSRSTIC TIVTYQSVKT
     KDSGMQPQLQ IRGVGFDRTL GGIEMDLRLR DHLAKLFNEQ KKSKKDVREN QRAMSKLLKE
     ANRVKTILSA NNDHMAQIEG LMDDIDFKAK VTRQELEDLC ADLFNRVSAP VQHALSSAEM
     KMEEIDQVIL VGGATRVPKV QELLLKVVGK EELGKNINAD EAAAMGAVYQ AAALSKAFKV
     KPFIVRDAAI FPIQVEFTRE VEEEDHSKSL KHNKRILFQR LAPYPQRKVI TFNRYTDNFA
     FSINYGDLSY LGPDDLKVFG SLNLTTVKLN GVGESFQKRS DYESKGIKAH FNMDESGLLT
     LDRVEAVFET VVDEKPEQES TLTKLGNTIS SLFGGGSSVP ETKENATDSV QEEDEVPTEP
     TKEEEQESAD AADKQKDKEK GTTATNEEEE GKKEEEKSEP QEE