ID   HYOU1_XENLA             Reviewed;         646 AA.
AC   Q566I3; Q6DCF7; Q7ZYD2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Hypoxia up-regulated protein 1;
DE   Flags: Precursor; Fragment;
GN   Name=hyou1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20029839; DOI=10.1002/pmic.200900281;
RA   Devreese B., Sergeant K., Van Bakel N.H., Debyser G., Van Beeumen J.,
RA   Martens G.J., Van Herp F.;
RT   "A proteome map of the pituitary melanotrope cell activated by black-
RT   background adaptation of Xenopus laevis.";
RL   Proteomics 10:574-580(2010).
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; BC043837; AAH43837.1; ALT_TERM; mRNA.
DR   EMBL; BC078088; AAH78088.1; ALT_TERM; mRNA.
DR   EMBL; BC093532; AAH93532.1; ALT_TERM; mRNA.
DR   AlphaFoldDB; Q566I3; -.
DR   SMR; Q566I3; -.
DR   PRIDE; Q566I3; -.
DR   Proteomes; UP000186698; Genome assembly.
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; 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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Endoplasmic reticulum; Nucleotide-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..646
FT                   /note="Hypoxia up-regulated protein 1"
FT                   /id="PRO_0000379422"
FT   REGION          572..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        603
FT                   /note="E -> D (in Ref. 1; AAH43837)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         646
SQ   SEQUENCE   646 AA;  72674 MW;  880943A0CC059B11 CRC64;
     MRPLVCVLWM FLFALLSSHT ESVAVMSVDL GSEWVKVAIV KPGVPMEIVL NKESRRKTPA
     AIALKENERL FGENALGMAV KNPKVTFRYF QDLLGKRLDN PQVQAFEARF PEYHLVKDER
     RETVLFKLSE DLTYSPEELL GMVLNYSRSL AEDFAEQPVK DVVITVPAFF NQAERRAVLQ
     AAQLSGLKVL QLINDNTAVA LNYGVFRRKD INATAQNVMF YDMGTRSTIC TIVTYQTIKT
     KDSGTQPQLQ IRGVGFDRTL GGLEIDLRLR DHLAKLFNEQ KKSKKDVREN QRAMNKLLKE
     ANRVKTILSA NNDHMAQIEG LMDDIDFKAK VTRQELEDLC ADLFNRVSAP VQQALASAEM
     KMEEIDQVIL VGGATRVPKV QEFLLKVVGK EELSKNINAD EAAAMGAVYQ AAALSKAFKV
     KPFIVRDAAI FPIQVEFTRE VEEENHSKSL KHNKRILFQR LAPYPQRKVI TFNRYTDDFA
     FSINYGDLSY LGPEDLKVFG SLNLTTVKLN GVGESFQKRS DYESKGIKAH FNMDESGLLT
     LDRVEAVFET VADEKPELES TLTKLGNTIS SLFGGGSSVS ETKENVTDSV QEEDEVPTEP
     TKEEEQESAD PADKQQDKEN NKEKGTSATN EKEEGKKEEE KAEPQE