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HYOU1_DANRE
ID   HYOU1_DANRE             Reviewed;         980 AA.
AC   Q7ZUW2; Q6IQN2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Hypoxia up-regulated protein 1;
DE   Flags: Precursor;
GN   Name=hyou1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2004) 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; BC047807; AAH47807.1; -; mRNA.
DR   EMBL; BC071372; AAH71372.1; ALT_TERM; mRNA.
DR   RefSeq; NP_997868.1; NM_212703.1.
DR   AlphaFoldDB; Q7ZUW2; -.
DR   SMR; Q7ZUW2; -.
DR   STRING; 7955.ENSDARP00000090804; -.
DR   PaxDb; Q7ZUW2; -.
DR   PeptideAtlas; Q7ZUW2; -.
DR   PRIDE; Q7ZUW2; -.
DR   GeneID; 327133; -.
DR   KEGG; dre:327133; -.
DR   CTD; 10525; -.
DR   ZFIN; ZDB-GENE-030131-5344; hyou1.
DR   eggNOG; KOG0104; Eukaryota.
DR   InParanoid; Q7ZUW2; -.
DR   OrthoDB; 708294at2759; -.
DR   PhylomeDB; Q7ZUW2; -.
DR   PRO; PR:Q7ZUW2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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; 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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Endoplasmic reticulum; Nucleotide-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..980
FT                   /note="Hypoxia up-regulated protein 1"
FT                   /id="PRO_0000379421"
FT   REGION          558..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           977..980
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        564..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..980
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        599
FT                   /note="A -> T (in Ref. 1; AAH71372)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        635
FT                   /note="D -> E (in Ref. 1; AAH71372)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   980 AA;  110320 MW;  8CC2B1D5C4E80433 CRC64;
     MREKLSLWAI FCLVVAFLPS QTESVAVMSV DLGSEWMKVA IVKPGVPMEI VLNKESRRKT
     PVAVCLKENE RLFGDGALGV AVKNPKVVYR FLQSILGKTA DNPQVAEYQK HFPEHQLQKD
     EKRGTVYFKF SEEMQYTPEE LLGMILNYSR TLAQDFAEQP IKDAVITVPA YFNQAERRAV
     LQAAHIAGLK VLQLINDNTA VALNYGVFRR KDINSTAQNI MFYDMGSGST TATIVTYQTV
     KTKESGTQPQ LQIRGVGFDR TLGGFEMELR LRDHLAKLFN EQKKSKKDVR DNLRAMAKLL
     KEAQRLKTVL SANAEHTAQI EGLMDDIDFK AKVTRSEFEA LCEDLFDRVP GPVKQALAAA
     EMSMDEIEQV ILVGGATRVP KVQDVLLKSV GKEELSKNIN ADEAAAMGAV YQAAALSKAF
     KVKPFLVRDA AVFPIQVEFS RETEEEDGVK SLKHNKRILF QRMAPYPQRK VITFNRYIDD
     FVFYINYGDL SFLSEQDMKV FGSQNLTTVK LSGVGSSFKK HSDAESKGIK AHFNMDESGV
     LILDRVESVF ETIVEEKEEE STLTKLGNTI SSLFGGGSSE PSANVTEPVT DEEEVTPEAG
     KEQDQPEKQE ETVQEKPETE EGKEAEPQAE EQKEDKEKAE NQGETESEKT EKPEEKTTDE
     EKEADMKPKL QKKSKISADI AVELEVNDVL DPSAEDMEGS KKKLQDLTDR DLEKQEREKT
     LNSLEAFIFE TQDKLYQDEY QAVVTEEEKE QISGRLSVAS SWMDEEGYRA GTKLLKEKLS
     ELKKLCKGMF FRVEERKKWP DRLAALDSML NHSNIFLKSA RLIPESDQIF TDVELKTLEK
     VINETITWKN ETVAEQEKLS PTVKPVLLSK DIEAKLSLLD REVNYLLNKA KFAKPKPKDK
     AKDKNSTSES SKANSTDDAE KVIPPKTEDG AEKVKPAEEP PVVEEKAEET ILELNPAENT
     DDKTESTESS KSENHIEDEL
 
 
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