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