ID   HYOU1_CHICK             Reviewed;        1002 AA.
AC   Q5ZLK7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Hypoxia up-regulated protein 1;
DE   Flags: Precursor;
GN   Name=HYOU1; ORFNames=RCJMB04_5l9;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719727; CAG31386.1; -; mRNA.
DR   RefSeq; NP_001006588.1; NM_001006588.1.
DR   AlphaFoldDB; Q5ZLK7; -.
DR   SMR; Q5ZLK7; -.
DR   STRING; 9031.ENSGALP00000039757; -.
DR   PaxDb; Q5ZLK7; -.
DR   PRIDE; Q5ZLK7; -.
DR   GeneID; 428251; -.
DR   KEGG; gga:428251; -.
DR   CTD; 10525; -.
DR   VEuPathDB; HostDB:geneid_428251; -.
DR   eggNOG; KOG0104; Eukaryota.
DR   InParanoid; Q5ZLK7; -.
DR   OrthoDB; 708294at2759; -.
DR   PhylomeDB; Q5ZLK7; -.
DR   PRO; PR:Q5ZLK7; -.
DR   Proteomes; UP000000539; 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; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1002
FT                   /note="Hypoxia up-regulated protein 1"
FT                   /id="PRO_0000379420"
FT   REGION          576..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           999..1002
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        604..673
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..947
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        948..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1002 AA;  112319 MW;  E0460AA89BF60628 CRC64;
     MARAPRWMLG WLLLACCVPH TEPLAVMSVD MGSESMKIAI VKPGVPMEIV LNKESRRKTP
     VAVALKENER LFGDSALGMS IKTPKVAFRY FQDLLGKQID NPQVALYQSR FPEHELVKDE
     KRQTVIFKLS QTLQYSPEEM LGMVLNYSRG LAEEFAEQPI KDAVITVPAY FNQAERRAVL
     HAARMADLKV LQLINDNTAV ALNYGVSGGK TSMPLHSFSF QNIMFYDMGA GSTVCTIVTY
     QTVKTKDSGT QPQLQIQGIG FDRTLGGLEM ELRLRDYLAK LFNDQHPSKD VRKNPRAMAK
     LLKEANRLKT VLSANADHMA QIEGLLDDID FKAKVSRQEF EDLCSDLFQR VPGPVQQALS
     SAEMNLDGID QVILVGGATR VPKVQEVLLK AVGKEELGKN INADEAAAMG AVYQAAALSK
     AFKVKPFMVR DAAMFPIQVE FTREVEEDDK SKSLKHNKRI LFQRMAPYPQ RKVITFNRYT
     DDFEFYVNYG DLSFLNQDDL RIFGSLNLTT VRLKGVGESF KKHSDYESKG IKAHFNMDES
     GVLSLDRVES VFETLVEDKL EEESTLTKLG NTISSLFGGG GHTPEAGENL TDSVQEEEES
     LAEAAKEEQG VKQGQKSSAE DAGEEQGEEK QQSPHPDQAE AVPPKEESQK NEEGEKSEAR
     DPKEDKETVN EEELSKSSGA GTAAKAEEEK KIKAPKKQKL VHEITMELDV NDVPDLLEDE
     LKSSMKKLQD LTIRDLEKQE REKSANSLES FIFETQDKLY QEEYLFVSTE EEREEISKKL
     SEASNWMEEE GYAAATKELK DKLAELKKLC RNLFFRVEER RKWPERLAAL ESLLNHSNIF
     LKGARMIPES DQIFTEVELG TLEKAINETT VWKNETLAEQ NKLSPAEKPV LLSKDIELKI
     AGLDREVQYL LDKAKFAKPK PKKEKNATKS DSGKNATGTS ESENTIPPTE GKQEEKPEDI
     SPAKEPPTTE KVVTDDEPGS DSSSKKEKKP EAGGESRKND EL