ID   G3Q9L0_GASAC            Unreviewed;       998 AA.
AC   G3Q9L0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Hypoxia up-regulated protein 1 {ECO:0000256|ARBA:ARBA00040503};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000026575.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000026575.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000026575.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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.
CC       {ECO:0000256|ARBA:ARBA00037692}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   AlphaFoldDB; G3Q9L0; -.
DR   STRING; 69293.ENSGACP00000026575; -.
DR   Ensembl; ENSGACT00000026626.1; ENSGACP00000026575.1; ENSGACG00000020113.1.
DR   eggNOG; KOG0104; Eukaryota.
DR   GeneTree; ENSGT00940000157686; -.
DR   InParanoid; G3Q9L0; -.
DR   OMA; SRTPMIQ; -.
DR   TreeFam; TF105048; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000020113; Expressed in mesonephros and 13 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10230; HYOU1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT   REGION          583..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        918..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  111654 MW;  1602BBBBC1F0C1D2 CRC64;
     AGDKGNRKRK TASISHACVT VSLVQHTRFL MCLAVTVAVM SIDLGSEWMK VAIVKPGVPM
     EIVLNKESRR KTPTAVCLKE NERFLGDSAL GMSVKNPTTV YRHLQGLLGK KYDNLQVALY
     QKRFPEHQLL EDPVRGTVYF KNSEEMQFTP EELLGMLLNY SRGLAQDFAE QPIKDAVITV
     PAFFNQAERR AVLQAAQMAG VKVLQLINDN TAVALNYGVF RRKDIDNTVK NVMFYDMGSG
     STTATIVTYQ TVKTKEAGTQ PQLQIRGVGF DRGLGGFEMD LRLRDHLAKL FNEQKKSKKD
     VRENQRAMAK LLKEAQRLKT VLSANVDFMA QVEGLMDDID FKAKVTRTEF EELCADLFER
     VPGPVQEALT TAEMKLEEIE QVILVGGSTR VPKVQEVLLK AVEKEELGKN INADEAAAMG
     AVYQAAALSK AFKVKPFLVR DAAIFPIQVE FTRETEEEGL KIHKHNKRVL FQRMAPYPQR
     KVITFNRYSA DFAFYINYGD LSFLSQHDLS VFGSLNLTTV KLSGVGDSFQ KHTDAESKGI
     KAHFNMDESG VLLLDRVESV FETIVEDKEE ESTLTKLGNT ISTLFGGGSS EPSLNATEPV
     QDEEEVPPES EKDGKEEEGK AEGEKEEAAK EKQEEAEKSA DEETSQEKTE ETGSKTDAKE
     EDGEKSVNAE AEKDAEKDAE KQTKPQKKSK IAEEITVELV INDILDPTLD DVTSSKKKLQ
     DLTDRDLAKQ EREKSLNSLE AFIFETQDKL YQEDYQQVVS EEEKEQISSK LSEASEWMDE
     DGYAATTKQL REKLSQLKSL CKDMFFRVEE RRKWPDRLAA LDSMLNTSSF FLRSAKLIPE
     DDQIFTQVEL NTLEKVINET AKWKNETVAA QEKNSLTERP VLLSKDIESK LTLLDREVNY
     LLNKAKFAKP KAKAKAKNGT SSGKSSKGNN TEDKVIPPTE ESTDTKTANT ENSEEVQPGQ
     APPTEESTEH TGSDSQSQPT EETKTTGRSA TPVADDAR
//