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Database: UniProt
Entry: H3CT55_TETNG
LinkDB: H3CT55_TETNG
Original site: H3CT55_TETNG 
ID   H3CT55_TETNG            Unreviewed;       950 AA.
AC   H3CT55;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Hypoxia up-regulated protein 1 {ECO:0000256|ARBA:ARBA00040503};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000011439.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000011439.1}
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; H3CT55; -.
DR   STRING; 99883.ENSTNIP00000011439; -.
DR   Ensembl; ENSTNIT00000011621.1; ENSTNIP00000011439.1; ENSTNIG00000008598.1.
DR   GeneTree; ENSGT00940000157686; -.
DR   HOGENOM; CLU_005965_5_0_1; -.
DR   InParanoid; H3CT55; -.
DR   OMA; SRTPMIQ; -.
DR   TreeFam; TF105048; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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:UP000007303};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..950
FT                   /note="Hypoxia up-regulated protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003581201"
FT   REGION          562..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   950 AA;  106458 MW;  D6992E0B5B787C66 CRC64;
     FSQLIMEGRK LALVAIFSLV LSSLPSHTVS VAVMSVDLGS EWMKMAIVKP GVPMEIVLNK
     ESRRKTPTAV CLKENERLFG DSALGMSVKN PRSVYLHLQS LLGKKHGNLQ VALYQKRFPE
     HQLQEDSVRG TAYFKYSQEM QYTAEELLGM VLNYSRVLAQ DFAEQPIKDA VITVPAFFNQ
     AERRAVLQAA QLAGLKVLQL INDNTAVALN YGVFRRKDID STAKNVMFYD MGSGSTTATI
     VTYQTVKTKE SGTQPQLQIR GVGFDRGLGG FEMDLRLRDH LAKLFNGQKK SGKDVRENHR
     AMAKLLKEAQ RLKTVLSANV DFMAQVEGLM DDIDFKAKVT RAEFEDLCAD LFERVPQPVR
     DALSTAEMTM SEIEQVILVG GSTRVPKVQE VLLKAVGKEE LGKNINADEA AAMGAVYQAA
     ALSKAFKVKP FLVRDAAVFP IQVDFTRETE EEGTKTVKHN KRILFDRMAP YPQRKVITFN
     RYNADFAFDI NYGDLSFLSK EDISVFGSLN LTTVKLSGVG SSFQKHADAE SKGIKAHFNM
     DESGVLLLDR VESVFETMEE EKEEESTLTK LGNTISTLFG GGSSEPTPNV TEPVQDEEEV
     PPESGTEDEA EEKTQKPEET GSKTNPKVRG VVSAGRSVAL KRQTWRRFYA LLVKGEQDNK
     TSGEADAERK AKPKKKSKIS EDIAVELLIN DVLDPTPEEL TSSKKKLQDL TDRDMAKHER
     EKTLNSLEAF IFETQDKLYQ EEYQFVVSEE EKEQISGKLR DASEWMDEDG YAATTKQLRE
     KLSQLKSSCK DMFFRVEERR KWPEHLAALE SMLNTSSFFL RSAKLIPEDD QIFTEVELNL
     LEKVINETTT WKNETVAEQE KRSPQERPIL LSKDIESKLA LLDREVNYLL NKAKFAKPKA
     KAKAKNSTSA DKDNSTSEEK TIPPAEQEKA PPPTVADTEA KSDSFPGPTE
//
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