ID Q22758_CAEEL Unreviewed; 925 AA.
AC Q22758;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 175.
DE SubName: Full=Hypoxia up-regulated protein 1 {ECO:0000313|EMBL:CCD66143.1};
GN ORFNames=CELE_T24H7.2 {ECO:0000313|EMBL:CCD66143.1}, T24H7.2
GN {ECO:0000313|EMBL:CCD66143.1, ECO:0000313|WormBase:T24H7.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD66143.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD66143.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD66143.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; BX284602; CCD66143.1; -; Genomic_DNA.
DR PIR; G88175; G88175.
DR RefSeq; NP_495249.1; NM_062848.3.
DR AlphaFoldDB; Q22758; -.
DR SMR; Q22758; -.
DR STRING; 6239.T24H7.2.1; -.
DR EPD; Q22758; -.
DR PaxDb; 6239-T24H7-2; -.
DR PeptideAtlas; Q22758; -.
DR EnsemblMetazoa; T24H7.2.1; T24H7.2.1; WBGene00020781.
DR GeneID; 174033; -.
DR KEGG; cel:CELE_T24H7.2; -.
DR UCSC; T24H7.2.1; c. elegans.
DR AGR; WB:WBGene00020781; -.
DR WormBase; T24H7.2; CE02884; WBGene00020781; -.
DR eggNOG; KOG0104; Eukaryota.
DR HOGENOM; CLU_005965_5_0_1; -.
DR InParanoid; Q22758; -.
DR OMA; VNQQAHI; -.
DR OrthoDB; 5491443at2759; -.
DR PhylomeDB; Q22758; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00020781; Expressed in adult organism and 4 other cell types or tissues.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
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:0006950; P:response to stress; IEA:UniProt.
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; 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:SF9; PROTEIN CBG02604; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:Q22758,
KW ECO:0007829|PeptideAtlas:Q22758};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..925
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004201142"
FT REGION 574..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 679..706
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 580..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 104211 MW; E0E9B8964CC6CE34 CRC64;
MRLHGTVLLV ILLGCLFATS DGQLAAMTID LGTQFLKIGI VKPGIPMDIA LNTESRRKTP
NVVMIQDGHR TFADAAIGMQ VRYPHLVHGQ LNDLVGKSTQ HPSFELFKRR NTFFEVDDAP
KNASSINFKL GGESYTVEAL TAMILANAKK FTEEYAQAAE IKDVVITVPV YFTPAERLAV
ERAAQMAGLT VLQLINDGTA AALSHGIFRR KEIGEKPQRL MVYDMGAAKT TATIVEFKLV
KEKYEKQPKM TVLGVGFDRT LGGIEMTNRL RDHLIEMFEK NYKPKTKVNT NRRAMTKFSK
EAERLKQVLS ANAEHFAQIE SAHEDIDAKL KVTREDFNHL ISDMESRFGE PIEQALRMAQ
IPIDDIDQFV LMGAGTRVPK VQEIVQKTIG TKEIGKFLNT DEAVAMGALF QAAHLSKGFK
VKPFNIEEKV IFPVEVHFVS KIRDEKTEEI TGEKNVVKTL FAANSVYPTH PKTISLTSYS
DDFSVALKYG KIESFTKQQV QEIGSLLDNL VDVEISGLSE ALKNRSSEES EFKGVKVSFI
VDASGIVRVR RAEALFEPKS GLVGSIASTI SGLFSSKTEE GEPTTDDSTP QSTEEKTEEK
ESVKVEDSTP EPEPETPVNS TSEESPKTNE TEKNASSGNA TEVKEKKKEL PSIVRLRITN
KYPSAFVPNK YDVQEEKRRM EAFAEKERLA SERAAVENEL ESFNFECSQY LEETEFTDYM
ADEEKTKLED SVKRIRAWLE DDVTKDTPTK DFTDNLLELK NVVRSVKKRQ EHDKAVPEKL
KSLETLLETT FSLTTLGNNV DEEKALFKKE DRDGLKSKLD KLKIWVTDVR KHLDLKKKTD
DFNFTGKDID TKTKNLNREV DRFMKKMKKI TTLDDLAKDG KIDIDTIVEE AEKKKAEQDK
KKEKKSTKKA NESKVENESE IKTEL
//
