ID   A0A2K5YJR6_MANLE        Unreviewed;       989 AA.
AC   A0A2K5YJR6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Hypoxia up-regulated protein 1 {ECO:0000256|ARBA:ARBA00040503};
GN   Name=HYOU1 {ECO:0000313|Ensembl:ENSMLEP00000015755.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000015755.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000015755.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A2K5YJR6; -.
DR   Ensembl; ENSMLET00000039217.1; ENSMLEP00000015755.1; ENSMLEG00000031666.1.
DR   GeneTree; ENSGT00940000157686; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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:UP000233140};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..989
FT                   /note="Hypoxia up-regulated protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014366458"
FT   REGION          564..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..989
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   989 AA;  110298 MW;  9A19CAB3C7C61FCA CRC64;
     MTVKVRRQRP RRRVFWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
     NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF QHLLGKQADN PHVALYQARF
     PEHELTFDPQ RQTVHFQISR QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPVFF
     NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC
     TIVTYQMVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAGLFNEQ RKGQRAKDVR
     ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFERVP
     GPVQQALQSA EMSLDEIEQV ILVGGATRVP KVQEVLLKAV GKEELGKNIN ADEAAAMGAV
     YQAAALSKAF KVKPFVVRDA VVYPILVEFT REVEEEPGVH SLKHNKRVLF SRMGPYPQRK
     VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK
     AHFNLDESGV LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT
     VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPLPPE PKGDAAPEGE KATEKENGDK
     SEAQKPSEKA EAGPEGIAPA PEGEKKQKPA RKQRMVEEIG VELVVLDLPD LPEDKLAQSV
     QKLQDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSAAST
     WWNGSSPSSP RMLKEKLAEL RKLCQGLFFR VEERKKWPER LSALDNLLNH SSMFLKGARL
     IPEMDQIFTE VEMTTLEKVI NETWAWKNAT LAEQAKLPAT EKPVLLSKDI EAKMMALDRE
     VQYLLNKAKF TKPRPRPKDK NGTRAEPPLN ASASDQGEKV ILPAGEGRVP GSGSEPGDTE
     PLELGGPGAE PEQKEQSTGQ KRPLKNDEL
//