ID   A0A182Q0R7_9DIPT        Unreviewed;       966 AA.
AC   A0A182Q0R7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Hypoxia up-regulated protein 1 {ECO:0000256|ARBA:ARBA00040503};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF000770-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF000770-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF000770-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   EMBL; AXCN02000185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182Q0R7; -.
DR   STRING; 69004.A0A182Q0R7; -.
DR   EnsemblMetazoa; AFAF000770-RA; AFAF000770-PA; AFAF000770.
DR   VEuPathDB; VectorBase:AFAF000770; -.
DR   OrthoDB; 5491443at2759; -.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          568..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..918
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..966
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   966 AA;  107506 MW;  0677EC68AED61C65 CRC64;
     MGTRQRLCTG GGGRIRAGAW TTKTLLMTLA VMVTVLATVA NGAAVMSVDL GSEWMKVGVV
     SPGVPMEIAL NKESKRKTPT TIAFRNGDRV FGEDAQTLGV RFPANSYGYL IDLLGKTIDN
     PMVDLYRKRF PYYDIVEDPA RRTVVFRTGD EQYTIEELIA QLLQVAKGYA EDSTGQPITE
     CVLIVPGFYG QAERTALVSA ARLANLKVLQ LINDYTAVAL NYGIFRRKEI NETAQYFLFY
     DMGAYKTSAA VVSYQLVKDK ATRETHPVVQ VLGVGFDRTL GGLEMQIRLR DYLGQEFNKQ
     GKTKTDVFSN PRAMAKLFKE AGRLKNVLSA NTEHYAQIEG LLDEQDFRLL VTREQFEGLC
     KDLYERVTAP LDKALAASGL ALDVINQVVL FGGNTRVPKV QDILRTHIGQ ELAKNLNADE
     AACMGAVYRA ADLATGFKVK KFITKDAVLF PLQVVFDREG DSGALRQVRR TLFGAMNSYP
     QKKVITFNKH TDDFEFSVQY AELEPVVGDA VGTVDLARVR LSEVAKKLKA SVTENVESKG
     IKAHFLLDDS GIFSLANVEL VLEKTVTKED DEDESTFQKI GNTISKLFSG DATPEEKPTP
     EGVEKEEEEA TGAKESKEEE QPSKDKVEES GKDAKPEANE TVGDKKTEEG TEAKNATVKP
     KIVTLKETIP SKVDLTYVVP LDGELFEASA KRLAALEEVD NAKKRRETAL NALESFVIDA
     QVKLDEEEYA SCGTEEEIAS IRKRCGEISE WLYEDGSDAD AETYERKLDE LRTVANEVYA
     RHWEHQERPE ALNALKQMIN GSEAFLRNAR NLTKDTNPEK DVFTAVEIET LEKAIRSTIE
     WRDAEVAEQK KLARNAPVRL TVKDITDRMA TLDREVKYLV NKLKLWRPKV KPTPPPKPEK
     TSGKKEDEKS SKEEGQEGEE TAKEEEPVLE QTPDASAEEP TVVDAKEEID PTATEKAHEE
     GDHTEL
//