ID G7PS17_MACFA Unreviewed; 803 AA.
AC G7PS17;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Transitional endoplasmic reticulum ATPase {ECO:0000256|ARBA:ARBA00019970};
DE EC=3.6.4.6 {ECO:0000256|ARBA:ARBA00012674};
DE AltName: Full=15S Mg(2+)-ATPase p97 subunit {ECO:0000256|ARBA:ARBA00031475};
DE AltName: Full=Valosin-containing protein {ECO:0000256|ARBA:ARBA00031860};
DE Flags: Fragment;
GN ORFNames=EGM_06879 {ECO:0000313|EMBL:EHH57283.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH57283.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH57283.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000161};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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DR EMBL; CM001290; EHH57283.1; -; Genomic_DNA.
DR AlphaFoldDB; G7PS17; -.
DR eggNOG; KOG0730; Eukaryota.
DR Proteomes; UP000009130; Chromosome 15.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:UniProt.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0033554; P:cellular response to stress; IEA:UniProt.
DR CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 6.10.20.150; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01243; CDC48; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF69; TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 2.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}.
FT DOMAIN 22..105
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 122..188
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 234..370
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 507..646
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 705..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH57283.1"
FT NON_TER 803
FT /evidence="ECO:0000313|EMBL:EHH57283.1"
SQ SEQUENCE 803 AA; 89034 MW; F374577EC6486350 CRC64;
ASSSKGDDLS TAILKQKNRP NRLIVDEAIN EDNSVVSLSQ PKMDELQLFR GDTVLLKGKK
RREAVCIVLS DDTCSDEKIR MNRVVRNNLR VRLGDVISIQ PCPDVKYGKR IHVLPIDDTV
EGITGNLFEV YLKPYFLEAY RPIRKGDIFL VRGGMRAVEF KVVETDPSPY CIVAPDTVIH
CEGEPIKRED EEESLNEVGY DDIGGCRKQL AQIKEMVELP LRHPALFKAI GVKPPRGILL
YGPPGTGKTL IARAVANETG AFFFLINGPE IMSKLAGESE SNLRKAFEEA EKNAPAIIFI
DELDAIAPKR EKTHGEVERR IVSQLLTLMD GLKQRAHVIV MAATNRPNSI DPALRRFGRF
DREVDIGIPD ATGRLEILQI HTKNMKLADD VDLEQVANET HGHVGADLAA LCSEAALQAI
RKKMDLIDLE DETIDAEVMN SLAVTMDDFR WALSQSNPSA LRETVVEVPQ VTWEDIGGLE
DVKRELQELV QYPVEHPDKF LKFGMTPSKG VLFYGPPGCG KTLLAKAIAN ECQANFISIK
GPELLTMWFG ESEANVREIF DKARQAAPCV LFFDELDSIA KARGGNIGDG GGAADRVINQ
ILTEMDGMST KKNVFIIGAT NRPDIIDPAI LRPGRLDQLI YIPLPDEKSR VAILKANLRK
SPVAKDVDLE FLAKMTNGFS GADLTEICQR ACKLAIRESI ESEIRRERER QTNPSAMEVE
EDDPVPEIRR DHFEEAMRFA RRSVSDNDIR KYEMFAQTLQ QSRGFGSFRF PSGNQGGAGP
SQGSGGGTGG SVYTEDNDDD LYG
//
