ID A0A8J6HHZ5_TENMO Unreviewed; 1319 AA.
AC A0A8J6HHZ5;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=GEV33_008355 {ECO:0000313|EMBL:KAH0814436.1};
OS Tenebrio molitor (Yellow mealworm beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrio.
OX NCBI_TaxID=7067 {ECO:0000313|EMBL:KAH0814436.1, ECO:0000313|Proteomes:UP000719412};
RN [1] {ECO:0000313|EMBL:KAH0814436.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stoneville {ECO:0000313|EMBL:KAH0814436.1};
RC TISSUE=Whole head {ECO:0000313|EMBL:KAH0814436.1};
RA Eriksson T., Andere A., Kelstrup H., Emery V., Picard C.;
RT "The yellow mealworm (Tenebrio molitor) genome: a resource for the emerging
RT insects as food and feed industry.";
RL J Insects Food Feed 6:445-455(2020).
RN [2] {ECO:0000313|EMBL:KAH0814436.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stoneville {ECO:0000313|EMBL:KAH0814436.1};
RC TISSUE=Whole head {ECO:0000313|EMBL:KAH0814436.1};
RA Eriksson T.;
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a proteasomal ubiquitin receptor. May promote
CC the deubiquitinating activity associated with the 26S proteasome.
CC {ECO:0000256|ARBA:ARBA00054744}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR606539-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004653}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000256|ARBA:ARBA00004198}. Membrane
CC {ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU362033}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ADRM1 family.
CC {ECO:0000256|ARBA:ARBA00009216}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAH0814436.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JABDTM020024288; KAH0814436.1; -; Genomic_DNA.
DR Proteomes; UP000719412; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:TreeGrafter.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005802; C:trans-Golgi network; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006897; P:endocytosis; IEA:TreeGrafter.
DR GO; GO:0045332; P:phospholipid translocation; IEA:TreeGrafter.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:TreeGrafter.
DR CDD; cd13314; PH_Rpn13; 1.
DR FunFam; 3.40.1110.10:FF:000008; Phospholipid-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000009; Phospholipid-transporting ATPase; 1.
DR FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR606539-
KW 2}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR606539-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR606539-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR606539-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000719412};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 759..782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 838..859
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 935..1048
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 1186..1296
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 1096..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1157
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-1"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-3"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-3"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 673
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-3"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-2"
FT BINDING 677
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR606539-3"
SQ SEQUENCE 1319 AA; 146353 MW; 5EAB275C8D12ED98 CRC64;
MGVLASKNSV TCKIHFIGKH DYSQKKRFID EHLNHPLPAN AIVWLQYLYP LNMIGVPPLL
SAECDIPQTE KLEIHELTAR HLLTVPFSRE QQPEMFANTE DDMPETFPDT KLVPLRQHHL
HFRSKLDSLN SDESLDLENT LWTNCVIASG QALGVVIYTG TETRSVMNNS APRSKVGLLD
IEVNTITKLL FVAVIALALI MMALKGFGGP WYRYLFRFIL LFSYIIPISL RVNLELGKSF
YSWAIGKDPS MTGTAVRCTT IPEELGRISY LLSDKTGTLT QNSMVLKRLH LGTVSYAADS
FEELSATLKS TYLGSDTSTS SKTKFRRSEN TRIRDAVQAL ALCHNVTPVY ETSETSETDT
GSIASEAEAD QHLQITEKQV VSYQASSPDE VALVQWTQEV GLALSRRDLS SMQLRGPDDR
LYNYTILQVF PFTSETKRMG IIVKDLQTGE IVFYLKGADV VMSPIVQYTD WLDEEVGNMA
RDGLRTLVVA RKMLSEEQYL DFESRYNAAR LSVTDRVARV AQVVESLERE MELLCITGVE
DKLQDNVRPT LELLRNAGIK IWMLTGDKLE TATCIAKSSR LVSRTQGLHI LKKVVTRTDA
HLELNSFRRK QDCALVISGE SLEVCLSYYQ QEFMELATAA PAVVCCRCSP TQKAQVVQLI
QKHTGKRTAA VGDGGNDVSM IQQADAGIGI EGREGKQASL AGDFSIPQFS HLANLLLVHG
RRSYKRSASL AQFVIHRGLI ISTMQAVFSS VFYLSSVALY QGFLTVGYAT VYTMFPVFSL
VLDQDVSAEI ALTYPELYKE LAKGRSLSYK TFFMWVLISI YQGGVIMYGA LLLFEDEFIH
IVAISFSSLI LTELIMVALN IRTWHYLMIL AELISLVLYL LSLIILHDYF DSEFIRTNDF
IWKVLVITLF HQRRHKMPAG GALFGSAATG PGSTGGNKHL VEVRAGKMNL KGRMVCPDKR
KGLLYVYQSD DSLMHFCWQD RTTGIVEDDL IIFPDDCEYI KVSQCTTGRV YLLKFKSSNR
KFFFWLQEPR TDKDDDNCKR INELLNNPSS AVQSSQSPDQ DLQSLFNNMS QSQLMQLFGS
GVGQMGGLSS LLGTIRGPNS GSARTSTTPA ITHRTTVPST PTTNTTTTTV SQSPVTTTPQ
TTSAPTAAPG APARSTTNSG RTSDSCSHRI QLSDLQNFLQ GITPISSSQQ QSVDLSTALN
ADGLSGILSN PNALEALQNH LPAVEGDPQE ALRSTINSPQ FQQAVSQFSS ALESGQLGPV
VSQLSVNSDA VAAATQGNMQ EFMKALEKDE SSSSKEEPEK DKKEEKKDDK DDDHNMQLD
//
