ID   VA0D_MANSE              Reviewed;         348 AA.
AC   Q25531;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=V-type proton ATPase subunit d;
DE            Short=V-ATPase subunit d;
DE   AltName: Full=M40;
DE   AltName: Full=V-ATPase 40 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit d;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9271213; DOI=10.1016/s0014-5793(97)00699-6;
RA   Merzendorfer H., Harvey W.R., Wieczorek H.;
RT   "Sense and antisense RNA for the membrane associated 40 kDa subunit M40 of
RT   the insect V-ATPase.";
RL   FEBS Lett. 411:239-244(1997).
CC   -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying a
CC       variety of intracellular compartments in eukaryotic cells, thus
CC       providing most of the energy required for transport processes in the
CC       vacuolar system (By similarity). May play a role in coupling of proton
CC       transport and ATP hydrolysis (By similarity).
CC       {ECO:0000250|UniProtKB:P51863, ECO:0000250|UniProtKB:P61421}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits VhaAC45 and ATP6AP2 (By similarity).
CC       {ECO:0000250|UniProtKB:P61421}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; X98825; CAA67343.1; -; mRNA.
DR   AlphaFoldDB; Q25531; -.
DR   SMR; Q25531; -.
DR   DIP; DIP-61396N; -.
DR   IntAct; Q25531; 1.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 1.10.132.50; -; 1.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR036079; ATPase_su_c/d_sf.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR   InterPro; IPR035067; V-type_ATPase_suC/d.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..348
FT                   /note="V-type proton ATPase subunit d"
FT                   /id="PRO_0000119355"
SQ   SEQUENCE   348 AA;  39596 MW;  016BD4600B6EF098 CRC64;
     MKGCIFNIDA GYLEGLCRGF KCGILKQSDY LNLVQCETLE DLKLHLQGTD YGTFLANEPS
     PLSVSTIDDK LREKLVIEFQ HLRNHSVEPL STFLDFITYS YMIDNIILLI TGTLHQRPIS
     ELIPKCHPLG SFEQMEAIHV AATPAELYNA VLVDTPLAPF FVDCISEQDL DEMNIEIIRN
     TLYKAYLEAF YDFCKQIGGT TADVMCEILA FEADRRAIII TINSFGTELS KDDRAKLYPR
     CGKLNPDGLA ALARADDYEQ VKAVAEYYAE YSALFEGAGN NVGDKTLEDK FFEHEVNLNV
     HAFLQQFHFG VFYSYLKLKE QECRNIVWIS ECVAQKHRAK IDNYIPIF