ID D6WVU7_TRICA Unreviewed; 528 AA.
AC D6WVU7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=V-type proton ATPase subunit H variant-2 {ECO:0000313|EMBL:AHY84719.1};
DE SubName: Full=V-type proton ATPase subunit H-like Protein {ECO:0000313|EMBL:EFA08618.1};
GN Name=AUGUSTUS-3.0.2_06281 {ECO:0000313|EMBL:EFA08618.1};
GN Synonyms=VhaSFD {ECO:0000313|EMBL:AHY84719.1};
GN ORFNames=TcasGA2_TC006281 {ECO:0000313|EMBL:EFA08618.1};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA08618.1, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:EFA08618.1, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08618.1,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:EFA08618.1, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08618.1,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
RN [3] {ECO:0000313|EMBL:AHY84719.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Georgia-1 {ECO:0000313|EMBL:AHY84719.1};
RA Xiao D., Gao X., Xu J., Liang X., Li Q., Yao J., Zhu K.Y.;
RT "Clathrin-dependent endocytosis in the red flour beetle.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EFA08618.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA08618.1};
RA Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT "Tools and pipelines for BioNano data: molecule assembly pipeline and FASTA
RT super scaffolding tool.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of the V1 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 and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment (By similarity). Subunit H is
CC essential for V-ATPase activity, but not for the assembly of the
CC complex. {ECO:0000256|ARBA:ARBA00029425}.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC {ECO:0000256|ARBA:ARBA00008613}.
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; KJ476831; AHY84719.1; -; mRNA.
DR EMBL; KQ971358; EFA08618.1; -; Genomic_DNA.
DR RefSeq; NP_001280516.1; NM_001293587.1.
DR AlphaFoldDB; D6WVU7; -.
DR STRING; 7070.D6WVU7; -.
DR EnsemblMetazoa; TC006281_001; TC006281_001; TC006281.
DR GeneID; 657235; -.
DR KEGG; tca:657235; -.
DR CTD; 34997; -.
DR eggNOG; KOG2759; Eukaryota.
DR HOGENOM; CLU_025709_2_0_1; -.
DR InParanoid; D6WVU7; -.
DR OMA; DMLQEDK; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000007266; Linkage group 8.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd00256; VATPase_H; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.25.40.150; V-type ATPase, subunit H, C-terminal domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR PANTHER; PTHR10698; V-TYPE PROTON ATPASE SUBUNIT H; 1.
DR PANTHER; PTHR10698:SF0; V-TYPE PROTON ATPASE SUBUNIT H; 1.
DR Pfam; PF11698; V-ATPase_H_C; 1.
DR Pfam; PF03224; V-ATPase_H_N; 1.
DR PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; ARM repeat; 2.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Transport {ECO:0000256|ARBA:ARBA00023065}.
FT DOMAIN 387..501
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 528 AA; 60625 MW; 29244A5585FBBBEB CRC64;
MSSSQVPAGA DPKIKEIITS LDDEKIDMLA ATSVLQQRAT DIRAQKVNWQ SYFQSQMISQ
DDHQFIAAFD VSDSAKREKL LQTDRLQCAQ TFLNLLGHVS KDQTLQYILV LIDDMLQEDR
SRVEIFHEYA NKKKESVWGP FLNLLNRQDG FITNMTSRII AKIACWSQTP MERSDLHFYL
TWLKDQLKMQ YDDLAVQLAK SDATRGPSGE QATETYTEVS FDEQQTPTEI TNNEYIQSVG
RCLQMMLRID EYRFAFVSVD GISTLLSVLS GRVNFQVQYQ LIFCLWVLTF NPLLAEKMNK
FNVIPILADI LSDSVKEKVT RIILAVFRNL IEKPEDAQVA KEHCIAMVQC KVLKQLNILE
QRKFDDEDVA GDVEFLTEKL QNSVQDLSSF DEYATEVKSG RLEWSPVHKS KFWRENAQRL
NEKNYELLRI LIHLLETSKD PLVLSVASYD IGEYVRHYPR GKHVIEQLGG KQLVMQLLAH
EDPNVRYEAL LAVQKLMVHN WEYLGKQLEK EQSDKTAPKG GAPVAGKA
//