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Database: UniProt
Entry: A9V9J6_MONBE
LinkDB: A9V9J6_MONBE
Original site: A9V9J6_MONBE 
ID   A9V9J6_MONBE            Unreviewed;       506 AA.
AC   A9V9J6;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN   ORFNames=MONBRDRAFT_34046 {ECO:0000313|EMBL:EDQ85875.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ85875.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ85875.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
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. V-ATPase is responsible for acidifying and maintaining the pH
CC       of intracellular compartments. {ECO:0000256|PIRNR:PIRNR032184}.
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. {ECO:0000256|PIRNR:PIRNR032184}.
CC   -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC       {ECO:0000256|ARBA:ARBA00008613, ECO:0000256|PIRNR:PIRNR032184}.
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DR   EMBL; CH991570; EDQ85875.1; -; Genomic_DNA.
DR   RefSeq; XP_001749354.1; XM_001749302.1.
DR   AlphaFoldDB; A9V9J6; -.
DR   STRING; 81824.A9V9J6; -.
DR   EnsemblProtists; EDQ85875; EDQ85875; MONBRDRAFT_34046.
DR   GeneID; 5894568; -.
DR   KEGG; mbr:MONBRDRAFT_34046; -.
DR   eggNOG; KOG2759; Eukaryota.
DR   InParanoid; A9V9J6; -.
DR   OMA; DMLQEDK; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-UniRule.
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; 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   SUPFAM; SSF48371; ARM repeat; 2.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|PIRNR:PIRNR032184};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|PIRNR:PIRNR032184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW   Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT   DOMAIN          374..489
FT                   /note="ATPase V1 complex subunit H C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11698"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  56217 MW;  64E92F5D2C1436B2 CRC64;
     MAATASTTNP QSGSAAGFED PRKNSILEQA ERIRSHKVPW EAFSGIAGDE AVAAIKQLDG
     SSESTAAELA KADPKALIAT LKLFSKLSNA VTLEYLVTLL DDFAELDSAH TSRIMSAGEK
     LEDGKADTSI DIFVKRLAAD NDYVAHQAAR MLARFALDGF KFEEDAIKKY LDWAANRIAS
     GDRPGVLLAL TSLSRTFRKD EFREGAVKHA TLLDVLKTLL TSTSQIQTQY QVLLVLWVLT
     FTEHSVAGMR QHAHALLTPT AEIMKAASKE KVVRMAFGFA RNMIVKSAKN DGHEYCALLI
     KCVRSLTCPS APGTDSHIVT HLHLASIYPP TPPHSHKVMP RVTELVTQQP YSDEDLLQDA
     TEISEQLKMV FESLSSYDEY LVEAKSGALR WSPVHRSERF WHESVARFND NDYELLKIVA
     AYLDREDDAE SVAVAIHDCG EYVRHYPYGK NALSKLGAKE KIMALMEGRD QRVRYEALIA
     VQKMMTDHWE FLGQQTRKVA EGVATK
//
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