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Database: UniProt
Entry: A0A383Z0M0_BALAS
LinkDB: A0A383Z0M0_BALAS
Original site: A0A383Z0M0_BALAS 
ID   A0A383Z0M0_BALAS        Unreviewed;       465 AA.
AC   A0A383Z0M0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN   Name=ATP6V1H {ECO:0000313|RefSeq:XP_007168672.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007168672.1};
RN   [1] {ECO:0000313|RefSeq:XP_007168672.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007168672.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
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   RefSeq; XP_007168672.1; XM_007168610.2.
DR   AlphaFoldDB; A0A383Z0M0; -.
DR   GeneID; 103005586; -.
DR   CTD; 51606; -.
DR   OrthoDB; 176803at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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   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; 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; 1.
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:UP000261681};
KW   Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT   DOMAIN          331..446
FT                   /note="ATPase V1 complex subunit H C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11698"
SQ   SEQUENCE   465 AA;  54120 MW;  5911CC0134FE9D7E CRC64;
     MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISSEDCEFI QRFEMKRSPE
     EKQEMLQTEG SQCAKTFINL MTHISKEQTV QYILTVVDDT LQENHQRVSI FFDYAKRSKN
     TAWSYFLPML NRQDLFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQSSQYV
     QCVAGCLQLM LRVNEYRFAW VEADGVNCIM GVLSNKCGFQ LQYQMIFSIW LLAFSPQMCE
     HLRRYNIIPV LSDILQESVK EKVTRIILAA FRNFLEKSTE RETRQEYALA MIQCKVLKQL
     ENLEQQKYDD EDISEDIKFL LEKLGESVQD LSSFDEYSSE LKSGRLEWSP VHKSEKFWRE
     NAVRLNEKNY ELLKILTKLL EVSDDPQVLA VAAHDVGEYV RHYPRGKRVI EQLGGKQLVM
     NHMHHEDQQV RYNALLAVQK LMVHNWEYLG KQLQSEQPQT AAARS
//
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