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Database: UniProt
Entry: A0A2K3K4D5_TRIPR
LinkDB: A0A2K3K4D5_TRIPR
Original site: A0A2K3K4D5_TRIPR 
ID   A0A2K3K4D5_TRIPR        Unreviewed;        95 AA.
AC   A0A2K3K4D5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=V-type proton ATPase subunit c1 {ECO:0000313|EMBL:PNX61157.1};
DE   Flags: Fragment;
GN   ORFNames=L195_g060530 {ECO:0000313|EMBL:PNX61157.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNX61157.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNX61157.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX61157.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNX61157.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX61157.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
CC   -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC       integral V0 complex of vacuolar ATPase. V-ATPase is responsible for
CC       acidifying a variety of intracellular compartments in eukaryotic cells.
CC       {ECO:0000256|ARBA:ARBA00002481}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004128}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000256|ARBA:ARBA00007296}.
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:PNX61157.1}.
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DR   EMBL; ASHM01140450; PNX61157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3K4D5; -.
DR   EnsemblPlants; Tp57577_TGAC_v2_mRNA29120; Tp57577_TGAC_v2_mRNA29120; Tp57577_TGAC_v2_gene28167.
DR   Gramene; Tp57577_TGAC_v2_mRNA29120; Tp57577_TGAC_v2_mRNA29120; Tp57577_TGAC_v2_gene28167.
DR   Proteomes; UP000236291; Unassembled WGS sequence.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   NCBIfam; TIGR01100; V_ATP_synt_C; 1.
DR   PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR   PANTHER; PTHR10263:SF57; V-TYPE PROTON ATPASE SUBUNIT C5; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
PE   3: Inferred from homology;
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236291};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   TRANSMEM        30..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..50
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PNX61157.1"
FT   NON_TER         95
FT                   /evidence="ECO:0000313|EMBL:PNX61157.1"
SQ   SEQUENCE   95 AA;  9306 MW;  B8E675E2251A0399 CRC64;
     GMGAAYGTAK SGVGVASMGV MRPELVMKSI VPVVMAGVLG IYGLIIAVII STGINPKAKS
     YYLFDGYAHL SSGLACGLAG LSAGMAIGIV GDAGV
//
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