ID A0A1R3RVX9_ASPC5 Unreviewed; 564 AA.
AC A0A1R3RVX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Vacuolar calcium ion transporter {ECO:0000256|RuleBase:RU365028};
GN ORFNames=ASPCADRAFT_204432 {ECO:0000313|EMBL:OOF98648.1};
OS Aspergillus carbonarius (strain ITEM 5010).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF98648.1, ECO:0000313|Proteomes:UP000188318};
RN [1] {ECO:0000313|Proteomes:UP000188318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- FUNCTION: Has a role in promoting intracellular calcium ion
CC sequestration via the exchange of calcium ions for hydrogen ions across
CC the vacuolar membrane. Involved also in manganese ion homeostasis via
CC its uptake into the vacuole. {ECO:0000256|RuleBase:RU365028}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC {ECO:0000256|RuleBase:RU365028}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. {ECO:0000256|ARBA:ARBA00008170, ECO:0000256|RuleBase:RU365028}.
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DR EMBL; KV907495; OOF98648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3RVX9; -.
DR STRING; 602072.A0A1R3RVX9; -.
DR VEuPathDB; FungiDB:ASPCADRAFT_204432; -.
DR OMA; WNPFRHV; -.
DR OrthoDB; 276371at2759; -.
DR Proteomes; UP000188318; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015369; F:calcium:proton antiporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1420.30; NCX, central ion-binding region; 2.
DR InterPro; IPR004713; CaH_exchang.
DR InterPro; IPR004798; CAX-like.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR NCBIfam; TIGR00378; cax; 1.
DR PANTHER; PTHR31503:SF20; CA(2+)_H(+) EXCHANGER, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR31503; VACUOLAR CALCIUM ION TRANSPORTER; 1.
DR Pfam; PF01699; Na_Ca_ex; 2.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|RuleBase:RU365028};
KW Calcium {ECO:0000256|RuleBase:RU365028};
KW Calcium transport {ECO:0000256|RuleBase:RU365028};
KW Ion transport {ECO:0000256|RuleBase:RU365028};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365028};
KW Reference proteome {ECO:0000313|Proteomes:UP000188318};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365028};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365028}; Transport {ECO:0000256|RuleBase:RU365028};
KW Vacuole {ECO:0000256|RuleBase:RU365028}.
FT TRANSMEM 164..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 224..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 252..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 288..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 324..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 475..503
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 509..530
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365028"
FT DOMAIN 192..344
FT /note="Sodium/calcium exchanger membrane region"
FT /evidence="ECO:0000259|Pfam:PF01699"
FT DOMAIN 411..555
FT /note="Sodium/calcium exchanger membrane region"
FT /evidence="ECO:0000259|Pfam:PF01699"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 61407 MW; F9AD2945D675C248 CRC64;
MHIYKRHARK LAWYDQEGEP SSHNPFKKFR RQPRRTNSIQ LENRLTPIMS EGDMRLSEER
RRRRDMTDGL VGPEHADSFP PQSAGTDMMA RTESGDKVGT DPSMHSQVPI NVPLQDEPGD
MQGPRKRRTF MSNTLNPGDD RLTSDTGKPV AEKRKFTAMG QLKATIFNSW INVLLVAAPV
GIALNYVNVS PVAVFVVNFI AIIPLAAMLS YATEEIAMRT GETIGGLLNA TFGNAVELIV
AIIALVDNEV TIVQTSLIGS MLSNLLLVMG MCFFFGGVDR LEQHFNPVVA QTAASLLALA
VGSLIIPTAF HAWSDAGDAG VAPLSRGTSV ILLVVYGCYL FFQLKSHTEI YNAPSPKVEK
RRQKVNEGDA SRGIAQIGKM SASMAGEYAQ KVELQEPEDD AEEPQLSVTV AVLTLVISTV
FVALCAEFMV DSIDALTTQG HISETFVGLI LLPIVGNAAE HATAVTVACK DKMDLAIGVA
VGSSMQIALL VLPLIIVIGW GMGNDDMTLY FDAFQVILLF VAVLLVNYLI ADGKSHWLEG
VLLMMMYLII AVAAWFYPSK TDAT
//
