ID Q6CA91_YARLI Unreviewed; 1254 AA.
AC Q6CA91;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 24-JAN-2024, entry version 137.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=YALI0_D04873g {ECO:0000313|EMBL:CAG80609.2};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG80609.2, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG80609.2, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU361146}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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; CR382130; CAG80609.2; -; Genomic_DNA.
DR RefSeq; XP_502421.2; XM_502421.2.
DR AlphaFoldDB; Q6CA91; -.
DR STRING; 284591.Q6CA91; -.
DR EnsemblFungi; CAG80609; CAG80609; YALI0_D04873g.
DR GeneID; 2910658; -.
DR KEGG; yli:YALI0D04873g; -.
DR VEuPathDB; FungiDB:YALI0_D04873g; -.
DR HOGENOM; CLU_002360_9_3_1; -.
DR InParanoid; Q6CA91; -.
DR OMA; ARGFWVF; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 431..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 858..879
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 928..952
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1008..1034
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1228..1245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 122..194
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1254 AA; 136906 MW; DA76EFC1A793E11C CRC64;
MPDTTQDPPT HTDSTPQGTP GAIMNPQAPP VISIDTSIVD ADEKHPPVLI EPTNSYSPTI
KEETATPSTC NDSDFSTHAE EAQQHLNEDA DGTLAGGYKW APKQLSHLID PKSVFVLAEM
GGLEGLATDL NTNLQSGLSE EDAGARDARI EAYDRNILPE KKAKSLFYLM WMALQDKVLI
LLTVAAIISL ALGLYETFGQ PAEHDAQGRK LPKVDWVEGV AIMVAIIIVV VVGAGNDWQK
ELRFVKLNKK KEDRMIRVIR SGKTQEVPIA DLLVGDLVLL EPGDMIPADG ILVSGHNIKC
DESSATGETD TMKKMSGFDA MTAYESRVDG LTRGKVDPFI LSGSKVLEGI GTYVVTAVGP
NSLFGKTLLS LNIEDEATPL QAKLNDIAEG IAKAGGLAAL ILFIVLFIRF CARLPGNKDT
PAEKGNEFMD ILITAITIIV VAVPEGLPLA VTLALAFATT RMLKDNNLVR ELRACETMGN
ATTVCSDKTG TLTENRMTVT RGTIGVEEFA VEEITQFFET LPAEAREILF ESIVFNTTAF
ETDQIADTDA ERFVGSKTET ALLNFAHLYM GLQNLANQRD AREIVQIVPF DSSRKCMAVI
LKMKGFYRMY IKGASEVLSA QSSMIYNNNV VSPITKEQRQ DIDQKILHYG EQSLRGIALA
YRDFECSSWP PKGMASSDDS SQAEFEPMFS DLTLFGLIGI MDPLREGVTK AVADCQSAGV
IVRMVTGDNV NTAKAIAREC GIYSEGGLVM EGPVFRRLAD HEMKEMLPQL QVLARSSPED
KRILVKALKE MGETVAVTGD GTNDGPALKL ADVGFSMGIA GTEVAKEASS IILMDDNFSS
IVKAIMWGRT VNDAVKKFLQ FQLTVNVTAV VLTFVSAVVN KHGKSVLTAV QLLWVNLIMD
TLAALALATD PPSPDVLERK PDRKSQNLIT VTMWKMIFGQ AIFQLGVTFV LFFAGKYFWT
VDTPRQQDEL DATVFNTFVW MQFFNLFVNR RLDNKMNMFS GIHRNIFFIL IVVIIGGFQV
LIMFVGGAAF SIVHLNGGQW ATSLICGVIS LPAGMLLRLI PDAWISAMYP QFLHNWISKL
WRIMRPKNKE IVEIHVPRDD GFQGSDYKWH SGIEEARVQL EFMRALRGGR MYQVPNLVPV
KIRQMFQRSR ANSVASLSKK EPSVSTTTAS PTQTVFDESG RDRWTENDGH LAVPGAHYGG
SGNGNNGNTS PTSPGGSSSR SSSRGSSIGA LVMVPAIVGG AVAGWNPELK PPSN
//