ATC1_YARLI
ID ATC1_YARLI Reviewed; 928 AA.
AC O43108;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Calcium-transporting ATPase 1;
DE EC=7.2.2.10;
DE AltName: Full=P-type calcium ATPase;
GN Name=PMR1; Synonyms=SCA1; OrderedLocusNames=YALI0E09471g;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9461422; DOI=10.1016/s0378-1119(97)00573-8;
RA Park C.S., Kim J.-Y., Crispino C., Chang C.C., Ryu D.D.Y.;
RT "Molecular cloning of YlPMR1, a S. cerevisiae PMR1 homologue encoding a
RT novel P-type secretory pathway Ca2+ ATPase, in the yeast Yarrowia
RT lipolytica.";
RL Gene 206:107-116(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium. Has a role in the secretory
CC pathway.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; U75447; AAC03419.1; -; Genomic_DNA.
DR EMBL; CR382131; CAG79326.1; -; Genomic_DNA.
DR RefSeq; XP_503736.1; XM_503736.1.
DR AlphaFoldDB; O43108; -.
DR SMR; O43108; -.
DR STRING; 4952.CAG79326; -.
DR EnsemblFungi; CAG79326; CAG79326; YALI0_E09471g.
DR GeneID; 2911589; -.
DR KEGG; yli:YALI0E09471g; -.
DR VEuPathDB; FungiDB:YALI0_E09471g; -.
DR HOGENOM; CLU_002360_3_1_1; -.
DR InParanoid; O43108; -.
DR OMA; GVHRMAK; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0140613; F:P-type manganese transporter activity; IEA:EnsemblFungi.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0061454; P:release of sequestered calcium ion into cytosol by Golgi; IEA:EnsemblFungi.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01522; ATPase-IIA2_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Calcium transport; Golgi apparatus; Ion transport;
KW Magnesium; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..928
FT /note="Calcium-transporting ATPase 1"
FT /id="PRO_0000046230"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 887..907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 928 AA; 100051 MW; CBA53B0DD075EBE7 CRC64;
MDSHTSTEGV PLSETNNRSH ATPSAQYCQM TVEETCSKLQ TNPETGLTSS QEAMHRRDIH
GSNEFAQEEE DSLIKKFFEQ FSENPLLLLL IGAAAVSFFM GNHDDAISIT LAILIVTTVG
FVQEYRSEKS LEALNKLVPP EAHLIRAGNS QTVLASTLVP GDLVEFSVGD RIPADCRIVK
AVHLSIDESN LTGETTPVTK DTNPVTGTPP IGLADRTNTA YMGTLVRDGN GTGIVVGTGS
HTAFGAVYDM VSEISTPKTP LQASMDNLGK DLSLVSFGVI GVICLIGMFQ GRDWLEMFTI
GVSLAVAAIP EGLPIIVTVT LALGVLRMSR QKAIVRKLPS VETLGSVNVI CSDKTGTLTR
NHMSCTTCWT VDMGDLANAV TLKPGQSHTE ADPKAVAALK NSVSLANMLK VGNLCNNSKF
NREAGHLVGN ATDIALIEVL DYFGLEDTRE TRKRVAEVPF SSSRKWMLTS TTTGDSSTPM
ISVKGAGEVI APFCEYYCKK DGKTAPFNDD MRKKVTEIAS EMSNDGLRII AFAYKQGKYE
EGSEEAPEGL VFAGLMGLYD PPRPDVPRAI RRLTTGGVRV VMITGDSAAT ALSIGRRIGM
PLMPGTQSVV EGSKLATMSD QALDECLQTA SIFARTSPED KMKIVKGFQR RGDVVAMTGD
GVNDAPALKL ADIGIAMGQG GTDVAKEAAD MILTDDDFAT ILSAIEEGKG IFNNIRNFIT
FQLSTSMAAL SIVAVATIMG LENPLNPMQI LWINILMDGP PAQSLGVEPV DPDVMNKPPR
PRNEKVMTPD LVKKCVEAAV IILVGTMLVY VTQMQDGVID KRDTTMTFTC FVFYDMFNAL
ACRSATKSVF EIGFFSNKMF LYACGASIIG QLAVVYVPFL QSVFQTEALS VKDLLSLVLI
SSSVWILDEA KKYFLKSRST NNYTNSVV
