ID G3RHJ3_GORGO Unreviewed; 946 AA.
AC G3RHJ3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=ATP2C2 {ECO:0000313|Ensembl:ENSGGOP00000015114.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000015114.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000015114.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000015114.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000015114.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00024147};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000256|ARBA:ARBA00024147};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
CC Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024272};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC Evidence={ECO:0000256|ARBA:ARBA00024272};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675,
CC ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR EMBL; CABD030102472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030102481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004058123.2; XM_004058075.2.
DR AlphaFoldDB; G3RHJ3; -.
DR Ensembl; ENSGGOT00000015546.3; ENSGGOP00000015114.3; ENSGGOG00000015486.3.
DR GeneID; 101140883; -.
DR KEGG; ggo:101140883; -.
DR CTD; 9914; -.
DR GeneTree; ENSGT00940000160275; -.
DR HOGENOM; CLU_002360_3_1_1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000001519; Chromosome 16.
DR Bgee; ENSGGOG00000015486; Expressed in adult mammalian kidney and 3 other cell types or tissues.
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; IEA:UniProtKB-EC.
DR GO; GO:0140613; F:P-type manganese transporter activity; IEA:RHEA.
DR CDD; cd02085; P-type_ATPase_SPCA; 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; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF23; CALCIUM-TRANSPORTING ATPASE TYPE 2C MEMBER 2; 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 PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW 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:UP000001519};
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 298..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 323..352
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 805..825
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 837..855
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 875..892
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 904..922
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 48..130
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 946 AA; 103225 MW; BBA82D12BB11E230 CRC64;
MVEGRVSEFL KKLGFSGGGR QYQALEKDEE EALIDEQSEL KAIEKEKKVT ALPPKEACKC
QKEDLAKAFC VDLHTGLSEF SVTQRRLAHG WNEFVADNSE PVWKKYLDQF KNPLILLLLG
SALVSVLTKE YEDAVSITTA VLIVVTVAFI QEYRSEKSLE ELTKLVPPEC NCLREGKLQH
LLARELVPGD VVSLSIGDRI PADIRLTEVT DLLVDESSFT GEAEPCSKTD SPLTGGGDLT
TLSNIVFMGT LVQYGRGQGV VIGTGESSQF GEVFKMMQAE ETPKTPLQKS MDRLGKQLTL
FSFGIIGLIM LIGWLQGKQL LSMFTIGVSL AVAAIPEGLP IVVMVTLVLG VLRMAKKRLI
VKKLPIVETL GCCSVLCSDK TGTLTANEMT VTQLVTSDGL RAEVSGVGYD GQGTVCLLPS
KEVIKEFSNV SVGKLVEAGC VANNAVIRKN AVMGQPTEGA LMALAMKMDL SDIKNSYIRK
KEIPFSSEQK WMAVKCSLKT EDQEDIYFMK GALEEVIRYC TMYNNGGIPL PLTPQQRSFC
LQEEKRMGSL GLRVLALASG PELGQLTFLG LVGIIDPPRV GVKEAVQVLS ESGVSVKMIT
GDALETALAI GRNIGLCNGK LQAMSGEEVD SVEKGELADR VGKVSVFFRT SPKHKLKIIK
ALQESGAIVA MTGDGVNDAV ALKSADIGIA MGQTGTDVSK EAANMILVDD DFSAIMNAVE
EGKGIFYNIK NFVRFQLSTS ISALSLITLS TVFNLPSPLN AMQILWINII MDGPPAQSLG
VEPVDKDAFR QPPRSVRDTI LSRALILKIL MSAAIIISGT LFIFWKEMPE DRASTPRTTT
MTFTCFVFFD LFNALTCRSQ TKLIFEIGFL RNHMFLYSVL GSILGQLAVI YIPPLQRVFQ
TENLGVLDLL FLTGLASSVF ILSELLKLCE KYCCSPKRVQ MHPQDV
//
