ID A0A0D2TMP7_GOSRA Unreviewed; 1018 AA.
AC A0A0D2TMP7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=B456_007G277500 {ECO:0000313|EMBL:KJB44880.1}, Gorai_019663
GN {ECO:0000313|EMBL:MBA0590974.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB44880.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB44880.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
RN [2] {ECO:0000313|EMBL:MBA0590974.1, ECO:0000313|Proteomes:UP000593578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:MBA0590974.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0590974.1};
RX PubMed=30476109;
RA Grover C.E., Arick M.A. 2nd, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Frelichowski J.E., Scheffler J.A., Scheffler B.E.,
RA Wendel J.F.;
RT "Insights into the Evolution of the New World Diploid Cottons (Gossypium,
RT Subgenus Houzingenia) Based on Genome Sequencing.";
RL Genome Biol. Evol. 11:53-71(2019).
RN [3] {ECO:0000313|EMBL:MBA0590974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8 {ECO:0000313|EMBL:MBA0590974.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0590974.1};
RA Grover C.E., Arick M.A. II, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Scheffler J.A., Scheffler B.E., Wendel J.F.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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:ARBA00000363,
CC ECO:0000256|RuleBase:RU361146};
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 IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
CC 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; CM001746; KJB44880.1; -; Genomic_DNA.
DR EMBL; JABEZZ010000007; MBA0590974.1; -; Genomic_DNA.
DR RefSeq; XP_012492797.1; XM_012637343.1.
DR AlphaFoldDB; A0A0D2TMP7; -.
DR STRING; 29730.A0A0D2TMP7; -.
DR EnsemblPlants; KJB44880; KJB44880; B456_007G277500.
DR GeneID; 105804648; -.
DR Gramene; KJB44880; KJB44880; B456_007G277500.
DR KEGG; gra:105804648; -.
DR eggNOG; KOG0204; Eukaryota.
DR OMA; GIRMHEN; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000032304; Chromosome 7.
DR Proteomes; UP000593578; Unassembled WGS sequence.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; 3.
DR PANTHER; PTHR24093:SF509; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING 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; 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:UP000032304};
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 144..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 184..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 386..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 809..829
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 841..860
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 983..1001
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 96..172
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 112231 MW; A98112F64A7A23C9 CRC64;
MSLRLRKPSE PTMHRQVEPS KSSVRRWRVA VTAISVTRFL VGLTKKVAEK NAELLRSLSF
VTIDVEGSGD ERVPILDVDP QGLAKMVKDK SFQSLNDQYG GVKQVATLLQ TDFKTGIPGD
DNDLALRTKV FGANKYQKQP AKSFFSFVLE AFKDTIIIIL LVCAVLSLAF GIKQHGLKEG
WYDGGSIIVA VVLVVVVSAV SNYRQSKQFE ELSHETNDIR VQVVRNRRYQ PVSIFELVVG
DIVSLKTGDQ IPADGLFVEG HSLKVDESSM TGESDHVEVN EKKNPFLLSG TKVTDGHGYM
LVTAVGMNTA WGEMMSSIRR DLNEETPLQV RLSKLTSYIG NIGLSVAVLV LLVLLIRYFT
GHTKAENGRS AFNGSRTKFD DVMNSVVSII AAAVTIVVVA IPEGLPLAVT LTLAYSMKRM
MRDHAMVRKL SACETMGSAT IICTDKTGTL TLNEMKVTEF WLGKEPIDNS MSSEIAPNVL
QLLSEGVGLN TTGTVYKPEP TSVPEIYGSP TEKAILSWAL NDMGLNIDES KQSCEIIHVE
AFNSEKKRSG VLIRRSNNKR VLATHWKGAA EMLLAMCSCY CDKKGVLKFM NEDERAHIGM
VIESMAAKSL RCIAFATSDV TVTDGNEENH TKLEETGLTW LGLVGLKDPC RPGVKQAVES
CKKAGVSIKM ITGDNMHTAR AIAFECGILN SESSLHNEAV VEGVQFRNYS EEERRQKIET
IRVMARSSPF DKLLMVQCLK QKGHVVAVTG DGTNDAPALK EADIGLSMGI QGTEVAKESS
DIVILDDNFT SVATVLRWGR CVYNNIQKFI QFQLTVNVAA LVINFIAAVS SGDVPLTAVQ
LLWVNLIMDT LGALALATEQ PTNDLMDKRP VGRTEPLITK VMWRNLIAQA LYQVAILLIL
QFKGKSIFGV PEEVKDTLIF NTFVLCQIFN EFNARNMDKK NIFKGIHKNR LFLAIIGITL
VLQAIMVEFL QRFANTERLS WEQWGACIGI AALTWPIGWI VKCIPVDKKV QTRSSAAS
//
