ID A0A1S3JPF3_LINUN Unreviewed; 1503 AA.
AC A0A1S3JPF3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=LOC106174750 {ECO:0000313|RefSeq:XP_013411879.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013411879.1};
RN [1] {ECO:0000313|RefSeq:XP_013411879.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26383154;
RA Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT "The Lingula genome provides insights into brachiopod evolution and the
RT origin of phosphate biomineralization.";
RL Nat. Commun. 6:8301-8301(2015).
RN [2] {ECO:0000313|RefSeq:XP_013411879.1}
RP IDENTIFICATION.
RG RefSeq;
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|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. {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 RefSeq; XP_013411879.1; XM_013556425.2.
DR STRING; 7574.A0A1S3JPF3; -.
DR EnsemblMetazoa; XM_013556425.2; XP_013411879.1; LOC106174750.
DR GeneID; 106174750; -.
DR KEGG; lak:106174750; -.
DR InParanoid; A0A1S3JPF3; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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 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; 2.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 4.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR022141; ATP_Ca_trans_C.
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; 4.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 2.
DR Pfam; PF00122; E1-E2_ATPase; 3.
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; 2.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 2.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 2.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000085678};
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 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 164..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 639..662
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 682..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1129..1149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1202..1223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1243..1260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1281..1302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1314..1335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 73..149
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT DOMAIN 291..382
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1503 AA; 163964 MW; 76B6F04B0A04695D CRC64;
MSGVKGKGTP GAASDQNGEN KVGPTECTGQ PDQAVNMDEV DARLGHPANY GCSAKELSQL
MAVRGHEAVN AIKERYGSVA ELCKRLYTNP NEGLNGSPVD LDHRRQVFGT NVIPPKPPKT
FLQLAWEALQ DITLIILLVA ALISLGLSFY HGPEDEGEGS ESEANWIEAV AILVAVILVV
LVTAFNDWRK EKQFRGLQNK IEGEHKFAVI RNGEAANIPV GELVVGDICQ VKYGDLLPAD
GIIIQSNDLK VDESSLTGES DHVKKGEERD PMLLSGTHVM EGSGKMLVTA VGIASQAGII
FSLLGATHEG DSKDKKKNKN KDGDQGLNGS PVDLDHRRQV FGTNVIPPKP PKTFLQLAWE
ALQDITLIIL LVAALISLGL SFYHGPEDEG EGSESEANWI EAVAILVAVI LVVLVTAFND
WRKEKQFRGL QNKIEGEHKF AVIRNGEAAN IPVGELVVGD ICQVKYGDLL PADGIIIQSN
DLKVDESSLT GESDHVKKGE ERDPMLLSGT HVMEGSGKML VTAVGIASQA GIIFSLLGAT
HEGDSKDKKK NKNKDGDQGA PHNVPLLSGD DQKSDVEANA STGNSHFKAG TANADGDRDV
EAPPPGEEGE QGEQQKKEGG GQGFGRKEKS VLQAKLNKLA IQIGYAGTII AVLVVIVLIV
RFCVETYAGE NARAWNTKDL QFFVKYFILG VTVLVVAVPE GLPLAVTLAL AYSVRKMMHD
NNLVRHLDAC ETMGNATAIC SDKTGTLTTN RMTVVQSYIG EQHYKSTPEF KSLPAQTGQL
LIRCVSINSG YSTRVIKSPT EDLPKQLGNK TECALLGFVM DLGQSYQAIR EEVPEERFHR
VYTFNSMRKS MSTVIPTEHG FRLFNKGASE MVLRRCTFIL GAGGRVRPFS AHDADNLIKR
VIEPMAMDGL RTIGIAYKDF VKHNPATNEV HFDSEPNWDD EDSIVSGLTL IAITGIEDPV
RPEVPEAIRK CQRAGITVRM VTGDNINTAR SIATKCGIIH PGDDFLVLEG GDFNKQVKND
HDEVVQENLD KIWPRLRVLA RSSPTDKYVL VKGIIDSKLS ANREVVAVTG DGTNDGPALK
KADVGFAMGI AGTDVAKEAS DIILTDDNFT SIVKAVMWGR NVYDSIAKFL QFQLTVNVVA
VIVAFIGSLT VRDSPLKAIQ MLWVNLIMDT LASLALATEM PTEELLQRKP YGRTKALISR
TMMKNIIGHS IYQLTVLFVI LYAGDVLFDI DSGINVDINA PPTQHFTIIF NAFVMMTLFN
EINSRKIHGQ RNVFEGLQRN VLFIGIWITT MFFQVILVEL LGFAFSTTNL EPEHWMWCLF
LGIGSLLWGQ LITTLPTAKL PKRLSLGKMK EAEIVAMESE DVVERPVGAP AATSGHILWV
RGLTRLQTQL RVVRAFRSTL EDLEEKRSVH SFHSLRSFHS SRSHQGPRGL SDEAYSPSDK
STDKNGTFLT ADAAYENIMG ALSRSTENVP LMDKSTSDQT KPAASAKSSS TSDLNSKSHE
TTI
//
