UniProt: A0A0D8XA37

Database: UniProt
Entry: A0A0D8XA37_DICVI

LinkDB:  A0A0D8XA37_DICVI 
Original site:  A0A0D8XA37_DICVI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (10)   
   Pfam (5)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   A0A0D8XA37_DICVI        Unreviewed;      1265 AA.
AC   A0A0D8XA37;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=DICVIV_12570 {ECO:0000313|EMBL:KJH41455.1};
OS   Dictyocaulus viviparus (Bovine lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX   NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH41455.1, ECO:0000313|Proteomes:UP000053766};
RN   [1] {ECO:0000313|EMBL:KJH41455.1, ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH41455.1,
RC   ECO:0000313|Proteomes:UP000053766};
RA   Mitreva M.;
RT   "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX   PubMed=26856411; DOI=10.1038/srep20316;
RA   McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA   Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA   Sternberg P.W., Gasser R.B., Mitreva M.;
RT   "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT   lungworm biology and support future intervention.";
RL   Sci. Rep. 6:20316-20316(2016).
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}.
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DR   EMBL; KN716821; KJH41455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8XA37; -.
DR   STRING; 29172.A0A0D8XA37; -.
DR   Proteomes; UP000053766; 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: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; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
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; 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:SF253; 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; PF08282; Hydrolase_3; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053766};
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        100..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        426..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        891..911
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        964..985
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1005..1024
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1044..1064
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1076..1097
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          40..116
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          316..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1230..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          498..525
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        318..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1251..1265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1265 AA;  139441 MW;  4B54154DF65AC69C CRC64;
     MKLIRKKSEV NDYSKEYGCT LAQMRSLMEA RGAEAIVRLS TEHDGVEGLC KKLKVDPVRG
     LPNQASELER RRAAFGANTI PPAKSKGFAR LVFEACRDPT LVILVVAGFV NLALSFYEPE
     MQSPDDDVTA AVTTVAGLLS NNTFGFDLLN TTLPSNVTAK PTGEGHGTAW IEGVAILLCV
     VVVVLVTAVN DYSKERQFRD LQEKIETGQK FSVIRDGEAI DVPVSDLVVG DIARVKYGDL
     IPADGFLIQG NDLKIDESSL TGESDHIKKT PESDPVLLSG TYAMEGSGKM ILTAVGVNSQ
     TGIIMTLLGA GKPGFGSADD DSTSTSSSSS SSSSSSSSSS SSSSNSSSSS KSSDDDDGLS
     AKSVLQSKLS KLALQIIYCG TTVAVVALVV LITRFCIEHY VRDGIPFSIA DIQSIKNANI
     KMFVKFFIIA VTILVISIPE GLPLAIALAL TYSVRKMMFD NNLVRHLDAC ETMGNATSIC
     SDKTGTLTTN RMTVVDSYIN ATDIKQQYEE EAVQLEEIVT QHSNITHLRG LHYEGQQNQP
     NGATLPVEPT RSGEQLQQLG NKTECGLLGF VQKLGGDYVT IRRKFPEESL VKVYTFNSSR
     KCMMTVIRLV EDGVDVGYRV HCKGASEIIL ARCSYLIGSD GKPHTFSSDR LKEITATIIS
     KMANNGLRTI CVAYKDYIRK SAREADRTET PFENDIDWND EAEISKNLVG IAICGIQASD
     PVRQEVPEAI EKCKRAGITV RMVTGDNINT ARAIAMTCKI LEPGEDFLAL EGKEFNERIR
     DADGKVSQAK LDQIWPRLRV LARAQPADKY TLVKGIIDSK YTPQREIVAV TGDGTNDGPA
     LKKADVGFAM GIAGTDVAKE ASDIILTDDN FTSIVKAVMW GRNVYDSISK FLQFQLTVNI
     VAVITAFIGA VTVSDSPLKA VHMLWINLIM DTLASLALAT EVPTDDLLNR KPYGRKKSLI
     SRTMMKNILC HALYQLLILF TIFYYGDRLF NIKSGLYAPL FAPPSQHFTI VFNAFVMMTL
     FNEINARKVH GERNVFKGLA SNHVFCVIWL STFIGQILIT QFGGAWFSTA PLNKNQWIVC
     LALGLSTLVW GQVVATIPSK KLPKNWKVGR GEVEPSKIHI NGDYNVRVRS RALIARRTGK
     SLWMRGMFLM AQQLRIIRAF QLRDKNFGKT APTMTAEAAE RWRSSYRKYR HQKHLEKRAS
     GTLEAERPKL PDDIKVKRKT FRQIKLVARG RSAEKRVRNS CVHDRHSKKK KQQQQTIDID
     DIDHS
//

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