UniProt: A0A091L4B4

Database: UniProt
Entry: A0A091L4B4_CATAU

LinkDB:  A0A091L4B4_CATAU 
Original site:  A0A091L4B4_CATAU

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (12)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
All databases (26)   

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ID   A0A091L4B4_CATAU        Unreviewed;      1209 AA.
AC   A0A091L4B4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, 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=N323_03085 {ECO:0000313|EMBL:KFP51294.1};
OS   Cathartes aura (Turkey vulture) (Vultur aura).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX   NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP51294.1, ECO:0000313|Proteomes:UP000053745};
RN   [1] {ECO:0000313|EMBL:KFP51294.1, ECO:0000313|Proteomes:UP000053745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP51294.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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|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|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; KL301031; KFP51294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091L4B4; -.
DR   Proteomes; UP000053745; Unassembled WGS sequence.
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; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
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; 3.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093:SF435; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 4; 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; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
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   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:UP000053745};
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        105..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        150..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        367..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        410..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        846..867
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        919..940
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        998..1019
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1031..1052
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          48..122
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          296..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1209 AA;  133296 MW;  DD0509EBC97FF805 CRC64;
     MTNNVADHHP GNSVAEGNHE GDFGCSMVEL RNLMELRSAE AVARLNDSYG GVQNVCKRLK
     TSPVEGLSGN PTDLEKRRQV FGQNFIPPKK AKTFLQLVWE ALQDVTLIIL EIAAIISLGL
     SFYHPPGGDN ELCGQSTGGV EDEGESQAGW IEGAAILFSV IIVVLVTAFN DWSKEKQFRG
     LQSRIEQEQK FTVIRKGQVI QIPVAEIVVG DIAQIKYGDL LPADGILIQG NDLKIDESSL
     TGESDQVKKS LDKDPMLLSG THVMEGSGRM VVTAVGINSQ TGIIFTLLGA GEGDEEKKVK
     KGKKTGAPEN RNKAKTQDGV ALEIQPLKSQ EGVENEEKEK KKVKVPKKEK SVLQGKLTRL
     AVQIGKAGLI MSAITVIILV LYFVIDTFGV QGRPWLAECT PIYIQYFVKF FIIGVTVLVV
     AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT LTMNRMTVVQ
     AYVGDTHYRQ IPDPEAILPK ILDLIVNGVA INSAYTSKIL PPEKEGGLPR QVGNKTECAL
     LGFVLDLKQD YQAVRNEVPE EKLYKVYTFN SVRKSMSTVL KNGNGGFRMY SKGASEIILR
     KCTRILDKNG DPRVFKVKDR DEMVKKVIEP MACHGLRTIC LAFRDFPADA EPDWDSENEI
     LSDLTCIAVV GIEDPVRPEV PDAILKCQRA GITVRMVTGD NINTARAIAT KCGILLPGED
     FLCLEGKEFN RLIRNEKGEV EQEQLDKIWP KLRVLARSSP TDKHTLVKGI IDSTVGDQRQ
     VVAVTGDGTN DGPALKKADV GFAMVRTGGT DVAKEASDII LTDDNFTSIV KAVMWGRNVY
     DSISKFLQFQ LTVNIVAVIV AFTGACITQD SPLKAVQMLW VNLIMDTFAS LALATEPPSE
     SLLLRKPYGR NKPLISRTMM KNILGHAVYQ LTIIFTLLFA GEKFFDIDSG RNAPLHSPPT
     EHYTIVFNTF VMMQLFNEIN ARKIHGERNV FESIYRNPIF CTVVLGTFAA QIIIVEFGGK
     PFSCSGLTLS QWFWCIFIGV GELLWGQLIC TVPTSHLKFL KEAGHGITKE EIPEEELPED
     VDEIDHAEME LRRGQILWFR GLNRIQTQIK VVNAFRSSLY EGLEKPESRS SIHNFMTHPE
     FILEEDEPRT PFLDGAEDDP ETDGLTKRGG GSLGGSTSLN RNNNAVDSDQ AEVTVPEPES
     PLHSLETSV
//

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