UniProt: A0A2K5P0V5

Database: UniProt
Entry: A0A2K5P0V5_CERAT

LinkDB:  A0A2K5P0V5_CERAT 
Original site:  A0A2K5P0V5_CERAT

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Ontology (34)   
   GO (34)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (5)   
   RefSeq(pep) (5)   
Protein domain (20)   
   InterPro (12)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
All databases (65)   

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ID   A0A2K5P0V5_CERAT        Unreviewed;      1205 AA.
AC   A0A2K5P0V5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=ATP2B4 {ECO:0000313|Ensembl:ENSCATP00000043266.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000043266.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000043266.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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. 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   RefSeq; XP_011893629.1; XM_012038239.1.
DR   RefSeq; XP_011893631.1; XM_012038241.1.
DR   RefSeq; XP_011893632.1; XM_012038242.1.
DR   RefSeq; XP_011893634.1; XM_012038244.1.
DR   RefSeq; XP_011893635.1; XM_012038245.1.
DR   AlphaFoldDB; A0A2K5P0V5; -.
DR   STRING; 9531.ENSCATP00000043266; -.
DR   Ensembl; ENSCATT00000067703.1; ENSCATP00000043266.1; ENSCATG00000044125.1.
DR   GeneID; 105575889; -.
DR   KEGG; caty:105575889; -.
DR   CTD; 493; -.
DR   GeneTree; ENSGT00940000154527; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000044125; Expressed in heart and 12 other cell types or tissues.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR   GO; GO:0036487; F:nitric-oxide synthase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
DR   GO; GO:1901660; P:calcium ion export; IEA:Ensembl.
DR   GO; GO:1905145; P:cellular response to acetylcholine; IEA:Ensembl.
DR   GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
DR   GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0071878; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:1900082; P:negative regulation of arginine catabolic process; IEA:Ensembl.
DR   GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR   GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR   GO; GO:1902548; P:negative regulation of cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
DR   GO; GO:1903249; P:negative regulation of citrulline biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0098736; P:negative regulation of the force of heart contraction; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
DR   GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl.
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; 3.
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   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|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:UP000233060};
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        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        147..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        368..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        409..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        916..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        957..974
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        995..1016
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1028..1049
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          45..121
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          294..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1205 AA;  133743 MW;  3B4DA74ED0050773 CRC64;
     MTNPSDRVLP ANSMAESREG DFGCTVMELR KLMELRSRDA LTQINVHYGG VQNLCSRLKT
     SPVEGLSGNP ADLEKRRQVF GHNVIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS
     FYRPAGEENE LCGQVASTPE DESEAQAGWI EGAAILFSVI IVVLVTAFND WSKEKQFRGL
     QNRIEQEQKF SIIRNGQLIQ LPVAEIVVGD IAQVKYGDLL PADGILIQGN DLKIDESSLT
     GESDHVKKSL DKDPMLLSGT HVMEGSGRMV VTAVGVNSQT GIILTLLGVN EDDEGEKKKK
     GKKQGVPENR NKAKTQDGVA LEIQPLNSQE GIDNEEKDKK AVKVPKKEKS VLQGKLTRLA
     VQIGKAGLLM SALTVFILIL YFVIDNFVIN RRPWLPECTP IYIQYFVKFF IIGVTVLVVA
     VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMTVVQA
     YVGGIHYRQI PSPDVFLPKV LDLIVNGISI NSAYTSKILP PEKEGGLPRQ VGNKTECALL
     GFVTDLKQDY QAVRNEVPEE KLYKVYTFNS VRKSMSTVIR NPSGGFRMYS KGASEIILRK
     CNRILDRKGE AVPFRNKDRD DMIRTVIEPM ACDGLRTICI AYRDFNDAEP SWDNENEILT
     ELTCIAVVGI EDPVRPEVPD AIAKCKQAGI TVRMVTGDNI NTARAIATKC GILTPGDDFL
     CLEGKEFNRL IRNEKGEVEQ EKLDKIWPKL RVLARSSPTD KHTLVKGIID STVGEQRQVV
     AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI
     SKFLQFQLTV NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTESLL
     KRRPYGRNKP LISRTMMKNI LGHAFYQLLV IFILVFAGEK FFDIDSGRKA PLHSPPTQHY
     TIVFNTFVLM QLFNEINSRK IHGEKNVFSG IYRNIIFCSV VLGTFICQIF IVEFGGKPFS
     CTSLSLSQWL WCLFIGIGEL LWGQFISAIP TRSLKFLKEA GHGTTKEEIT KDAEGLDEID
     HAEMELRRGQ ILWFRGLNRI QTQIKVVKAF HSSLHETIQK PYSQHSIHNF MTHPEFAIDE
     ELPRTPLLDE EEEENPDKAS KFGTGVLLLD GEVTPYANTN NNAVDCNQAQ LPQSDSSLQS
     LETSV
//

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