UniProt: A0A668ANH1

Database: UniProt
Entry: A0A668ANH1_9TELE

LinkDB:  A0A668ANH1_9TELE 
Original site:  A0A668ANH1_9TELE

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (20)   
   InterPro (12)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
All databases (28)   

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ID   A0A668ANH1_9TELE        Unreviewed;      1182 AA.
AC   A0A668ANH1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005046476.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005046476.1}
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   AlphaFoldDB; A0A668ANH1; -.
DR   Ensembl; ENSMMDT00005047397.1; ENSMMDP00005046476.1; ENSMMDG00005021120.1.
DR   GeneTree; ENSGT00940000165254; -.
DR   Proteomes; UP000472263; 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; 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:SF284; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 3; 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; 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:UP000472263};
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        375..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        416..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        932..952
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        967..984
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1004..1024
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          53..129
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1182 AA;  130205 MW;  5DF62E0AC5361132 CRC64;
     MGDIANSSVD FHPKKRGSAG GMEVNHAGDF GVTLDELKAL MELRGPEALQ KIQETYQDTE
     SLCRRLKTSP ANGLSDNVAD LEKRTQVFGK NFIPPKKPKT FLQLVWEALQ DVTLIILEIA
     AIISLGLSFY QPPEGESEGK SASQQDEGEA EASWIEGAAI LLSVICVVLV TAFNDWSKEK
     QFRGLQSRIE QEQRFAVVRN GTVLQIPVAD MVVGDVAQVK YGDLLPADGI LMQGNDLKID
     ESSLTGESDH VRKSVEKDPI LLSGTHVMEG SGKMLVTAVG VNSQTGIIFT LLGAGEPEEE
     RKDKKGKPDG TLETNQNKAK KQDEAVAMEM QPLKSAEGGE VEEKEKKKAN IPKKEKSVLQ
     GKLTKLAVQI GKAGLVMSTI TVVIMVVFFV IETFVMQGQS WTTECTPVYM QYFVKFFIIG
     VTVLVVAVPE GLPLAVTISL AYSVKKMMKD NNLVRHLDAC ETMGNATAIC SDKTGTLTTN
     RMTAVQMYAC DHHFHEVPQP DQLNPKVLEM LVNSISINSA YTSKIMPPDK EGGLPKQVGN
     KTECALLGLV LDLKRDYAPI REQIPEEKLY KVYTFNSVRK SMSTVVQLPD GSFRLYSKGA
     SEIVLKKCST IMTTGGELRV FRPRDKDEMV KKVIEPMACN GLRTICVAYR DLPGNPEPDW
     DNEIDILTNL ACIAVVGIED PVRPEVPDAI KKCQRAGITV RMVTGDNINT ARAIAAKCGI
     IHPGEDFLCL EGKDFNHRIR NEKGEIEQER IDKIWPKLRV LARSSPSDKH TLVKGIIDST
     IFEQRQVVAV TGDGTNDGPA LKKADVGFAM GIAGTDVAKE ASDIILTDDN FSSIVKAVMW
     GRNVYDSISK FLQFQLTVNV VAVVVAFTGA CITKDSPLKA VQMLWVNLIM DTFASLALAT
     EPPTESLLLR KPYGRNNPLI SRTMMKNILG HAVYQLVIIF TLLFVGDILF NIDNGHDAPL
     HAPPSEHYTI IFNTFVLMQL FNEINARKIH GERNVFDSIF SNPIFCSIVL GTFAVQIVIV
     QFGGKPFSCA PLSIDQWLWC LFIGLGELLW GQVITSIPTS HLKCLKEAGH GPAEDEIMDE
     DLAEDEEEID YAERELRRGQ ILWFRGLNRI QTQMEVVSTF KRSGSFQGAV RRRSSVLSQL
     HDVTNISTPT HVVLSTANAT GALGSEFLPP LATHNKRALP PC
//

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