UniProt: A0A4U5UR32

Database: UniProt
Entry: A0A4U5UR32_COLLU

LinkDB:  A0A4U5UR32_COLLU 
Original site:  A0A4U5UR32_COLLU

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
All databases (24)   

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ID   A0A4U5UR32_COLLU        Unreviewed;      1229 AA.
AC   A0A4U5UR32;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=D9C73_011041 {ECO:0000313|EMBL:TKS76951.1};
OS   Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Collichthys.
OX   NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS76951.1, ECO:0000313|Proteomes:UP000298787};
RN   [1] {ECO:0000313|EMBL:TKS76951.1, ECO:0000313|Proteomes:UP000298787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS76951.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TKS76951.1};
RA   Cai M., Xiao S.;
RT   "Genome Assembly of Collichthys lucidus.";
RL   Submitted (JAN-2019) 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; CM014087; TKS76951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U5UR32; -.
DR   STRING; 240159.A0A4U5UR32; -.
DR   Proteomes; UP000298787; Chromosome 10.
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   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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
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; PF08282; Hydrolase_3; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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   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   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:UP000298787};
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        115..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        167..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        391..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        433..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        946..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          64..140
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          17..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1018..1045
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        350..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1148..1191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1192..1208
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1229 AA;  135334 MW;  243655B7ECF7B346 CRC64;
     MSTTATMGEM ANSAVEFYPK GTRGTGGGGG RPDGSHAGGD FGVTVMELRE LMELRGTDAL
     QKIQDSYGDT EGLCQRLQSS TTEGLSGDPA DLERRGQTFG QNFIPPKKPK TFMELVWEAL
     QDVTLIILEA AAIISLGLSF YQPPGKDTES CGNVSAGEEE EEGDTGWIEG AAILLSVVCV
     VLVTAFNDWS KEKQFRGLQS RIEQEQKFTV VRKGNVIQIP VADMVVGDMA QVKYGDLLPA
     DGILVQANDL KIDESSLTGE SDHVRKSVDK DPMLLSGTHV MEGSGRMLVT AVGVNSQTGI
     IFTLLGAGEM EEDGKEKKGK QPDGAVENNQ NKAKKQDGGV AMEMQPLKSA EGGEVEDREK
     KKTNIPKKEK SVLQGKLTKL AVQIGKAGKN CLVMSAITVI ILVLFFVINT FVVEGHTWLT
     ECTPVYIQYF VKFFIIGVTV LVVAVPEGLP LAVTISLAYS VKKMMKDNNL VRHLDACETM
     GNATAICSDK TGTLTTNRMT VVQSFLGDVH HRVVPDPGLV NPRTMDLLVN AIAINSAYTS
     KILPPDVEGG LAKQVGNKTE CGLLGFVLDL QQDYAPVREQ IPEERLYKVY TFNSVRKSMS
     TVIKLPDGSF RLYSKGASEI MLKKCSYILD PNGESRGFRP RDRDEMVKQV PDAIRKCQRA
     GITVRMVTGD NINTARAIAA KCGIIHPGDD FICLEGKDFN RRIRNEKGEI EQERIDKIWP
     KLRVLARSSP TDKHTLVKGI IDSTVIEQRQ VVAVTGDGTN DGPALKKADV GFAMGIAGTD
     VAKEASDIIL TDDNFSSIVK AVMWGRNVYD SISKFLQFQL TVNVVAVIVA FTGACITQDS
     PLKAVQMLWV NLIMDTFASL ALATEPPTEA LLLRKPYGRN NPLISLTMMK NILGHGVGRN
     APLHSPPSEH YTIIFNTFVL MQLFNEINAR KIHGERNVFD GIFSNPIFCS IVLGTFAVQI
     VIVQWGGKPF SCAPLNVEQW LWCLFVGVGE LLWGQVIATV PTERLPCLKE AGLGLEPGEE
     EGEELAEDEE EIDCAERELR RGQILWFRGL NRIQTQMRVV KAFRSSLYEG REKPESRNSI
     HNFMAHPEFL INDLIHNIPL IDDTDVDDES ELSRYQHLHP ALRKPPPPPA QPQPPARTRP
     TRPYRQYSLP VTPCNRNNNN NSSSSSSSSS ISSTVTHCNK YSTNAVTPSN RSPHHHQHHH
     HHYNHHGRDR PVKPSAPHLA HLYCVETSL
//

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