GenomeNet

Database: UniProt
Entry: A0A4W4E5W3_ELEEL
LinkDB: A0A4W4E5W3_ELEEL
Original site: A0A4W4E5W3_ELEEL 
ID   A0A4W4E5W3_ELEEL        Unreviewed;       932 AA.
AC   A0A4W4E5W3;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 {ECO:0000256|ARBA:ARBA00040288};
DE            EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE   AltName: Full=Calcium pump 2 {ECO:0000256|ARBA:ARBA00042814};
DE   AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform {ECO:0000256|ARBA:ARBA00042557};
DE   AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase {ECO:0000256|ARBA:ARBA00041515};
OS   Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC   Gymnotoidei; Gymnotidae; Electrophorus.
OX   NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000007308.1, ECO:0000313|Proteomes:UP000314983};
RN   [1] {ECO:0000313|Proteomes:UP000314983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24970089;
RA   Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H.,
RA   Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R.,
RA   Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.;
RT   "Nonhuman genetics. Genomic basis for the convergent evolution of electric
RT   organs.";
RL   Science 344:1522-1525(2014).
RN   [2] {ECO:0000313|Proteomes:UP000314983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28695212;
RA   Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.;
RT   "A tail of two voltages: Proteomic comparison of the three electric organs
RT   of the electric eel.";
RL   Sci. Adv. 3:e1700523-e1700523(2017).
RN   [3] {ECO:0000313|Ensembl:ENSEEEP00000007308.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   STRING; 8005.ENSEEEP00000007308; -.
DR   Ensembl; ENSEEET00000007408.1; ENSEEEP00000007308.1; ENSEEEG00000003792.1.
DR   GeneTree; ENSGT00940000159986; -.
DR   OMA; WSENEPR; -.
DR   Proteomes; UP000314983; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0061371; P:determination of heart left/right asymmetry; IEA:Ensembl.
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; 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; 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; IPR001757; P_typ_ATPase.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF18; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 2; 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   PRINTS; PR00119; CATATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 2.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Calcium {ECO:0000256|ARBA:ARBA00022568};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314983};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT   TRANSMEM        60..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        642..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        676..698
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        704..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        794..812
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..77
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          890..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  102771 MW;  C167F898ED2DC923 CRC64;
     MENAHTKTVE EVYSHFSVNE STGLGLDQVK RQRERWGPNE LPAEEGKSLW ELVVEQFEDL
     LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA NAIVGVWQER NAENAIEALK
     EYEPEMGKVY RQDRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRLTSIKS TTLRVDQSIL
     TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAV GVVVATGVNT EIGKIRDEMA
     STEQERTPLQ QKFRIQRQCT TACPRHCSVL VLSVPPAGGF MNCVCVCVCV CVCVCVCQMF
     IVDQVEGDSC FLRQFTVTGS TYAPEGEVYQ DGKPVKCYKY DALVEMATIC ALCNDSSLDY
     NEVKGVYEKV GEATETALAC LVEKMNVFDT DLKGLSKIER ANACNSVIKQ LMKKEFTLEF
     SRDRKSMSVY CTPNKARSAM GKMFVKGAPE GVIDRCTHVR VGSNKVPLTA GIKEKLLSVI
     REYGTGRDTL RCLALATRDN PISREHLVLD DSSRFVEYET DLTFVGCVGM LDPPRAEVAA
     SIKLCCLAGI RVIMITGDNK GTAVAICRRI GIFGEDEDVS HMAFTGREFD DLSSDAQREA
     VLTARCFARV EPSHKSKIVE YLQSYDEITA MVTLQPLPPC SLGGGVCVCV CVCVCVCVCV
     CVCVCACVCG SXXXXVCVCV CVCVCVCVCV CVCAKMMGLT LSPPGYVGAA TVGAAAWWFV
     AAEDGPRVTF YQLSHFLQCG PENPEFMDIK CEVFESPYPM TMALSVLVTI EMCNALNSVS
     ENQSLLRMPP WENVWLLGAI CMFLPLMFII FVPQMIFQIT PLNVTQWLMV LKISLPVILL
     DEVLKFAARN YLEPGKELDK AADRACSLFA WTEGISWPFI YRHAHGWERP DEPPXSGSTL
     STDMPMDGRD QTRPLLHLGS RSNPVFSSLP HI
//
DBGET integrated database retrieval system