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Database: UniProt
Entry: A0A1S4E1L7_CUCME
LinkDB: A0A1S4E1L7_CUCME
Original site: A0A1S4E1L7_CUCME 
ID   A0A1S4E1L7_CUCME        Unreviewed;      1065 AA.
AC   A0A1S4E1L7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Calcium-transporting ATPase 4, endoplasmic reticulum-type-like {ECO:0000313|RefSeq:XP_008457516.1, ECO:0000313|RefSeq:XP_016902118.1};
GN   Name=LOC103497190 {ECO:0000313|RefSeq:XP_008457516.1,
GN   ECO:0000313|RefSeq:XP_016902118.1};
GN   Synonyms=103497190 {ECO:0000313|EnsemblPlants:MELO3C020683.2.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_016902118.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|EnsemblPlants:MELO3C020683.2.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_008457516.1, ECO:0000313|RefSeq:XP_016902118.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   RefSeq; XP_008457516.1; XM_008459294.2.
DR   RefSeq; XP_016902118.1; XM_017046629.1.
DR   EnsemblPlants; MELO3C020683.2.1; MELO3C020683.2.1; MELO3C020683.2.
DR   GeneID; 103497190; -.
DR   Gramene; MELO3C020683.2.1; MELO3C020683.2.1; MELO3C020683.2.
DR   KEGG; cmo:103497190; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   Proteomes; UP000596662; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   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; 1.
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; 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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF4; CALCIUM-TRANSPORTING ATPASE 1, ENDOPLASMIC RETICULUM-TYPE-RELATED; 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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000089565};
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}.
FT   TRANSMEM        82..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        867..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        989..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1024..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..99
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1065 AA;  116636 MW;  9F3B75FE0B6DD11B CRC64;
     MGRGGENYGK KEIFAANSSK KETYPAWARD VQECLEIYQV NPDLGLSTEE VENKRKIYGY
     NELEKHEGTS IFKLILEQFN DTLVRILLAA AVVSFVLAWY DGEEGGEMEI TAFVEPLVIF
     LILIVNAIVG IWQENNAEKA LEALKEIQSE QASVLRNGKR TSIVAKELVP GDIVELRVGD
     KVPADMRVLR LISSTFRVEQ GSLTGESEAV SKTSKTVPED TDIQGKKCMV FAGTTVVNGN
     CICIVTQTGM STELGQVHCQ IQEAAQSEDD TPLKKKLNEF GELLTAIIGV ICALVWLINV
     KYFLTWEYVD GWPANFKFSF EKCTYYFEIA VALAVAAIPE GLPAVITTCL ALGTRKMAQK
     NALVRKLPSV ETLGCTTVIC SDKTGTLTTN QMAVAKIVAL GSRVGTLRAF DVEGTTYDPL
     DGKIIGWLEG QLDANLQMLA KIAAVCNDAG VEKSGHHFVA SGMPTEAALK VLVEKMGLPE
     GYDSSSVETN GDVLRCCQAW NKNEQRIATL EFDRDRKSMG VITNSKSGKK SLLVKGAVEN
     LLDRSSFIQL LDGTIVNLDS DSKKYLLDCL REMSSSALRC LGFAYKEYLP EFSDYTVGDE
     DHPAHQLLLD PSKYSTIESN LIFAGFVGLR DPPRKEVHQA IEDCKAAGIR VMVITGDNQN
     TAEAICREIG VFGQHEAINS RSLTGKQFMT MSREDQKFHL RQDGGLLFSR AEPRHKQEIV
     RLLKEDGEVV AMTGDGVNDA PALKLADIGI AMGIAGTEVA KEASDMVLAD DNFSTIVAAV
     GEGRSIYDNM KAFIRYMISS NIGEVASIFL TAALGIPEGM IPVQLLWVNL VTDGPPATAL
     GFNPPDNDIM KKPPRKSDDS LITTWILIRY LVIGLYVGLA TVGVFIIWYT HGSFLGIDLS
     GDGHSLVSYS QLANWGQCPS WEGFSVSPFT AGDEVFNFDS DPCEYFRSGK IKASTLSLSV
     LVAIEMFNSL NALSEDGSLL TMPPWVNPWL LLAMSVSFGL HFLILYVPFL AKIFGIVPLS
     LNEWLLVLAV ALPVIIIDEI LKFIGRLTSG LRTSRPSRSS KQKSE
//
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