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Database: UniProt
Entry: A0A2K1K3F6_PHYPA
LinkDB: A0A2K1K3F6_PHYPA
Original site: A0A2K1K3F6_PHYPA 
ID   A0A2K1K3F6_PHYPA        Unreviewed;      1051 AA.
AC   A0A2K1K3F6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=PHYPA_012784 {ECO:0000313|EMBL:PNR48308.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR48308.1};
RN   [1] {ECO:0000313|EMBL:PNR48308.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c9_16670V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [2] {ECO:0000313|EMBL:PNR48308.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c9_16670V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
RN   [3] {ECO:0000313|EnsemblPlants:Pp3c9_16670V3.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; ABEU02000009; PNR48308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1K3F6; -.
DR   STRING; 3218.A0A2K1K3F6; -.
DR   PaxDb; 3218-PP1S78_99V6-2; -.
DR   EnsemblPlants; Pp3c9_16670V3.1; Pp3c9_16670V3.1; Pp3c9_16670.
DR   EnsemblPlants; Pp3c9_16670V3.2; Pp3c9_16670V3.2; Pp3c9_16670.
DR   EnsemblPlants; Pp3c9_16670V3.3; Pp3c9_16670V3.3; Pp3c9_16670.
DR   EnsemblPlants; Pp3c9_16670V3.4; Pp3c9_16670V3.4; Pp3c9_16670.
DR   Gramene; Pp3c9_16670V3.1; Pp3c9_16670V3.1; Pp3c9_16670.
DR   Gramene; Pp3c9_16670V3.2; Pp3c9_16670V3.2; Pp3c9_16670.
DR   Gramene; Pp3c9_16670V3.3; Pp3c9_16670V3.3; Pp3c9_16670.
DR   Gramene; Pp3c9_16670V3.4; Pp3c9_16670V3.4; Pp3c9_16670.
DR   InParanoid; A0A2K1K3F6; -.
DR   OMA; WSENEPR; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000006727; Chromosome 9.
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:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
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        64..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        857..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        979..999
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1011..1031
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..81
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1051 AA;  115336 MW;  32C34E40041FAC41 CRC64;
     MAGEYFPAWA RSVQQCLDHF EVDVRSGLSQ SSIAKRRKQY GWNELEKEPG KPMWKLVLEQ
     FDDMLVKILL VAALISFILA YIDGHSPDTS GIGAYVEPLV ILFILILNAI VGVWQESNAE
     NALEALKEMQ SENAKVFRDG KYISDLPARE LVPGDIVELR VGDKVPADMR IVKLKTSTVR
     VEQSSLTGES MSVTKTSYAV EENIELQGKE CMVFAGTTIV NGCFLSVVIT TGMKTEIGKI
     QSQIQEASLE EADTPLKKKL DEFGELLTKV IGVICLLVWI INYKYFLSWE MKDGWPTNFQ
     FSFEKCTYYF KIAVALAVAA IPEGLPAVIT TCLALGTRKM AAKNAIVRKL PSVETLGCTT
     VICSDKTGTL TTNQMSVTDL VLNGPAAGVT RQFHVEGTTY SFLDGKIAGL RIGQLDPNIQ
     SFAEIASLCN DAGILYQGNT FKATGMPTEA ALKVVVEKMG VPDPATQSII TNQRSSEALA
     LNGEVPLGCN DWWSENEPRI AILEFDRSRK SMSCIVRKDG VNRLLVKGAV ENILERSTRV
     QLSDGSVVKM TQSARDDLLA KLDSLSAKAL RCLGLAYKDD LQDLGDYDGD HHPGHARLLD
     TSNYDKIESD LIFVGMAGIR DPPREEVRGA IEDCNEAGIR VMVITGDNKN TAEAICSEIG
     IFKDGEDLKD KSFTGREFME FSPERRRKIL SGTGGRVFSR AEPKHKQDIV RILKEAGEVV
     AMTGDGVNDA PALKLADIGV AMGIAGTEVA KEAADMVLAD DNFSTIVAAV GEGRSIYNNM
     KAFIRYMISS NIGEVASIFM TAALGMPEGL VPVQLLWVNL VTDGPPATAL GFNPPDLDIM
     QKPPRKSDDV LINAWVFFRY LVIGLYVGVA TVGAFALWYT QASFLGINLA ADGHTLVSFS
     QLTHWGECST WKDFKVAPFT AGDLTLSFDD NPCDYFTTGK VKATTLSLSV LVAIEMFNSL
     NALSEDGSLV SMPPWVNPWL LLAMGLSFSL HFLILYIPFL AKIFGIVPLS LLEWLLVLVV
     SLPVILIDEV LKFIGRRMNQ RERQARKLKW A
//
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