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Database: UniProt
Entry: A0A670I4S9_PODMU
LinkDB: A0A670I4S9_PODMU
Original site: A0A670I4S9_PODMU 
ID   A0A670I4S9_PODMU        Unreviewed;       182 AA.
AC   A0A670I4S9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=P-type ATPase N-terminal domain-containing protein {ECO:0000259|Pfam:PF16209};
OS   Podarcis muralis (Wall lizard) (Lacerta muralis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC   Lacertibaenia; Lacertidae; Podarcis.
OX   NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000006495.1, ECO:0000313|Proteomes:UP000472272};
RN   [1] {ECO:0000313|Ensembl:ENSPMRP00000006495.1, ECO:0000313|Proteomes:UP000472272}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA   Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA   Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA   Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA   Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA   Andersson L., Carneiro M.;
RT   "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT   polymorphisms in the wall lizard.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN   [2] {ECO:0000313|Ensembl:ENSPMRP00000006495.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A670I4S9; -.
DR   Ensembl; ENSPMRT00000006920.1; ENSPMRP00000006495.1; ENSPMRG00000004385.1.
DR   GeneTree; ENSGT00940000156162; -.
DR   OMA; CNERRYI; -.
DR   Proteomes; UP000472272; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF57; PHOSPHOLIPID-TRANSPORTING ATPASE IF; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472272}.
FT   DOMAIN          32..65
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
SQ   SEQUENCE   182 AA;  20755 MW;  10A7B4FDB6594320 CRC64;
     NNGWKRQRGF DPPHQSDNRT IYIANRFPQH GHYVPQKFAE NRIISSKYTV WNFVPKNLFE
     QFRRVLMIDT PTSPITSGLP LFFVITVTAI KQGYEDWLRH KADNEVNGAP VYVVRSGGLV
     KTRSKNIRVG DIVRVAKDET FPVDLVLLSS DRADGSCYVT TASLDGETNL KVCFHHLLYT
     LS
//
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