ID A0A091II15_CALAN Unreviewed; 1154 AA.
AC A0A091II15;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN ORFNames=N300_04093 {ECO:0000313|EMBL:KFO99330.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO99330.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO99330.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO99330.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; KL217819; KFO99330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091II15; -.
DR STRING; 9244.A0A091II15; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF225; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 286..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 330..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 883..901
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 930..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 968..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 999..1019
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1039..1059
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 26..79
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 817..1068
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO99330.1"
FT NON_TER 1154
FT /evidence="ECO:0000313|EMBL:KFO99330.1"
SQ SEQUENCE 1154 AA; 130556 MW; 0BE271D7E81A496C CRC64;
TGYEKTDDVS EKTSLADQEE LRTIFINQPQ LTKFCNNHVS TAKYNIITFL PRFLYSQFRR
AANAFFLFIA LLQELTDQTK ITEIMAHVVP CVLFLPSLQM CQEVDTPILD QKRHKADNAV
NKKQTQVLRN GAWEIVHWEK VDVGDIVIIK GKEYIPADTV LLSSSEPQAM CYIETSNLDG
ETNLKIRQGL PLTSEIKDIE SLMRLSGRIE CESPNRHLYD FVGNIRLDGH GTVPLGADQI
LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKMSNV ERITNIQILI LFCILIAMSL
ICSIGSAIWN RRHTGRDWYL DLNYGGASNF GLNFLTFIIL FNNLIPISLL VTLEVVKFIQ
AYFINWDIDM HYELTDTAAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ FKKCTVAGVA
YGQGSQIGEE KTFSDSTLLE NLQSNHPTAP IICEFLTMMA VCHTAVPERE GDKIIYQAAS
PGNDEGKMIK VCSSLQCKHI ITHFDGRNYM KQSLQPSSSC LPQLLGQEER YELLNVLEFT
STRKRMSVIV RTPSGKLRLY CKGADTVIYD RLAETSKYKE ITLKHLEQFA TEGLRTLCFA
VAEISESDYQ EWLNVYHRAS TAVQNRALKL EESYELIEKN LQLLGATAIE DKLQDNVPET
IETLMKADIK IWILTGDKQE TAINIGHSCK LLKKNMGLIV INEGSLDGTR ETLSHHCSTL
GDALRKENDF ALIIDGKSLK YALTFGVRQY FLDLALSCKA VICCRVSPLQ KSEVVEMVKK
QVKVVTLAIG DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL KNLLLVHGAW
NYNRVAKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNLMF TAMPPLTLGI
FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF HSFILFWFPL KALQHGTVFS
NGKTSDYLLL GNTVYTFVVL TVCLKAGLET SYWTLFSHIA IWGSIALWVV FFGIYSSLWP
VIPMAPDMSG EAAMMFSSGV FWMGLLCIPM AALLFDVVYK VIKRATFKTL VDEVQELEAK
SEDPGEVVHG KSLTERAQLL KNVFRKNHVN LYRSDSLQQN LLHGYAFSQD EHGIVSQSEV
IRAYDTTKQR PEEW
//
