ID A0A1U7R4G6_ALLSI Unreviewed; 1520 AA.
AC A0A1U7R4G6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP10A {ECO:0000313|RefSeq:XP_006017133.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006017133.1};
RN [1] {ECO:0000313|RefSeq:XP_006017133.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_006017133.1; XM_006017071.3.
DR GeneID; 102367742; -.
DR KEGG; asn:102367742; -.
DR CTD; 57194; -.
DR eggNOG; KOG0206; Eukaryota.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000189705; Unplaced.
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; 2.
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; 2.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF81; PHOSPHOLIPID-TRANSPORTING ATPASE VA; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000189705};
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 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 305..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1115..1135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1165..1188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1194..1215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1222..1242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1267..1286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 57..106
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1051..1296
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 171607 MW; FFAE60F47F37F8DE CRC64;
MVEAAESRGD VPPVQEEAKE RKKKKKRKKK ESKTRTVRSN LLLPGLEVEK PKGGPLANNR
LKTTKYTALS FLPKNLFEQF HRLANVYFVF IALLNFVPTV NAFQPELALA PVLFILAVTA
IKDLWEDYSR YRSDKEINHM ECLVYCRNEK KYISRYWKEV EVGDFVQLRC NEIIPADILL
LSSSDPDGLC HIETANLDGE TNLKQRQVLR RFLELDSEFD PLKFTSVIEC EKPNNDLTRF
RGYIIHTNGN RDGLYKENLL LRGCTIRNTE EVTGIVIYAG HETKALLNNN GPRYKRSKLE
RQMNIDVLWC VLILIVMCLF SAIGHGLWVW QFSEKKKPVF DVPGPDGNYL SPVLAAVYLF
LTMIIVFQVL IPISLYVSIE IVKICQVYFI HQDKDLYDEE TDSQLQCRAL NITEDLGQIQ
YIFSDKTGTL TENKMVFRRC TVSGIEYSHD ANAKRLAMYQ EPDSEEEETA PKGVTLSQRD
SICSHQSVKA VHRSQSTKSH RRTGSRAEAK RASILSKHTA FSSPMEKDIT PDPNLLEKVN
ECARYLEVMR SHEQPLSQLS PELSDIFDFF IALTICNTVV VTSPNQPRQK VRVRFELKSP
VKTIEDFIRR FTPSRLTAGS NSSSSSSLAT SKSMHRFGSS LLSSTSTEST LLKLEEKLAY
SVQMNNNGYS AQQEKGAIES GPEEGELRYE AESPDEAALV YAARAYNCTL VGRLSDQVSI
ELPHLGTLTF EVLHTLGFDS IRKRMSVVVR HPITDEINVY TKGADSVIMD LLLPCSSDDP
RGKHQKKIES KTQNYLNLYA VDGLRTLCIA KRVLSKDEYA CWLKNHLEAE SCIENREELL
FQSALHIEKN LHLLGATGVE DRLQEGVPET IANLRKAGLQ IWVLTGDKQE TAINIAYACK
LLDHDEEIIT LNAESPETCA ILLEQCLHCV ESKFSSNTID NTSGDMKIGF ASFCPPSSSA
HSKLGLVIDG KTLAYALDKT LENRFLLLAK RCRSVLCCRS TPLQKSMVVK LVRDKLKAMT
LAIGDGANDV SMIQVADVGV GISGPEGMQA VMASDFAVPR FRHLEKLLLV HGHWCYSRLA
NMVLYFFYKN AMFVALLFWY QFYCGFSGSS MIDQWYLIFF NLLFSSLPQL ITGVLDKDVP
AEALISIPQL YKSGQNMEDY QPHMFWMNMI DALYQSLVCF FIPYFTFYDS DMDIFSLGTP
ITTIALFTII LHLAVETKTW TFFHWSSCIF SILLFFFVAL VYNASCPTCY PPSNPYWTME
KLMGDPMFYL TCIISPVIAL LPRFLYRTLQ GTLFPTQRQL GCQLHRWPLG TCNHILSKLK
IKKKSTPQKH PFAEPSMQNP TSNVNPCYKV SNENIPSQVS EHGSESALPA STRAEHTRVL
GAAASPQGPL LFGEIKQSSL ASNQERSFGF HEVTCSTSEM ESASVEEMFP WNSTVDQSDF
SLLKWITSTP LFSRFGRVLQ LSSNSLQNET QNNISVLGSG SSLHLGFKGI TEQNSNNFQE
KIKGTPADCC ISDTLETTFL
//
