UniProt: A0A3Q0H8W1

Database: UniProt
Entry: A0A3Q0H8W1_ALLSI

LinkDB:  A0A3Q0H8W1_ALLSI 
Original site:  A0A3Q0H8W1_ALLSI

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (24)   

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ID   A0A3Q0H8W1_ALLSI        Unreviewed;      1162 AA.
AC   A0A3Q0H8W1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP11C {ECO:0000313|RefSeq:XP_025068501.1};
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_025068501.1};
RN   [1] {ECO:0000313|RefSeq:XP_025068501.1}
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_025068501.1; XM_025212716.1.
DR   AlphaFoldDB; A0A3Q0H8W1; -.
DR   STRING; 38654.A0A3Q0H8W1; -.
DR   InParanoid; A0A3Q0H8W1; -.
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; 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; 2.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24092:SF38; PHOSPHOLIPID-TRANSPORTING ATPASE IG; 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: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        291..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        345..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        903..923
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        953..975
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        987..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1021..1044
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1064..1084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          38..92
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          840..1087
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1162 AA;  132934 MW;  E8E69B1FDC9AC103 CRC64;
     MALLLPGASQ CAGEEKRVGT RTVLVGHRPV SETDAYVAQK FCDNRIVSSK YTVWNFLPKN
     LFEQFRRIAN FYFLIIFLVQ VIVDTPTSPV TSGLPLFFVI TVTAIKQGYE DWLRHRADNE
     VNKSNVFVIE NAKQVRKESE KIKVGDIVEV KADETFPCDL IFLASSSPDG TCYVTTASLD
     GESNFKTHYA VRDTTVLCTH EAIDSLAATI ECEQPQPDLY KFVGRINIYR SNQEPIARSL
     GPENLLLKGS TLKNTKKIYG VAVYTGMETK MALNYQGKSQ KRSAVEKSIN AFLVVYLCIL
     LSKATVCTTM KYVWQSNPFN DEPWYNEKTK KEKEAFKVLR MFTDFLSFMV LFNFIIPVSM
     YVTVEMQKFL GSFFISWDKE MYDEEIKEGA LVNTSDLNEE LGQVEYVFTD KTGTLTENSM
     EFIECCIDGH KYKESISEVD GPLKYYGKAE KCREELFLRA LCLCHTVQIK EGDQVDGLIG
     HLEHRSTYIS SSPDEIALVK GAKKYGFSFL GLENDYMKVK NQNNETERYQ LLHILNFDPV
     RRRMSVIVRT ITGKLLLFCK GADSSIFPKV QQDEIQQTKA HVDRNAMDGY RTLCVAFKEL
     SQEEYDQIDK QICEAKMALQ DREEKMAKVF EDIEANMHLI GATAVEDKLQ EQAAETIEAL
     HAAGMKVWVL TGDKMETAKS TCYACRLFQT NTELLELTTK TVGHSERKED RLHELLMEYH
     KRLLQDFPKN RGGHKRSWML NHEYGLIIDG STLSLILNPS QDSSSSNYKT IFLQICLKCT
     AVLCCRMAPL QKAQIVRMVK STKGSPITLS IGDGANDVSM ILEAHVGIGI KGKEGRQASR
     NSDYAVPKFK HLRKLLLAHG HLYYVRIAHL VQYFFYKNLC FILPQFLYQF FCGFSQQPLY
     DAAYLTMYNI CFTSLPILAY SLLEQHINIE TLTSDPQLYM KISDNAMLQW KPFLYWTFLG
     AFEGLVFFFG VYYLFQNSSL EDNGKVFGNW TFGTIVFTIL VFTVTLKLAL DTRFWTWMNH
     FVIWGSLAFY VFFSFFWGGI IWPFLKQQRM YFVFAHMVTS LSTWLAIILL IFISLFPEIL
     LIVFKNVRRK AQEHPLSSCS LKLPAITAFL GVNKSNIQIE NQREVGAEGT SRGHPSSPAS
     CLRQHHPYPN YPIHATNQKC PL
//

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