UniProt: A0A4X2LZ71

Database: UniProt
Entry: A0A4X2LZ71_VOMUR

LinkDB:  A0A4X2LZ71_VOMUR 
Original site:  A0A4X2LZ71_VOMUR

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (29)   

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ID   A0A4X2LZ71_VOMUR        Unreviewed;      1188 AA.
AC   A0A4X2LZ71;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP8A2 {ECO:0000313|Ensembl:ENSVURP00010026916.1};
OS   Vombatus ursinus (Common wombat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX   NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010026916.1, ECO:0000313|Proteomes:UP000314987};
RN   [1] {ECO:0000313|Proteomes:UP000314987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Yazar S.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSVURP00010026916.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A4X2LZ71; -.
DR   STRING; 29139.ENSVURP00010026916; -.
DR   Ensembl; ENSVURT00010030666.1; ENSVURP00010026916.1; ENSVURG00010020634.1.
DR   GeneTree; ENSGT00940000157332; -.
DR   OMA; DMMIYQR; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000314987; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:SF98; PHOSPHOLIPID-TRANSPORTING ATPASE IB; 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; 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:UP000314987};
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        315..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        359..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        887..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        960..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        997..1017
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1029..1052
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1064..1084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          58..121
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          848..1098
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1168..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1188 AA;  133494 MW;  C3BF92954629C97A CRC64;
     MPNTSGLDKA LKMSLRRKSK IHSSAGPVYT TSSYKKADDE MSGTTSTADL EEAPTRTIYF
     NQPQQTKFHD NQVSTAKYSV VTFLPRFLYE QIRRAANAFF LFIALLQQIP DVSPTGRYTT
     LVPLIFILTV AGIKEIIEDY KRHKADNTVN RKKTIVLRNG MWQNIIWKEV AVGDVVKITN
     GQYFPADLIL ISSSEPQAMC YIETSNLDGE TNLKIRQSLT QTANLTSREQ LIKVSGRIEC
     EGPNRHLYDF TGNLYLDGNS SVSIGPDQIL LRGAQLRNTQ WVFGIVVYTG HDTKLMQNST
     KAPLKRSNVE KVTNVQILVL FCILLVMALV SSVGALLWNR THENMSWYIS EIEGISNNFG
     YNLLTFIILY NNLIPISLLV TLEVVKFIQA LFINWDLDMY YMENDTPAMA RTSNLNEELG
     QVKYLFSDKT GTLTCNIMTF KKCSIAGVTY GHFPELERER SSEDFSQLPP PTSDSCIFDD
     PRLLQNIEND HPTAACIQEF LTLLAVCHTV VPEPDGNTIN YQASSPDEGA LVKGAKKLGF
     VCTARTPDSV IIEALGQEET FKILNILEFS SDRKRMSVIV RTPSGQIRLY CKGADNVIYE
     RLSEKSEFTE QTLCHLEYFA TEGLRTLCIA YADISEDVYQ EWLTVYNTAS ATLKDRTRRL
     EECYEIIEKD LLLLGATAIE DRLQAGVPET ISTLMKAEIK IWILTGDKQE TAINIGYACR
     LVSQSMSLIL VNEHSLDATR EALTQHCVCL GNSLGKENDI ALIIDGHTLK YALSFEVRQI
     FLDLALSCKA VICCRVSPLQ KSEVVDMVKK HVKAITLAIG DGANDVGMIQ TAHVGVGISG
     NEGMQATNSS DYAIAQFAYL EKLLLVHGAW SYNRVTKCIL YCFYKNVVLY IIELWFAFVN
     GFSGQILFER WCIGLYNVIF TALPPFTLGI FERTCTQESM LRFPQLYSIT QNAEGFNTKV
     FWGHCINALI HSIILFWGPM KVLEHDAVLA SGRVVDYLFV GNIVYTYVVV TVCLKAGLET
     RAWTKFSHLA VWGSIVLWLA FFGVYSTFWP VIPLAPDMLG QAGMVLRCGY FWLGLLLVPG
     TCLLKDLAWT AAKHTYHKTL LEQVQELETK SKDLGKTMLR DSNGKSLNER DHLLKRLGRK
     TPPSLFRSNS IQQGVSHGYA FSQEEHGVVS QSEVVRSYDT TKQRAGVQ
//

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