UniProt: A0A287A265

Database: UniProt
Entry: A0A287A265_PIG

LinkDB:  A0A287A265_PIG 
Original site:  A0A287A265_PIG

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (15)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
All databases (25)   

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ID   A0A287A265_PIG          Unreviewed;      1063 AA.
AC   A0A287A265;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=LOC100625134 {ECO:0000313|Ensembl:ENSSSCP00000037839.1};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000037839.1, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000037839.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000037839.1,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000037839.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A287A265; -.
DR   Ensembl; ENSSSCT00000042573.3; ENSSSCP00000037839.1; ENSSSCG00000023771.4.
DR   GeneTree; ENSGT00940000165049; -.
DR   Proteomes; UP000008227; Chromosome 11.
DR   Bgee; ENSSSCG00000023771; Expressed in testis and 17 other cell types or tissues.
DR   ExpressionAtlas; A0A287A265; baseline and differential.
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; 2.
DR   PANTHER; PTHR24092:SF59; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 2.
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:UP000008227};
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        261..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        305..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        794..815
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        863..885
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        910..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        945..966
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          18..81
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          755..893
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   DOMAIN          898..965
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1063 AA;  119803 MW;  63CF6D6D3EB2748D CRC64;
     MGWRRPLQRT DVTKARTIYL NEPHRNSFCK NSISTAKYSL WSFLPRYLYL QFSKAANAFF
     LFITILQQIP DVSPTGKYTT LLPLLIILVI SGIKEIVEDY VSLLLLNAPN PTALGVNVGD
     IVKATDGQFL PADVVLISSS QPQATCYVAT SNLDGETNLK IRQALLETAE IQTEKQLSSL
     SGKIECEGPN CHFNNFIGTL YLNGKSPVSI GPDQVLLRGT QLKNTDWIFG IVVYTGFETK
     FMQVNMQSPL KRSRVEKVTN VQILVLFLML LVMALVSCVG AAFWNGTYGE NTWYIGKKGN
     FWFDILMFII LYHNLIPISL LVTLEIVKSI QAMFINWDED MHYERNDVYA MARTSSLNEE
     LGQVKYLFSD KTGTLTCNIM TFKKCTIAES SEFSDPKLLE NFEEDHPTKE YIKEFLFLLS
     VCHTVVPERD GNNISYQASS PDEAALVKGA KKLGFVFTAR TPYSVTIEAM GEEFTFQILN
     VLEFSSNRKR MSVIVRTPTG QLRLYCKGAD SVIYERLSED SLFVKETLTH LESFAREGLR
     TLCIAYIDLT ELEYQQWLAM YEEVCTVVQD RAQSLEHCYD TIEKFLLLGA TAIEDRLQAR
     VPETIANLLK ANIRIWLLTG DKEETAVNIG NRHKECFFLN LVVHEGSLGG STRTCDLGAL
     LGKENDLALI IDGKTLKHAL HFEVKKSFLN LALSCRAVLC CRLSPLQKAE IVDLVKSHVR
     AITLAIGDGA NDVGMIQTAH VGVGISGNEG MQATNNSDYA IAQFSHLEKL LLVHGAWSYF
     RVTKCVLYCF YKNVVLYIIE LWFAFVNGFS GQILFERWCI SLYNVIFTSL PTITLGIFEQ
     CCSQESLLRY PQLYTISQTG DIFNIKVLWI QCINAFVHSF ILFWLPTKML KHGNSFIVSN
     ICQRACYSHL AIWGSILIWL VFFTVYSFFW PTIPISPEMT GQASMVLACP YFWLGFFLVP
     IVSGFANRSL AVPARNVPCL GPWPGCDQCV PVQQEFEFLS PECSLYALCA LTASLCFALA
     GGYAFSQVEH AVISQEELVR SYDTTKSKTR RTFSTAFSES IFE
//

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