ID I3LIK9_PIG Unreviewed; 1209 AA.
AC I3LIK9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B2 {ECO:0000313|Ensembl:ENSSSCP00000023915.2,
GN ECO:0000313|VGNC:VGNC:85680};
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:ENSSSCP00000023915.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000023915.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000023915.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDA61794.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000023915.2}
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 EMBL; DQIR01106318; HDA61794.1; -; Transcribed_RNA.
DR RefSeq; XP_005663437.1; XM_005663380.2.
DR STRING; 9823.ENSSSCP00000023915; -.
DR PaxDb; 9823-ENSSSCP00000026958; -.
DR Ensembl; ENSSSCT00000027624.3; ENSSSCP00000023915.2; ENSSSCG00000006550.4.
DR GeneID; 100517341; -.
DR KEGG; ssc:100517341; -.
DR CTD; 57198; -.
DR VGNC; VGNC:85680; ATP8B2.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000160804; -.
DR HOGENOM; CLU_000846_3_2_1; -.
DR OMA; PECIHKL; -.
DR OrthoDB; 275833at2759; -.
DR TreeFam; TF300654; -.
DR Reactome; R-SSC-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000008227; Chromosome 4.
DR Bgee; ENSSSCG00000006550; Expressed in endocardial endothelium and 41 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
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; 1.
DR PANTHER; PTHR24092:SF46; PHOSPHOLIPID-TRANSPORTING ATPASE ID; 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; 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 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 295..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 337..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 890..911
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 973..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1012..1030
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1042..1063
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1083..1106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 36..101
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 859..1112
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1209 AA; 137358 MW; B0230BF6A8915298 CRC64;
MTVPKEMPEK WARAGAPPTW SRKKPSWGTE EERRARANDR EYNEKFQYAS NCIKTSKYNI
LTFLPVNLFE QFQEVANTYF LFLLILQLIP QISSLSWFTT IVPLVLVLTI TAVKDATDDY
FRHKSDNQVN NRQSQVLING ILQQEQWMNV CVGDIIKLEN NQFVAADLLL LSSSEPHGLC
YIETAELDGE TNMKVRQAIP ITSELGDISK LAKFDGEVIC EPPNNKLDKF SGTLYWKENK
FPLSNQNMLL RGCVLRNTEW CFGLVIFAGP DTKLMQNSGR TKFKRTSIDR LMNTLVLWIF
GFLVCMGVIL AIGNAIWEHE VGTRFQVYLP WDEAVDSAFF SGFLSFWSYI IILNTVVPIS
LYVSVEVIRL GHSYFINWDK KMFCTKKRTP AEARTTTLNE ELGQVEYIFS DKTGTLTQNI
MVFNKCSING RSYGDVFDVP GHKAELGERP EPVDFSFNPL ADKKFLFWDP TLLEAVKMGD
PHTHEFFRLL SLCHTVMSEE KNEGELYYKA QSPDEGALVT AARNFGFVFR SRTPKTITVH
EMGEAITYQL LAILDFNNIR KRMSVIVRNP EGKIRLYCKG ADTILLDRLH HSTQELLNTT
TDHLNEYAGE GLRTLVLAYK DLDEEYYEEW AERRLQASLA QDSREDRLAS VYEEVESDMM
LLGATAIEDK LQQGVPETIA LLTLANIKIW VLTGDKQETA VNIGYSCKML TDDMTEVFIV
TGHTVLEVRE ELRKAREKMM DSSRSVGNGF TYQEKLSSSK LSSVLEAVAG EYALVINGHS
LAHALEADME LEFLETACAC KAVICCRVTP LQKAQVVELV KKYKKAVTLA IGDGANDVSM
IKTAHIGVGI SGQEGIQAVL ASDYSFSQFK FLQRLLLVHG RWSYLRMCKF LCYFFYKNFA
FTMVHFWFGF FCGFSAQTVY DQYFITLYNI VYTSLPVLAM GVFDQDVPEQ RSMEYPKLYE
PGQLNLLFNK REFFICIAQG IYTSVLMFFI PYGVFAEATR DDGTQLADYQ SFAVTVATSL
VIVVSVQIGL DTGYWTAINH FFIWGSLAVY FAILFAMHSN GLFDMFPNQF RFVGNAQNTL
AQPTVWLTIV LTTVVCIMPV VAFRFLRLNL KPDLSDTVRY TQLVRKKQKA QHRCMRRVGR
TGSRRSGYAF SHQEGFGELI MSGKNMRLSS LALSSFTTRS SSSWIESLRR KKSDSASSPS
AGADKPLKG
//
