ID A0A2Y9GIQ3_NEOSC Unreviewed; 1202 AA.
AC A0A2Y9GIQ3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|RefSeq:XP_021537850.1};
OS Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Neomonachus.
OX NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021537850.1};
RN [1] {ECO:0000313|RefSeq:XP_021537850.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_021537850.1};
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_021537850.1; XM_021682175.2.
DR AlphaFoldDB; A0A2Y9GIQ3; -.
DR Proteomes; UP000248481; Chromosome 6.
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; 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; 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:UP000248481};
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 883..904
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 916..936
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 966..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1005..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1035..1056
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1076..1099
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 852..1105
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 1174..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 136180 MW; C45EE179C19E8677 CRC64;
MTVPKEMPEK WARAGAPPSW SRKKPSWGTE EERRARANDR EYNEKFQYAS NCIKTSKYNI
LTFLPVNLFE QFQEVANTYF LFLLILQLIP QVSSLSWFTT IVPLVLVLAI TAVKDATDDY
FRHKSDNQVN NRQSQVLING SLQQEQWMNV CVGDIIKLEN NQFVAADLLL LSSSEPHGLC
YIETAELDGE TNMKVRQAIP VTSELGDISR LAKFDGEVVC EPPNNKLDRF SGTLYWKDSK
FPLSNQNMLL RGCVLRNTEW CFGLVVFAGP DTKLMQNSGR TKFKRTSIDR LMNTLVLWIF
GFLVCMGVIL AIGNAIWEHE VGTRFQAYLP WDEAVDSAFF SGFLSFWSYI IILNTVVPIS
LYVSVEVIRL GHSYFINWDK KMFCMKKRTP AEARTTTLNE ELGQVEYVFS DKTGTLTQNI
MVFNKCSISG RSYGDVLDVL GHKAELGERP EPVDFSFNPL ADNKFLFWDP TLLEAVKMGD
PHTHEFFRLL SLCHTVMSEE KNEGELYYKA QSPDEGALVT AARNFGFVFR SRTPKTITVH
EMGTAVTYQL LAILDFNNIR KRMSVIVRNP EGRIRLYCKG ADTILLERLH PCTRELLSTT
TDHLNEYAGE GLRTLVLAYK DLDEEYYGEW AQRRLQASLA RDSREDRLAS VYEELLGATA
IEDKLQQGVP ETIALLTLAN IKIWVLTGDK QETAVNIGYS CKMLTDDMTE VFIVTGHTVL
EVREELRKAR EKMLDSPHAV GNGFTCPEKR SAKLTSVLEA VAGEYALVIN GHSLAHALEA
DMELEFLETA CACKAVICCR VTPLQKAQVV ELVKKHKKAV TLAIGDGAND VSMIKTAHIG
VGISGQEGIQ AVLASDYAFS QFKFLQRLLL VHGRWSYLRM CKFLCYFFYK NFAFTMVHFW
FGFFCGFSAQ TVYDQYFITL YNIVYTSLPV LAMGVFDQDV PEQRSMEYPK LYEPGQLNLL
FNKREFFICI AQGIYTSVLM FFIPYGVFAE ATRDDGTQLA DYQSFAVTVA TSLVIVVSVQ
IGLDTGYWTA INHFFIWGSL AIYFAILFAM HSNGLFDMFP NQFRFVGNAQ NTLAQPTVWL
TITLTTVVCI MPVVAFRFLK LSLKPDLSDT VRYTQLVRKK QKAQHRCLQR VGRTSSRRSG
YAFSHQEGFG ELIMSGKNMR LSSLALASFT TRSSSSWIES LRRKKSDSAS SPSGGADKPL
KE
//
