UniProt: A0A2Y9JBN9

Database: UniProt
Entry: A0A2Y9JBN9_ENHLU

LinkDB:  A0A2Y9JBN9_ENHLU 
Original site:  A0A2Y9JBN9_ENHLU

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (25)   

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ID   A0A2Y9JBN9_ENHLU        Unreviewed;      1137 AA.
AC   A0A2Y9JBN9;
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=LOC111146967 {ECO:0000313|RefSeq:XP_022358451.1,
GN   ECO:0000313|RefSeq:XP_022358452.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022358452.1};
RN   [1] {ECO:0000313|RefSeq:XP_022358451.1, ECO:0000313|RefSeq:XP_022358452.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022358451.1,
RC   ECO:0000313|RefSeq:XP_022358452.1};
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_022358451.1; XM_022502743.1.
DR   RefSeq; XP_022358452.1; XM_022502744.1.
DR   Proteomes; UP000248482; 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; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 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:UP000248482};
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        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        295..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        349..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        915..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        965..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        999..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1033..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1063..1088
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          43..96
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          851..1103
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1137 AA;  129881 MW;  63308792F8C99ABA CRC64;
     MDCGRVRTLV HRYCAGEENC VDSRTIYVGH REPPPGAEAY IPQRHPDNRI VSSKYTFWNF
     IPKNLFEQFR RIANFYFLII FLVQLIIDTP TSPVTSGLPL FFVITVTAIK QGYEDWLRHK
     ADNAMNQCPV HFIQHGKLVR KQSRKLRVGD IVMVKEDETF PCDLIFLSSS RGDGTCHVTT
     ASLDGESSHK THYAVQDTKG FHTEEDIDGL HATIECEQPQ PDLYKFVGRI NVYSDRSDPM
     VRPLGSENLL LRGATLKNTE KVFGVAIYTG METKMALNYQ SKSQKRSAVE KSMNVFLIVY
     LCILISKALI NTVLKYVWQS EPFRDEPWYN QKTESERQRN LLLRALTDFL AFMVLFNYII
     PVSMYVTVEM QKFLGSYFIT WDEEMFDEDT GEGPVVNTSD LNEELGQVEY IFTDKTGTLT
     ENNMEFKECC IEGHVYVPHA ICNGQVLPGA AGIDMIDSSP GVSTREREEL FFRALCLCHT
     IQVKDNDDMD GPRKSPDGGK SCVYISSSPD EVALVEGIQR LGFTYLRLRD GYMEILNREN
     DVERFELLEI LSFDSVRRRM SVIVKSVTGE IYLFCKGADS SIFPRVIEGK VDQIRARVER
     NAVEGLRTLC VAYKRLAPEE YDGVCTLLQA AKVALQDREK KLAEAYEQIE KDLILLGATA
     VEDRLQEKAA DTIEALQKAG IKVWVLTGDK METAAATCYA CRLFRRGTQL LELTTKRLEE
     QSLHDVLFEL SKTVLRHSGS LTRDNFSGLS ADLEDFGLII DGAALSLVMK PREDGSGGNY
     RELFLEICRN CSAVLCCRMA PLQKAQIVKL IKLSKEHPIT LAIGDGANDV SMILEAHVGI
     GVIGKEGRQA ARNSDYAVPK FKHLKKMLLV HGHFYYVRIS ELVQYFFYKN VCFIFPQFLY
     QFFCGFSQQT LYDTAYLTLY NISFTSLPIL LYSLMEQHVS IDTLRREPSL YRDIAKNALL
     RWRVFIYWTL LGVFDALVFF FGAYFLFENT TVTSNGQIFG NWTFGTLVFT VMVFTVTLKL
     ALDTHYWTWI NHFVIWGSLL FYVVFSLLWG GIIWPFLSYQ RMYYVFIQML SSGPAWLVII
     LLVTVSLFPD VLKKVLCRQL WPSATERIQQ STSLRASVAA GTERPLLKDL LSRPRRR
//

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