UniProt: A0A672ZNX8

Database: UniProt
Entry: A0A672ZNX8_9TELE

LinkDB:  A0A672ZNX8_9TELE 
Original site:  A0A672ZNX8_9TELE

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (26)   

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ID   A0A672ZNX8_9TELE        Unreviewed;      1154 AA.
AC   A0A672ZNX8;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=atp11c {ECO:0000313|Ensembl:ENSSORP00005018524.1};
OS   Sphaeramia orbicularis (orbiculate cardinalfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX   NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005018524.1, ECO:0000313|Proteomes:UP000472271};
RN   [1] {ECO:0000313|Ensembl:ENSSORP00005018524.1}
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; A0A672ZNX8; -.
DR   Ensembl; ENSSORT00005019071.1; ENSSORP00005018524.1; ENSSORG00005004147.1.
DR   InParanoid; A0A672ZNX8; -.
DR   Proteomes; UP000472271; 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:SF38; PHOSPHOLIPID-TRANSPORTING ATPASE IG; 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:UP000472271};
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        90..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        311..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        365..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1002..1024
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1039..1058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1070..1091
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          64..117
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          888..1135
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1154 AA;  132128 MW;  B138674CFE3C8C62 CRC64;
     MHRHDDISWI DAKISYNTCE GRGLLCLHHL FKNHFLGGDE RRVDSRTIYV GHRPCPASEP
     FIPPKFCDNR IVSSKYTVWN FLPKNLFEQF RRIANFYFLI IFLVQVIVDT PTSPVTSGLP
     LFFVITVTAI KQGYEDWLRH KADNEVNKYP VTVLEDGRRI RKESEKIKVG DVVQVEEDET
     FPCDLILLQS SRDDDTCFVT TASLDGESNH KTHYTVPDTE KDLESLNATI ECEQPQPDLY
     KFVGRMHIYK NNQEPAVRSL GPENLLLKGA TLKNTQKICG VAVYTGMETK MALNYQGKSQ
     KRSVVEKSIN AFLLVYLCIL VSKALVCTTL KYVWQSKPGQ DEPWYNEKTQ REKDTNLYLK
     MFTDFLSFMV LFNFIIPVSM YVTVEMQKFL GSFFITWDKD FFDPEIKEGA LVNTSDLNEE
     LGQVEYVFTD KTGTLTQNNM EFIECCIDGF QYKYRDASSE LDGFCVTDGP VSKLQQKAGR
     EKEELFLRAL CLCHTVQVKE STEQGQDQVD GLTDQLDGLG VDGELSQPQE QQRGFIASSP
     DEIALVKGAM RYGFTFLGLE SKTMKILNRN NDVEKYELLH VLNFDPVRRR MSVIVRSTSG
     DTLLFCKGAD SSIFPRVRQE EVERIRMHVE RNATEGYRTL CVAYKHLSAV EYAQADAGLR
     EARLALQDRE EKLMAVYNQV ETGMSLIGAT AVEDRLQEEA AETMEALQGA GIKVWVLTGD
     KMETAKSTCY ACRLFQRNTE LLELTVRTLE DGGRRREERL HELLLEYHKK AVQDAPPVKA
     GVTRSWSSAN QDYGFIVDGA TLSMVLNSSS DSNSSRYKNL FLQICQNCTA VLCCRMAPLQ
     KAQIVKMVKN SKGNPITLSI GDGANDVSMI LEAHVGIGIK GKEGRQAVRN SDYAIPKLKH
     LKKLLLAHGH LYYVRIAHLV QYFFYKNLCF ILPQFLYQFF CGYSQQPLYD AAYLTMYNIC
     FTSMPILAYS LLEQHICIEV LLDNATLYRE IAKNAMLRWG PFLYWTILGV FHGLLFFFGV
     RYLFSNPALQ DNGQVFGNWS YGTIVFTVLV FTVTLKLALD TRHWTWINHF VIWGSLAFYV
     FFSFFWGGII WPFLRQQRLY FVFANMLSSV SAWLVIILLI LLSLLPEILL VVFRKPRGPH
     SRQVQFVMIK FVLI
//

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