UniProt: A0A2I3RA51

Database: UniProt
Entry: A0A2I3RA51_PANTR

LinkDB:  A0A2I3RA51_PANTR 
Original site:  A0A2I3RA51_PANTR

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (33)   

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ID   A0A2I3RA51_PANTR        Unreviewed;      1123 AA.
AC   A0A2I3RA51;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
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:ENSPTRP00000061506.1,
GN   ECO:0000313|VGNC:VGNC:7635};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000061506.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000061506.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000061506.1}
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   EMBL; AACZ04057002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04057003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04057004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016799797.1; XM_016944308.1.
DR   AlphaFoldDB; A0A2I3RA51; -.
DR   Ensembl; ENSPTRT00000107673.1; ENSPTRP00000061506.1; ENSPTRG00000022333.6.
DR   GeneID; 465889; -.
DR   CTD; 286410; -.
DR   VGNC; VGNC:7635; ATP11C.
DR   GeneTree; ENSGT00940000158878; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000002277; Chromosome X.
DR   Bgee; ENSPTRG00000022333; Expressed in lymph node and 21 other cell types or tissues.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
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; 3.
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   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   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
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:UP000002277};
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}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT   TRANSMEM        58..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        284..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        900..920
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        950..972
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        984..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1018..1041
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1061..1081
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          30..85
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          836..1084
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1123 AA;  128609 MW;  EE3C302E37DB4E6C CRC64;
     MTVCAGEEKR VGTRTVFVGN HPVSETEAYI AQRFCDNRIV SSKYTLWNFL PKNLFEQFRR
     IANFYFLIIF LVQVTVDTPT SPVTSGLPLF FVITVTAIKQ GYEDWLRHRA DNEVNKSTVY
     IIENAKRVRK ESEKIKVGDV VEVQADETFP CDLILLSSCT TDGTCYVTTA SLDGESNCKT
     HYAVRDTIAL CTAESIDTLR AAIECEQPQP DLYKFVGRIN IYSNSLEAVA RSLGPENLLL
     KGATLKNTEK IYGVAVYTGM ETKMALNYQG KSQKRSAVEK SINAFLIVYL FILLTKAAVC
     TTLKYVWQST PYNDEPWYNQ KTQKERETLK VLKMFTDFLS FMVLFNFIIP VSMYVTVEMQ
     KFLGSFFISW DKDFYDEEIN EGALVNTSDL NEELGQVDYV FTDKTGTLTE NSMEFIECCI
     DGHKYKGVTQ EVDGLSQTDG TLTYFDKVDK NREELFLRAL CLCHTVEIKT NDAVDGATES
     AELTYISSSP DEIALVKGAK RYGFTFLGNR NGYMRVENQR KEIEEYELLH TLNFDAVRRR
     MSVIVKTQEG DILLFCKGAD SAVFPRVQNH EIELTKVHVE RNAMDGYRTL CVAFKEIAPD
     DYERINRQLI EAKMALQDRE EKMEKVFDDI ETNMNLIGAT AVEDKLQDQA AETIEALHAA
     GLKVWVLTGD KMETAKSTCY ACRLFQTNTE LLELTTKTIE ESERKEDRLH ELLIEYRKKL
     LHEFPKSTRS FKKAWTEHQE YGLIIDGSTL SLILNSSQDS SSNNYKSIFL QICMKCTAVL
     CCRMAPLQKA QIVRMVKNLK GSPITLSIGD GANDVSMILE SHVGIGIKGK EGRQAARNSD
     YSVPKFKHLK KLLLAHGHLY YVRIAHLVQY FFYKNLCFIL PQFLYQFFCG FSQQPLYDAA
     YLTMYNICFT SLPILAYSLL EQHINIDSLT SDPRLYMKIS GNAMLQLGPF LYWTFLAAFE
     GTVFFFGTYF LFQTASLEEN GKVYGNWTFG TIVFTVLVFT VTLKLALDTR FWTWINHFVI
     WGSLAFYVFF SFFWGGIIWP FLKQQRMYFV FAQMLSSVST WLAIILLIFI SLFPEILLIV
     LKNVRRRSAR RNLSCRRASD SLSARPSVRP LLLRTFSDES NVL
//

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