UniProt: A0A2Y9TB03

Database: UniProt
Entry: A0A2Y9TB03_PHYMC

LinkDB:  A0A2Y9TB03_PHYMC 
Original site:  A0A2Y9TB03_PHYMC

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Ontology (24)   
   GO (24)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG GENES (1)   
   ENSEMBL-UP (3)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (47)   

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ID   A0A2Y9TB03_PHYMC        Unreviewed;      1251 AA.
AC   A0A2Y9TB03;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP8B1 {ECO:0000313|RefSeq:XP_023988076.1,
GN   ECO:0000313|RefSeq:XP_054936238.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023988076.1};
RN   [1] {ECO:0000313|RefSeq:XP_023988076.1, ECO:0000313|RefSeq:XP_054936238.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023988076.1,
RC   ECO:0000313|RefSeq:XP_054936238.1};
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_023988076.1; XM_024132308.3.
DR   RefSeq; XP_054936238.1; XM_055080263.1.
DR   STRING; 9755.ENSPCTP00005008735; -.
DR   Ensembl; ENSPCTT00005009624; ENSPCTP00005008735; ENSPCTG00005006095.
DR   KEGG; pcad:102995646; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000248484; Chromosome 19.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR   GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR   GO; GO:0015247; F:aminophospholipid flippase activity; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:1901612; F:cardiolipin binding; IEA:Ensembl.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140345; F:phosphatidylcholine flippase activity; IEA:Ensembl.
DR   GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
DR   GO; GO:0015721; P:bile acid and bile salt transport; IEA:Ensembl.
DR   GO; GO:0008206; P:bile acid metabolic process; IEA:Ensembl.
DR   GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:2001225; P:regulation of chloride transport; IEA:Ensembl.
DR   GO; GO:0032534; P:regulation of microvillus assembly; IEA:Ensembl.
DR   GO; GO:1903729; P:regulation of plasma membrane organization; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0021650; P:vestibulocochlear nerve formation; IEA:Ensembl.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; IEA:Ensembl.
DR   CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF48; PHOSPHOLIPID-TRANSPORTING ATPASE IC; 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:UP000248484};
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        116..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        139..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        339..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        389..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        950..971
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        983..1003
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1033..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1069..1088
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1100..1124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1144..1167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          75..145
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          919..1173
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..38
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1251 AA;  144071 MW;  741FCEDD1497CB65 CRC64;
     MNTERDSETT FEEDSQPNDE VVPYSDDETE DELEDQEPAV EPEQNRVNRE AEENREPFKK
     DCTWQVKAND RNFHEQPHFM NTKFFCIKES KYENNAIKTY KYNAFTFLPM NLFEQFKRAA
     NFYFLVLLIL QAIPQITTLA WYTTLVPLLV VLGITAIKDL MDDVARHKMD NEINNRTCEV
     IKDGRFKIAK WKEIQVGDVI RLKKNDFIPA DILLLSSSEP NSLCYVETAE LDGETNLKFK
     MALEITHQYL QKENSLATFD GFIECEEPNN RLDKFTGTLF WRNTSFPLDA DKILLRGCVT
     RNTDFCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFVVLTL LSAGLAIGHA
     YWEAQVGNHS WYLYDGEDSA PSYRGFLNFW GYIIVLNTLV PISLYVSVEV IRLGQSYFIN
     WDLQMYYPEK DTPAKARTTT LNEQLGQIHY IFSDKTGTLT QNIMTFKKCC INGQIYGDHR
     DASQNSHSKI EPVDFSWNTY SDGKLVFYDH YLIEQIQSGK EPEVRQFFFL LAACHTVMVD
     RLDGQLNYQA ASPDEGALVS AARNFGFAFL TRTQNTITIS ELGTERTYNV LAILDFNSDR
     KRMSIIVRTP EGNIRLYCKG ADTVIYERLH RMNPMKQETQ DALDIFASET LRTLCLCYKE
     IEEKEFEEWN KKFTAASIAS TNRDEALDKV YEEIEKDLIL LGATAIEDKL QDGVPETISK
     LAKADIKIWV LTGDKKETAE NIGFACELLT EDTTICYGED ISALLHTRME NQRNRSGVYA
     KFVPQAHEPF FPSGGNRALI ITGSWLNEIL LEKKTKRSKI LKLKFPRTEE ERRMRTQSKR
     RLEAKKEQQQ QNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM
     IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF LRYFFYKNFA
     FTLVHFWYSF FNGYSAQTAY EDWFITLYNV LYSSLPVLLM GLLDQDVSDK LSLRFPGLYV
     VGQRDLLFNY RRFFVSLLHG VLTSLILFFI PLGAYLQTVG QDGEAPSDYQ SFAVTIASAL
     VITVNFQIGL DTSYWTFVNA FSIFGSIAIY FGIMFDFHSA GIHVLFPSAF QFTGTASNAL
     RQPYIWLTII LTVAVCLLPV VAIRFLSMTI WPSESDKIQK HRKQLKAEEQ WKRRQNVFRR
     GVSTRRSAYA FSHQRGYADL ISSGRSIRKK RYPLDAVIAD GTAEYRRTME S
//

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