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Probable phospholipid-transporting ATPase VD (EC 3.6.3.1) (ATPase class V type 10D) (P4-ATPase flippase complex alpha subunit ATP10D)

 AT10D_MOUSE             Reviewed;        1416 AA.
Q8K2X1;
25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 2.
07-NOV-2018, entry version 127.
RecName: Full=Probable phospholipid-transporting ATPase VD;
EC=7.6.2.1;
AltName: Full=ATPase class V type 10D;
AltName: Full=P4-ATPase flippase complex alpha subunit ATP10D;
Name=Atp10d;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAH29551.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANTS ALA-700 AND LEU-716.
STRAIN=BALB/cJ, C57BL/6J, CAST/EiJ, MAI, MBT, and PWK;
TISSUE=Monocyte;
PubMed=12532265; DOI=10.1007/s00335-002-3032-3;
Flamant S., Pescher P., Lemercier B., Clement-Ziza M., Kepes F.,
Fellous M., Milon G., Marchal G., Besmond C.;
"Characterization of a putative type IV aminophospholipid transporter
P-type ATPase.";
Mamm. Genome 14:21-30(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1079-1416 (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Catalytic component of a P4-ATPase flippase complex
which catalyzes the hydrolysis of ATP coupled to the transport of
aminophospholipids from the outer to the inner leaflet of various
membranes and ensures the maintenance of asymmetric distribution
of phospholipids. Phospholipid translocation seems also to be
implicated in vesicle formation and in uptake of lipid signaling
molecules (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
phosphate + phospholipid(Side 2).
-!- SUBUNIT: Component of a P4-ATPase flippase complex which consists
of a catalytic alpha subunit and an accessory beta subunit.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250}. Note=Exit from the endoplasmic reticulum requires
the presence of TMEM30A. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000305};
IsoId=Q8K2X1-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q8K2X1-2; Sequence=VSP_006959;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in placenta and kidney.
{ECO:0000269|PubMed:12532265}.
-!- POLYMORPHISM: In strain C57BL/6, a polymorphism generates a
premature stop codon at position 764.
{ECO:0000269|PubMed:12532265}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH29551.1; Type=Frameshift; Positions=1136; Evidence={ECO:0000305};
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EMBL; AJ441079; CAD29578.1; -; mRNA.
EMBL; BC029551; AAH29551.1; ALT_FRAME; mRNA.
RefSeq; NP_700438.3; NM_153389.3.
UniGene; Mm.32775; -.
UniGene; Mm.441066; -.
ProteinModelPortal; Q8K2X1; -.
iPTMnet; Q8K2X1; -.
PhosphoSitePlus; Q8K2X1; -.
PRIDE; Q8K2X1; -.
GeneID; 231287; -.
KEGG; mmu:231287; -.
UCSC; uc008xrh.2; mouse. [Q8K2X1-1]
CTD; 57205; -.
MGI; MGI:2450125; Atp10d.
HOVERGEN; HBG107129; -.
InParanoid; Q8K2X1; -.
KO; K01530; -.
PhylomeDB; Q8K2X1; -.
PRO; PR:Q8K2X1; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ATP10D; -.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IBA:GO_Central.
GO; GO:0006812; P:cation transport; NAS:UniProtKB.
GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030360; ATP10D.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
PANTHER; PTHR24092:SF84; PTHR24092:SF84; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01652; ATPase-Plipid; 2.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
2: Evidence at transcript level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Endoplasmic reticulum; Lipid transport; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome;
Translocase; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1416 Probable phospholipid-transporting ATPase
VD.
/FTId=PRO_0000046384.
TOPO_DOM 1 97 Cytoplasmic. {ECO:0000255}.
TRANSMEM 98 118 Helical. {ECO:0000255}.
TOPO_DOM 119 120 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 121 141 Helical. {ECO:0000255}.
TOPO_DOM 142 321 Cytoplasmic. {ECO:0000255}.
TRANSMEM 322 342 Helical. {ECO:0000255}.
TOPO_DOM 343 365 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 366 386 Helical. {ECO:0000255}.
TOPO_DOM 387 1110 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1111 1131 Helical. {ECO:0000255}.
TOPO_DOM 1132 1142 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 1143 1163 Helical. {ECO:0000255}.
TOPO_DOM 1164 1192 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1193 1213 Helical. {ECO:0000255}.
TOPO_DOM 1214 1221 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 1222 1242 Helical. {ECO:0000255}.
TOPO_DOM 1243 1252 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1253 1273 Helical. {ECO:0000255}.
TOPO_DOM 1274 1289 Exoplasmic loop. {ECO:0000255}.
TRANSMEM 1290 1310 Helical. {ECO:0000255}.
TOPO_DOM 1311 1416 Cytoplasmic. {ECO:0000255}.
NP_BIND 993 1000 ATP. {ECO:0000305}.
NP_BIND 1361 1368 ATP. {ECO:0000305}.
ACT_SITE 438 438 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 1053 1053 Magnesium. {ECO:0000250}.
METAL 1057 1057 Magnesium. {ECO:0000250}.
VAR_SEQ 1120 1135 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006959.
VARIANT 700 700 V -> A (in strain: CAST, MAI, MBT and
PWK). {ECO:0000269|PubMed:12532265}.
VARIANT 716 716 S -> L (in strain: CAST, MAI, MBT and
PWK). {ECO:0000269|PubMed:12532265}.
CONFLICT 1239 1239 L -> F (in Ref. 2; AAH29551).
{ECO:0000305}.
SEQUENCE 1416 AA; 158330 MW; 1799CCF062E22BB0 CRC64;
MTELLQWARH HWRRLSHGRA QGEDERPYNY ASLLACGGKS SRTPRPAGKH RVVIPHLQCF
KDEYERFSGT YVNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK
EITMLPLVVV LTIIAIKDGL EDYRKYKIDK QINNLITKVY SRKEKKYIDC CWKNVTVGDF
IRLSCNEIIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVVRGYTEQ DSEVDPEKFS
SRIECESPNN DLSRFRGFLE HANKERVGLS KENLLLRGCT IRNTEAVVGI VVYAGHETKA
MLNNSGPRYK RSKLERRANT DVLWCVLLLI VMCLTGALGH GIWLSRYENM LFFNIPEPDG
RVISPVLTGF YVFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQSDVDFY NEKMDSTIQC
RALNITEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY CHEENAKRLE SYQEAVSEEE
ECTDTLGGSL SNMARPRAQG CRTVPSGPLG KPSAQLSGST SAVGNGEGSG EVPHSRQAAF
SSPMETDVVP DTRLLDKFSQ LTPQLLTGLD GTAQSSPLET LYIMDFFIAL AICNTVVVSA
PNQPRQKIGL SSLGGMPIKS LEEIKNIFQK LSVRRSSSPS LASGKDSSSG TPCAFVSRIS
FFSRPKLSPP MEDESSQMDE IPQASNSACC TETEAQNRAV GLSVSSAEAL SGPPPSASNL
CYEAESPDEA ALVYAARAYR CTLQSRTPEQ VMVDFAALGS LTFQLLHILP FDSVRKRMSV
VVRHPLSKQV VVYTKGADSV IMELLSVAAS DGTNPEQQMI IRERTQRHLD EYAKRGLRTL
CVAKKVMSDT EYAEWLRNHF LAETSIDNRE ELLVESAMRL ENKLTLLGAT GIEDRLQEGV
PESIEALHQA GIKIWMLTGD KQETAVNIAY ACKLLEPDDK LFILNTQSQD ACGMLMSAIL
EELQKRAQVS PELASSRKNF PQPSDAQGQG RAGLVITGKT LEFALQESLQ RQFLELTAWC
QAVICCRATP LQKSEVVKLV RNHHHVLTLP IGDGANDVSM IQVADIGIGV SGQEGMQAVM
ASDFAISQFR HLSKLLLVHG HWCYTRLSNM ILYFFYKNVA YVNLLFWYQF FCGFSGTSMT
DYWVLIFFNL LFTSVPPIIY GVLEKDVSAE TLLQLPELYR SGQRSEEYLP LTFWITLLDA
FYQSLVCFFV PYFTYQGSDI DIFTFGNPLN TAALFIILLH LVIESKSLTW IHMLVTVGSI
LSYFFFALAF GALCVTCNPP SNPYGIMRKH MLDPVFYLVC VLTTFVALLP RFLYRVLQGS
VFPSPVLRAK YFDRLPPEER AEALKRWRGT AKVNHVASKH ASQSAAMSGR PTPGSSAVLA
MKSATVSTVE QSTRETALDR GCSEPGASKM TGSSAS


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