TAT1_CAEEL
ID TAT1_CAEEL Reviewed; 1139 AA.
AC Q9U280; C0P289; Q7JK70;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phospholipid-transporting ATPase tat-1;
DE Short=TAT-1 {ECO:0000303|PubMed:18436785, ECO:0000303|PubMed:21170358, ECO:0000303|PubMed:23427264};
DE EC=7.6.2.1 {ECO:0000269|PubMed:18436785};
GN Name=tat-1; ORFNames=Y49E10.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18436785; DOI=10.1126/science.1155847;
RA Darland-Ransom M., Wang X., Sun C.L., Mapes J., Gengyo-Ando K., Mitani S.,
RA Xue D.;
RT "Role of C. elegans TAT-1 protein in maintaining plasma membrane
RT phosphatidylserine asymmetry.";
RL Science 320:528-531(2008).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21170358; DOI=10.1371/journal.pgen.1001235;
RA Chen B., Jiang Y., Zeng S., Yan J., Li X., Zhang Y., Zou W., Wang X.;
RT "Endocytic sorting and recycling require membrane phosphatidylserine
RT asymmetry maintained by TAT-1/CHAT-1.";
RL PLoS Genet. 6:E1001235-E1001235(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23427264; DOI=10.1091/mbc.e12-10-0730;
RA Li X., Chen B., Yoshina S., Cai T., Yang F., Mitani S., Wang X.;
RT "Inactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores
RT endocytic sorting and recycling in tat-1 mutants.";
RL Mol. Biol. Cell 24:1163-1175(2013).
CC -!- FUNCTION: Transports phosphatidylserine from the outer to the inner
CC leaflet of the plasma membrane, thereby maintaining the enrichment of
CC this phospholipid in the inner leaflet (PubMed:18436785,
CC PubMed:21170358, PubMed:23427264). Ectopic exposure of
CC phosphatidylserine on the cell surface may result in removal of living
CC cells by neighboring phagocytes (PubMed:18436785). Regulation of the
CC phosphatidylserine distribution in plasma membranes is likely to help
CC in the maintenance and control of the membrane surface charge
CC (PubMed:23427264). Plays a role in the formation of the tubular
CC membrane structure and in membrane trafficking and is specifically
CC involved in the recycling and degradation of endocytic cargo, likely
CC with its chaperone protein chat-1 (PubMed:21170358, PubMed:23427264).
CC {ECO:0000269|PubMed:18436785, ECO:0000269|PubMed:21170358,
CC ECO:0000269|PubMed:23427264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:18436785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:18436785};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000269|PubMed:18436785};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18436785};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18436785}. Early
CC endosome membrane {ECO:0000269|PubMed:21170358}; Multi-pass membrane
CC protein. Recycling endosome membrane {ECO:0000269|PubMed:21170358};
CC Multi-pass membrane protein. Note=Colocalizes with its chaperone chat-1
CC at apical and basolateral cell membranes, on early endosomes and on
CC recycling endosomes. Also localizes to intracellular tubular and
CC vesicular structures. {ECO:0000269|PubMed:21170358}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q9U280-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9U280-2; Sequence=VSP_053522, VSP_053524;
CC Name=c;
CC IsoId=Q9U280-3; Sequence=VSP_053523;
CC -!- DISRUPTION PHENOTYPE: Results in abnormal formation of intestinal
CC vacuoles. {ECO:0000269|PubMed:23427264}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; Z98866; CAB11550.4; -; Genomic_DNA.
DR EMBL; Z98866; CAE54923.1; -; Genomic_DNA.
DR EMBL; Z98866; CAX51688.2; -; Genomic_DNA.
DR PIR; D88601; D88601.
DR PIR; T27057; T27057.
DR RefSeq; NP_001022894.1; NM_001027723.2. [Q9U280-1]
DR RefSeq; NP_001022895.1; NM_001027724.2.
DR RefSeq; NP_001255165.1; NM_001268236.1. [Q9U280-3]
DR AlphaFoldDB; Q9U280; -.
DR SMR; Q9U280; -.
DR BioGRID; 41845; 3.
DR STRING; 6239.Y49E10.11c.1; -.
DR SwissLipids; SLP:000000331; -.
DR TCDB; 3.A.3.8.15; the p-type atpase (p-atpase) superfamily.
DR EPD; Q9U280; -.
DR PaxDb; Q9U280; -.
DR PeptideAtlas; Q9U280; -.
DR EnsemblMetazoa; Y49E10.11a.1; Y49E10.11a.1; WBGene00013034. [Q9U280-1]
DR EnsemblMetazoa; Y49E10.11a.2; Y49E10.11a.2; WBGene00013034. [Q9U280-1]
DR EnsemblMetazoa; Y49E10.11b.1; Y49E10.11b.1; WBGene00013034. [Q9U280-2]
DR EnsemblMetazoa; Y49E10.11c.1; Y49E10.11c.1; WBGene00013034. [Q9U280-3]
DR GeneID; 176666; -.
DR KEGG; cel:CELE_Y49E10.11; -.
DR UCSC; Y49E10.11a; c. elegans.
DR CTD; 176666; -.
DR WormBase; Y49E10.11a; CE28133; WBGene00013034; tat-1. [Q9U280-1]
DR WormBase; Y49E10.11b; CE36241; WBGene00013034; tat-1. [Q9U280-2]
DR WormBase; Y49E10.11c; CE44010; WBGene00013034; tat-1. [Q9U280-3]
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000168736; -.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OMA; YWEIGVQ; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9U280; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q9U280; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013034; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005769; C:early endosome; IDA:WormBase.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0005770; C:late endosome; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IDA:WormBase.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IMP:WormBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0006897; P:endocytosis; IMP:WormBase.
DR GO; GO:0007040; P:lysosome organization; IMP:WormBase.
DR GO; GO:0060101; P:negative regulation of phagocytosis, engulfment; IMP:WormBase.
DR GO; GO:0045332; P:phospholipid translocation; IMP:WormBase.
DR GO; GO:0015914; P:phospholipid transport; IMP:WormBase.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:WormBase.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Endosome; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1139
FT /note="Phospholipid-transporting ATPase tat-1"
FT /id="PRO_0000424852"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 901..921
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1013..1033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 388
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1066..1089
FT /note="SYSSNVLENMRLLTSSLRGSTTGS -> RKHVHLHTIIVAIERRLKAVCEWV
FT (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053522"
FT VAR_SEQ 1067..1139
FT /note="YSSNVLENMRLLTSSLRGSTTGSTRSRTASEASLALAEQTRYGFAFSQDESS
FT AVAQTELIRNVDSTREKPTGR -> SWAAYQGPTKDGAHVFANRFSLRKRIQPTSTTAA
FT SHPSATSPPPNGYVEKSQLNGKNGKHHRAKSPDYGSTELSTWSTRDEHEVEYKIPRGRK
FT ERSSYTNRAFIAEDNNVTSIVVNDEEDGSGTRL (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_053523"
FT VAR_SEQ 1090..1139
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053524"
SQ SEQUENCE 1139 AA; 128411 MW; 4EB9BABE669824AC CRC64;
MPTEARDNNR HIHLGKVRDP HHQHAQRFCS NRISTCKYNG FSFLPRFLYE QFRRYNNIFF
LAIALLQQIP DVSPTGRYTT AVPFLIILSV SALKEIFEDV KRRRSDNKVN AFSVEILVDG
HWIEKQWKDV SVGDFIRIDN DSLFPADLLL LASSEQQGMA YIETSNLDGE TNLKIKQALD
ITSTMTSPEK LSQFESEITC EPPSRHVNEF NGNIEINGVA RHFGIDQLLL RGARLKNTAW
IFGAVIYTGH DSKLLMNSKR APLKSGTIDV QTNYRIIFLF FVLVALALIS ATGSEIWRGN
NIPQAWYLSF LEHDPKGSFL WGVLTFFILY NNLIPISLQV TLEVVRFFQA IYINNDIEMY
DVNSDSCAIA RTSNLNEELG QVKFIMSDKT GTLTRNVMKF KRLSIGSRNY GNNEDDEFAD
ASLIEDYRQG DEHSTSILEV LKMMAVCHTV VPENKDGQLI YQSSSPDEAA LVRGAASQSV
SFHTRQPQKV ICNVFGEDET IEILDVIDFT SDRKRMSVIV RDGAGGDIKL YTKGADTVIF
ERLEHGKEQE EAVEYCTEHL EDYASFGYRT LCFSMRHLTE QEYSQWAPEY KKAILAIDNR
AKLLADAAEK LERNMILVGA TAIEDKLQEW VPETIQALMA ADIRVWMLTG DKRETAINIA
HSCALCHTNT ELLIVDKTTY EETYQKLEQF VARAIELEKQ EKGFAMVIDG KSLLHALTGE
ARKHFGDLAL RCHAVVCCRM SPMQKAEVVE MVRKLAKHVV LAIGDGANDV AMIQAANVGV
GISGEEGLQA ASASDYAIPR FHFLRRLLLV HGAWNHDRSV KVILYSFYKN ICLYIIELWF
AMFSAWSGQT IFERWTIGMF NVIFTAWPPV VLGLFDHPVP AEQIMKYPAL YASFQNRAFS
IGNFSLWIGL AIVHSLSLFF LTYATMEHQV VWDNGLTGGW LMLGNCAYTF VVATVCFKAL
LECDSWTWPV VVACIGSIGL WIVFVIVYSL VFPHIGGIGA DMAGMAAIMM SSYTFWLALL
FIPLATLLWD LVIKSLFTIA MPTPRELAVM YNKRTTSFNG FERLASYSSN VLENMRLLTS
SLRGSTTGST RSRTASEASL ALAEQTRYGF AFSQDESSAV AQTELIRNVD STREKPTGR
