TAT5_CAEEL
ID TAT5_CAEEL Reviewed; 1074 AA.
AC G5EBH1; G5EE81; G5EGE0;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable phospholipid-transporting ATPase tat-5;
DE EC=7.6.2.1 {ECO:0000305|PubMed:30213940};
GN Name=tat-5; ORFNames=F36H2.1;
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] (ISOFORMS 1; 2 AND 3).
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, AND SUBCELLULAR LOCATION.
RX PubMed=22100064; DOI=10.1016/j.cub.2011.10.040;
RA Wehman A.M., Poggioli C., Schweinsberg P., Grant B.D., Nance J.;
RT "The P4-ATPase TAT-5 inhibits the budding of extracellular vesicles in C.
RT elegans embryos.";
RL Curr. Biol. 21:1951-1959(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-246.
RX PubMed=30213940; DOI=10.1038/s41467-018-06114-3;
RA McGough I.J., de Groot R.E.A., Jellett A.P., Betist M.C., Varandas K.C.,
RA Danson C.M., Heesom K.J., Korswagen H.C., Cullen P.J.;
RT "SNX3-retromer requires an evolutionary conserved MON2:DOPEY2:ATP9A complex
RT to mediate Wntless sorting and Wnt secretion.";
RL Nat. Commun. 9:3737-3737(2018).
CC -!- FUNCTION: Plays a role in regulating membrane trafficking of cargo
CC proteins during embryogenesis (PubMed:22100064, PubMed:30213940).
CC Regulates snx-3 retromer-mediated endosomal sorting of mig-14, a
CC transporter of Wnt egl-20 morphogen (PubMed:30213940). Together with
CC mon-2 and pad-1, may participate in the formation of endosomal carriers
CC that direct mig-14 trafficking back to Golgi, away from lysosomal
CC degradation. Required for Wnt egl-20 gradient formation along the
CC anteroposterior body axis and migration of QL neuroblast descendants
CC toward the posterior part (PubMed:30213940). Maintains
CC phosphatidylethanolamine (PE) asymmetry at the plasma membrane and
CC prevents the budding of ectosome vesicles that affect intercellular
CC communication and morphogenesis (PubMed:22100064).
CC {ECO:0000269|PubMed:22100064, ECO:0000269|PubMed:30213940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000305|PubMed:30213940};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22100064};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=G5EBH1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G5EBH1-2; Sequence=VSP_060963;
CC Name=3;
CC IsoId=G5EBH1-3; Sequence=VSP_060964;
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing.
CC {ECO:0000305}.
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; BX284601; CAB03079.2; -; Genomic_DNA.
DR EMBL; BX284601; CAD92377.2; -; Genomic_DNA.
DR EMBL; BX284601; CAJ43906.1; -; Genomic_DNA.
DR PIR; T21891; T21891.
DR RefSeq; NP_001021457.1; NM_001026286.3. [G5EBH1-1]
DR RefSeq; NP_001021458.1; NM_001026287.4. [G5EBH1-2]
DR RefSeq; NP_001040665.1; NM_001047200.2. [G5EBH1-3]
DR AlphaFoldDB; G5EBH1; -.
DR SMR; G5EBH1; -.
DR STRING; 6239.F36H2.1a; -.
DR EPD; G5EBH1; -.
DR PaxDb; G5EBH1; -.
DR PeptideAtlas; G5EBH1; -.
DR EnsemblMetazoa; F36H2.1a.1; F36H2.1a.1; WBGene00009498. [G5EBH1-1]
DR EnsemblMetazoa; F36H2.1b.1; F36H2.1b.1; WBGene00009498. [G5EBH1-2]
DR EnsemblMetazoa; F36H2.1c.1; F36H2.1c.1; WBGene00009498. [G5EBH1-3]
DR GeneID; 172748; -.
DR KEGG; cel:CELE_F36H2.1; -.
DR CTD; 172748; -.
DR WormBase; F36H2.1a; CE34183; WBGene00009498; tat-5.
DR WormBase; F36H2.1b; CE53504; WBGene00009498; tat-5.
DR WormBase; F36H2.1c; CE39367; WBGene00009498; tat-5.
DR eggNOG; KOG0210; Eukaryota.
DR GeneTree; ENSGT00940000168130; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; G5EBH1; -.
DR OMA; IAITTWH; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; G5EBH1; -.
DR BRENDA; 7.6.2.1; 1045.
DR Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009498; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5EBH1; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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 promoter usage; Alternative splicing; ATP-binding;
KW Cell membrane; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1074
FT /note="Probable phospholipid-transporting ATPase tat-5"
FT /id="PRO_0000452344"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..906
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 954..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 813
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 817
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT VAR_SEQ 1..70
FT /note="MGKRKKNDESSSSSSQKPCVSSSSDDFSVSFVRAEEDDVATTIRDKTASLKS
FT NATHFSAASAAKGGMFDF -> MRYSRLATSHEEADEYSRLLPMPDSEIGIEGSDDVYL
FT LPSVSSTSSSTFSMT (in isoform 2)"
FT /id="VSP_060963"
FT VAR_SEQ 68..71
FT /note="FDFR -> L (in isoform 3)"
FT /id="VSP_060964"
FT MUTAGEN 246
FT /note="E->Q: Causes aberrant migration of QL neuroblast
FT descendants toward the anterior part."
FT /evidence="ECO:0000269|PubMed:30213940"
SQ SEQUENCE 1074 AA; 120345 MW; 02F2708BA0E44C26 CRC64;
MGKRKKNDES SSSSSQKPCV SSSSDDFSVS FVRAEEDDVA TTIRDKTASL KSNATHFSAA
SAAKGGMFDF RCCRSLFSRR RVLHSRTVRV GYGPVGHDAN VTFTPNTVCN QKYNIFSFVP
IVLFQQFKFF LNLYFLLMAC SQFIPAIQIG APITYWGPLG FVLTITLIRE AFDDFVRYLR
DRDLNSEKYE KLTRDGTRIE IRSADIEVGD VIIMHKDRRV PADVVLLRTT DKSGACFIRT
DQLDGETDWK LRIPVPHTQH LPNEADIMEL NCEVYAEKPQ KDIHAFVGTL KITDDDNVQD
GSLNVENVLW ANTVVASGTA VGIVVYTGRE TRSVMNTTLP ESKVGLLDLE VNNLTKLLFC
FVLVLSSVMV AMKGLDNLWY RYLMRFILLF SYIIPISLRV NLDMAKLFYS WQIGRDKHIP
ETVIRSSTIP EELGRISFLL SDKTGTLTKN EMHFKKIHLG TVAFSSDAFE EVGQHVRSAY
AGRLAKHSFS AKLQNAVEAI ALCHNVTPIF ENGEISYQAA SPDEVALVKW TETVGVRLAS
RDLHAMSLSV QLPNGQTLMK QFQILYVFPF TSETKRMGII VKDETTDEVT LLMKGADTVM
SGMVQYNDWL DEECSNMARE GLRTLVVARK PLSQAELEAF DRAYHAAKMS ISDRSQNMAN
VVNRMLERDL QLLCLTGVED RLQDQVTTSL ELLRNAGIKI WMLTGDKLET AICIAKSSGL
FSRSDNIHVF GNVHNRTDAH NELNNLRRKT DVALVMPGSA LNVCLQYYEA EVAELVCACT
AVVCCRCSPE QKAQIVQLLR KYRAPLRVAA IGDGGNDVSM IQAAHAGIGI DANEGKQASL
AADFSITQFS HVCRLLLVHG RFCYKRSCAL SQFVMHRGLI ISTMQAIFSC VFYFASVSLY
QGVLMVAYST CYTMLPVFSL VVDRDVTATN ALTYPELYKE LGKGRSLSYK TFCIWVLISL
YQGAVIMYGA LLVFDADFIH VVSISFSALI VTELIMVAMT VHTWHWAMLL AQALSLGLYM
ISLILFDQYF DRQFVLSWVF ISKTTAITAV SCLPLYIVKA LRRKFSPPSY AKVN
