AT133_MACFA
ID AT133_MACFA Reviewed; 1226 AA.
AC Q95JN5; A0A2K5X2G9; G7NYR4;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Polyamine-transporting ATPase 13A3;
DE AltName: Full=ATPase family homolog up-regulated in senescence cells 1;
DE AltName: Full=Putrescine transporting ATPase;
DE EC=7.6.2.16 {ECO:0000250|UniProtKB:Q9H7F0};
GN Name=ATP13A3; Synonyms=AFURS1; ORFNames=QtsA-14967;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-493.
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- FUNCTION: ATP-driven pump involved in endocytosis-dependent polyamine
CC transport. Uses ATP as an energy source to transfer polyamine precursor
CC putrescine from the endosomal compartment to the cytosol.
CC {ECO:0000250|UniProtKB:Q9H7F0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + putrescine(out) = ADP + H(+) + phosphate +
CC putrescine(in); Xref=Rhea:RHEA:29995, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:326268, ChEBI:CHEBI:456216; EC=7.6.2.16;
CC Evidence={ECO:0000250|UniProtKB:Q9H7F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29996;
CC Evidence={ECO:0000250|UniProtKB:Q9H7F0};
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9H7F0}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9H7F0};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9H7F0}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Mainly targeted to the recycling endosomes and to a
CC lesser extent to the early and late endosomes.
CC {ECO:0000250|UniProtKB:Q9H7F0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q95JN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95JN5-2; Sequence=VSP_061098, VSP_061099, VSP_061100;
CC Name=3;
CC IsoId=Q95JN5-3; Sequence=VSP_061100;
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB63091.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AQIA01037294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIA01037295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIA01037296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIA01037297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB070146; BAB63091.1; ALT_SEQ; mRNA.
DR RefSeq; XP_005545411.1; XM_005545354.2. [Q95JN5-3]
DR RefSeq; XP_005545412.1; XM_005545355.2. [Q95JN5-3]
DR RefSeq; XP_005545415.1; XM_005545358.2. [Q95JN5-1]
DR RefSeq; XP_015300393.1; XM_015444907.1. [Q95JN5-3]
DR RefSeq; XP_015300394.1; XM_015444908.1. [Q95JN5-3]
DR RefSeq; XP_015300395.1; XM_015444909.1. [Q95JN5-3]
DR RefSeq; XP_015300396.1; XM_015444910.1. [Q95JN5-3]
DR RefSeq; XP_015300397.1; XM_015444911.1. [Q95JN5-1]
DR AlphaFoldDB; Q95JN5; -.
DR SMR; Q95JN5; -.
DR STRING; 9541.XP_005545411.1; -.
DR Ensembl; ENSMFAT00000017930; ENSMFAP00000043640; ENSMFAG00000039232. [Q95JN5-3]
DR GeneID; 102142290; -.
DR KEGG; mcf:102142290; -.
DR CTD; 79572; -.
DR VEuPathDB; HostDB:ENSMFAG00000039232; -.
DR eggNOG; KOG0208; Eukaryota.
DR GeneTree; ENSGT00940000155941; -.
DR OMA; GFKFYED; -.
DR OrthoDB; 172453at2759; -.
DR Proteomes; UP000233100; Chromosome 2.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0015594; F:ABC-type putrescine transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF12409; P5-ATPase; 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; TIGR01494; ATPase_P-type; 3.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Endosome; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1226
FT /note="Polyamine-transporting ATPase 13A3"
FT /id="PRO_0000046426"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT INTRAMEM 29..49
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TOPO_DOM 50..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..232
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..448
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..940
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 962
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..999
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 1000..1020
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1021..1073
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 1074..1094
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1095..1105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1143
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT ACT_SITE 498
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT BINDING 498..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 750
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 883..887
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7F0"
FT VAR_SEQ 161..187
FT /note="Missing (in isoform 2)"
FT /id="VSP_061098"
FT VAR_SEQ 616..619
FT /note="AIYE -> VSEECLL (in isoform 2)"
FT /id="VSP_061099"
FT VAR_SEQ 1161
FT /note="E -> ENFFLDMVLWKVVFNRDKQGEYRFSTTQPPQ (in isoform 2
FT and isoform 3)"
FT /id="VSP_061100"
SQ SEQUENCE 1226 AA; 137807 MW; 009AA7B13D92D565 CRC64;
MDKEERKIIN QGQEDEMEIY GYNLSRWKLA IVSLGVICTG GFLLLLLYWM PEWRVKATCV
RAAIKDCDVV LLRTTDEFKM WFCAKIRVLS LETHPISSPK SMSNKLSNGH AVCLTENPTG
ENRHGISKYS QAESQQIRYF THHSVKYFWN DTIHNFDFLK GLDEGVSCTS IYEKHSAGLT
KGMHAYRKLL YGVNEIAVKV PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYALAIVV
MSIVSIVSSL YSIRKQYVML HDMVATHSTV RVSVCRVNEE IEEIFSTDLV PGDVMVIPLN
GTIMPCDAVL INGTCIVNES MLTGESVPVT KTNLPNPSVD VKGIGDELYN PETHKRHTLF
CGTTVIQTRF YTGELVKAIV VRTGFSTSKG QLVRSILYPK PTDFKLYRDA YLFLLCLVAV
AGIGFIYTII NSILNEVQVG VIIIESLDII TITVPPALPA AMTAGIVYAQ RRLKKIGIFC
ISPQRINICG QLNLVCFDKT GTLTEDGLDL WGIQRVENAR FLSPEENVCN EMLVKSQFVA
CLATCHSLTK IEGVLSGDPL DLKMFEAIGW ILEEATEEET ALHNRIMPTV VRPPKQLLPE
STPAGNQEME LFELPAIYEI GIVRQFPFSS ALQRMSVVAR VLGDKKMDAY MKGAPEVIAS
LCKPETVPVD FQNVLEDFTK QGFRVIALAH RKLESKLTWH KVQNISRDAI ENNMDFMGLI
IMQNKLKQET PAVLEDLHKA NIRTVMVTGD NMLTAVSVAR DCGMILPQDK VIIAEALPPK
DGKVAKINWH YADSLTQCSH PSAIASEATP VKLVHDSLED LQMTRYHFAM NGKSFSVILE
HFQDLVPKLM LHGTVFARMA PDQKTQLIEA LQNVDYFVGM CGDGANDCGA LKRAHGGISL
SELEASVASP FTSKTPSISC VPNLIREGRA ALITSFCVFK FMALYSIIQY FSVTLLYSIL
SNLGDFQFLF IDLAIILVVV FTMSLNPAWK ELVAQRPPSG LISGALLFSV LSQIIICIGF
QSLGFFWVKQ QPWYEVWHPK SDACNATGSL LWNSSHLDNE TELDEHNIQN YENTTVFFIS
SFQYLIVAIA FSKGKPFRQP CYKNYFFVFS VIFLYVFILF IMLYPVASVD QVLQIVCVPY
QWRVTMLIIV LVNAFVSITV EESVDRWRKC CLPWALSCGK KIPKAKYMYL AQELLVDPEW
PPKPQTTTEA KGLVKENGSC QIITIT
