CATP5_CAEEL
ID CATP5_CAEEL Reviewed; 1203 AA.
AC Q21286; Q10461; Q65ZI7; Q65ZI8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cation-transporting ATPase catp-5 {ECO:0000312|WormBase:K07E3.7b};
DE EC=7.2.2.-;
GN Name=catp-5 {ECO:0000303|PubMed:19762559, ECO:0000312|WormBase:K07E3.7b};
GN ORFNames=K07E3.7 {ECO:0000312|WormBase:K07E3.7b};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19762559; DOI=10.1096/fj.09-135889;
RA Heinick A., Urban K., Roth S., Spies D., Nunes F., Phanstiel O. IV,
RA Liebau E., Lueersen K.;
RT "Caenorhabditis elegans P5B-type ATPase CATP-5 operates in polyamine
RT transport and is crucial for norspermidine-mediated suppression of RNA
RT interference.";
RL FASEB J. 24:206-217(2010).
CC -!- FUNCTION: Involved in the uptake and/or transport of polyamines,
CC probably through ATP hydrolysis. This contributes to the maintenance of
CC intracellular polyamine levels. Polyamines are essential for cell
CC proliferation and are implicated in cellular processes, ranging from
CC DNA replication to apoptosis. {ECO:0000269|PubMed:19762559}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:19762559}; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:K07E3.7b};
CC IsoId=Q21286-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:K07E3.7a};
CC IsoId=Q21286-2; Sequence=VSP_012458;
CC -!- TISSUE SPECIFICITY: Expressed in the 20 intestinal cells and in the
CC excretory cell. {ECO:0000269|PubMed:19762559}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryos, but expressed at all
CC larval stages of development and in adults.
CC {ECO:0000269|PubMed:19762559}.
CC -!- DISRUPTION PHENOTYPE: Disrupts the polyamine uptake and/or transport of
CC the polyamine conjugate Ant-4,4 and norspermidine, a toxic structural
CC analog of the polyamine spermidine. Intracellular levels of the natural
CC polyamines spermidine and putrescine are as wild-type. Double knockout
CC with either odc-1 or smd-1 (two enzymes involved in polyamine
CC synthesis) results in a reduced brood size, delayed postembryonic
CC development and reduced intracellular levels of spermidine. Double
CC knockout with odc-1 results in reduced levels of the polyamine
CC putrescine, while double knockout with smd-1 results in increased
CC accumulation of putrescine. {ECO:0000269|PubMed:19762559}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; FO080274; CCD62517.1; -; Genomic_DNA.
DR EMBL; FO080274; CCD62518.1; -; Genomic_DNA.
DR PIR; A89583; A89583.
DR RefSeq; NP_001024767.1; NM_001029596.2.
DR RefSeq; NP_001024768.1; NM_001029597.1.
DR AlphaFoldDB; Q21286; -.
DR SMR; Q21286; -.
DR STRING; 6239.K07E3.7b; -.
DR iPTMnet; Q21286; -.
DR EPD; Q21286; -.
DR PaxDb; Q21286; -.
DR PeptideAtlas; Q21286; -.
DR PRIDE; Q21286; -.
DR EnsemblMetazoa; K07E3.7a.1; K07E3.7a.1; WBGene00019493. [Q21286-2]
DR EnsemblMetazoa; K07E3.7a.2; K07E3.7a.2; WBGene00019493. [Q21286-2]
DR EnsemblMetazoa; K07E3.7a.3; K07E3.7a.3; WBGene00019493. [Q21286-2]
DR EnsemblMetazoa; K07E3.7a.4; K07E3.7a.4; WBGene00019493. [Q21286-2]
DR GeneID; 181067; -.
DR CTD; 181067; -.
DR WormBase; K07E3.7a; CE37253; WBGene00019493; catp-5. [Q21286-2]
DR WormBase; K07E3.7b; CE37254; WBGene00019493; catp-5. [Q21286-1]
DR eggNOG; KOG0208; Eukaryota.
DR InParanoid; Q21286; -.
DR OMA; DIMESEL; -.
DR OrthoDB; 172453at2759; -.
DR PhylomeDB; Q21286; -.
DR Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q21286; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00019493; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q21286; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015417; F:ABC-type polyamine transporter activity; 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:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015203; F:polyamine transmembrane transporter activity; IMP:WormBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:1902047; P:polyamine transmembrane transport; IMP:WormBase.
DR GO; GO:0055085; P:transmembrane transport; 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; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
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; Cell membrane; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1203
FT /note="Cation-transporting ATPase catp-5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000046356"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..962
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..1007
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1046
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1047..1067
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1068..1085
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1086..1106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1107..1120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1142..1203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 21..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 503
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 887
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_012458"
SQ SEQUENCE 1203 AA; 134704 MW; 474DAF607FF8BFA0 CRC64;
MNTSEREPLL DTTTRNRVYD TTDNPSTKIM KREKDNPKAK TTSFNQGKLN IGEETCDLYA
YKETIGRQIL FWLLTIVTLG FYQLLAYWVK SLFVKVRFQP TSHDECEYVM VEDIHGTQTI
KEVFKAESDV GLARPTRSGK QEKVKVMRFF TYRKIKYIWY EKDQEWLNPA DMDSAAPFNI
YQKLTLDVIG LKEQDVIASR KIYNMNALAL ALTPILVILF KEVLGPFYLF QCFSVALWYS
DNYAYYASVI VIITVGSAAV AVYQMRAQEK RIRNMVGDTI SVIVRRDGHD ITIDASEIVP
MDILILPSNT FILPCDCLLM NGTVIVNEAM LTGESVPVTK ASLKEADECG PEIRLSSEHN
RHTLFSGTTV LQTRNYKGQP VMARVIRTGF STLKGQLVRS IMYPKPQEKE ALKDVMVFIL
VLGFIALIGF IYTVIEMVSR GESLKHIIIR SLDIITIVVP PALPAAMSVG IINANSRLKK
KKIFCTSPTT VNVCGLINVA CFDKTGTLTE DGLDFNCLKA IRKNEDGKPE FTSEFEELDP
VKLSAENANL NIVVAAASCH SLTRIDGTLH GDPLELILVE KSKWIIEEAV NSDEETQDFD
TVQPTVLRPP PEQATYHPEN NEYSVIKQHP FNSALQRMSV IISTPSEHSA HDMMVFTKGS
PEMIASLCIP DTIPEDYMEV VDEYAQRGFR LIAVASKAVH LNFAKALKTP RDIMESELEF
LGLIVMENRL KDVTLSVINE LSVANIRCVM VTGDNLLTAM SVARECGIIR PTKKAFLITH
SKTEKDPLGR TKLFIKESVS SSENDIDTDS EVRAFDRKAV LRTATYQMAI AGPTYSVITH
EYPELVDRIT AMCDVYARMA PDQKAQLIGA LQEIGAKVSM CGDGANDCAA LKAAHAGISL
SQAEASIAAP FTSNVPDIRC VPTVIKEGRC ALVTSYAVSK YMAAYSLNEF LSVMLLYNDG
TNISDGQFLY IDLVLITLVA LFLGNTEASR KLSGIPPPRR LATSAFYFSV FGQMFFNIIT
QTTGYLLVRG QSWYVPNPEE LDNTTTMIGT TVFFTSCCMY LGYAFVYSKG HPYRRSVFTN
WLLCGIIFVI GAINMVMIFT NMGFLMNLMG FVYVPSTSMR FILLAISLAG VFLSLLYEHF
FVEKVVAIHF ESYLRQRRLR NGDPSLSAYE KILAAIGSSP RWFEDEINLS KSIDRKETIE
SKC
