ID AT131_CAEEL Reviewed; 1178 AA.
AC P90747; O02620;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 3.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Probable manganese-transporting ATPase catp-8 {ECO:0000305};
DE EC=7.2.2.-;
DE AltName: Full=Cation transporting ATPase 8 {ECO:0000312|WormBase:C10C6.6};
GN Name=catp-8 {ECO:0000312|WormBase:C10C6.6};
GN ORFNames=C10C6.6 {ECO:0000312|WormBase:C10C6.6};
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).
CC -!- FUNCTION: Mediates manganese transport into the endoplasmic reticulum.
CC The ATPase activity is required for cellular manganese homeostasis.
CC {ECO:0000250|UniProtKB:Q9HD20}.
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: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9HD20}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9HD20}.
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; Z83217; CAB05683.2; -; Genomic_DNA.
DR PIR; T19187; T19187.
DR RefSeq; NP_502165.2; NM_069764.5.
DR AlphaFoldDB; P90747; -.
DR SMR; P90747; -.
DR BioGRID; 43167; 5.
DR IntAct; P90747; 1.
DR STRING; 6239.C10C6.6.1; -.
DR EPD; P90747; -.
DR PaxDb; 6239-C10C6-6; -.
DR PeptideAtlas; P90747; -.
DR EnsemblMetazoa; C10C6.6.1; C10C6.6.1; WBGene00007514.
DR GeneID; 178070; -.
DR KEGG; cel:CELE_C10C6.6; -.
DR UCSC; C10C6.6; c. elegans.
DR AGR; WB:WBGene00007514; -.
DR WormBase; C10C6.6; CE30858; WBGene00007514; catp-8.
DR eggNOG; KOG0209; Eukaryota.
DR GeneTree; ENSGT00550000075064; -.
DR HOGENOM; CLU_001828_4_1_1; -.
DR InParanoid; P90747; -.
DR OMA; QKTKYVW; -.
DR OrthoDB; 6047at2759; -.
DR PhylomeDB; P90747; -.
DR Reactome; R-CEL-936837; Ion transport by P-type ATPases.
DR PRO; PR:P90747; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007514; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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 monoatomic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0140318; F:protein transporter activity; ISS:WormBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:WormBase.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd07543; P-type_ATPase_cation; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR047820; P5A-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endoplasmic reticulum; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1178
FT /note="Probable manganese-transporting ATPase catp-8"
FT /evidence="ECO:0000305"
FT /id="PRO_0000046357"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..970
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 991..997
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 998..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1015..1032
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1056
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1057..1076
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1077..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1100..1110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1131..1147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1148..1170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1171..1178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 868..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 822
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 826
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1178 AA; 131973 MW; 8394E3E368BE0488 CRC64;
MGVDQLVETI IPYNLRSIAT HLYVPPFTII TAIWTYVWLN IFGYEEYYEL GMLGYAAIFV
ILALVLLFCH WMMPVRCFLM CSKQEDVRIA SHVCVIPTQN NGWPELVKLM RTTRDKQTKL
WFEFQRVHYT WDEESREFQT KTLDTAKPMV FFQKSHGFEV EEHVKDAKYL LGDNKTEMIV
PQFLEMFIER ATAPFFVFQV FCVGLWCLED MWYYSLFTLF MLMTFEATLV KQQMKNMSEI
RNMGNKTYMI NVLRGKKWQK IKIEELVAGD IVSIGRGAEE ECVPCDLLLL RGPCIVDESM
LTGESVPQMK EPIEDVEKDK IFDIETDSRL HVIFGGTKIV QHTAPGKAAE GMVKSPDGNC
ICYVIRTGFN TSQGKLLRTI MFGVKKATAN NLETFCFILF LLIFAIAAAA YLWIKGSVDE
TRSKYKLFLE CTLILTSVIP PELPIELSLA VNSSLMALQK LGIFCTEPFR IPFAGKVDIC
CFDKTGTLTT DNLVVEGVAL NNQKEGMIRN AEDLPHESLQ VLASCHSLVR FEEDLVGDPL
EKACLSWCGW NLTKGDAVMP PKTAAKGISG IKIFHRYHFS SAMKRMTVVA GYQSPGTSDT
TFIVAVKGAP EVLRNMYADL PSDYDETYTR LTRQGSRVLA MGIRKLGETR VGELRDKKRE
NFENDLAFAG FVVISCPLKS DTKTMIREIM DSSHVVAMIT GDNPLTACHV SKVLKFTKKS
LPTLVLDEPA DGVDWMWKSV DGTIELPLKP ETKNKMERKA FFNSHEFCLT GSAFHHLVHN
EHTFLRELIL HVKVFARMAP KQKERIINEL KSLGKVTLMC GDGTNDVGAL KHANVGVALL
TNPYDAEKAA EKEKEKKAKI EEARSLVRSG AQLPQRPGAP GAPPAANAAR RDAPPGARAR
APLPPMANAA QARLDNLMKE LEEEEKAQVI KLGDASIAAP FTSKYTSIAS ICHVIKQGRC
TLVTTLQMFK ILALNALVSA YSLSALYLDG VKFSDTQATI QGLLLAACFL FISKSKPLKT
LSRQRPMANI FNAYTLLTVT LQFIVHFSCL LYIVGLAHEA NTEKAPVDLE AKFTPNILNT
TVYIISMALQ VCTFAVNYRG RPFMESLFEN KAMLYSIMFS GGAVFTLASG QATDLMIQFE
LVVLPEALRN ALLMCVTADL VICYIIDRGL NFLLGDMF
//
