ID A0A5F9DHC6_RABIT Unreviewed; 1184 AA.
AC A0A5F9DHC6;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000045210.1, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000045210.1, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000045210.1,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000045210.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000045210.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOCUP00000045210.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000045210.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme
CC that catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium out of the cell. By regulating sperm cell calcium homeostasis,
CC may play a role in sperm motility. {ECO:0000256|ARBA:ARBA00054883}.
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00048694,
CC ECO:0000256|RuleBase:RU361146};
CC -!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
CC Interacts with calmodulin. {ECO:0000256|ARBA:ARBA00062373}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000256|ARBA:ARBA00060429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00060429}. Membrane
CC {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
CC ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR EMBL; AAGW02025362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A5F9DHC6; -.
DR Ensembl; ENSOCUT00000036364.1; ENSOCUP00000045210.1; ENSOCUG00000002381.4.
DR GeneTree; ENSGT00940000154527; -.
DR Proteomes; UP000001811; Chromosome 16.
DR Bgee; ENSOCUG00000002381; Expressed in uterus and 16 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0036126; C:sperm flagellum; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0030165; F:PDZ domain binding; IEA:TreeGrafter.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:UniProtKB-ARBA.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:TreeGrafter.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR FunFam; 1.20.1110.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000002; Calcium-transporting ATPase; 1.
DR FunFam; 1.20.1110.10:FF:000008; Calcium-transporting ATPase; 1.
DR FunFam; 2.70.150.10:FF:000001; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000022; Calcium-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000144; copper-transporting ATPase 1 isoform X2; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR022141; ATP_Ca_trans_C.
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; IPR059000; ATPase_P-type_domA.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093:SF435; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 4; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Flagellum {ECO:0000256|ARBA:ARBA00022846};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 93..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 364..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 405..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 918..935
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 955..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 984..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 58..112
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 184..282
FT /note="P-type ATPase A"
FT /evidence="ECO:0000259|Pfam:PF00122"
FT DOMAIN 866..1008
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT DOMAIN 1051..1066
FT /note="Plasma membrane calcium transporting P-type ATPase
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12424"
FT REGION 44..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1153
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 129731 MW; 6E9C8FB3FCCA5D59 CRC64;
QEAWSHHTDS RSWVKAGLRQ AAHSFISVTT TSYIAKTSQS GQGAVYAPTN HSLPPSPSSS
AGLSGNPTDL EKRRQVFGQN LIPPKKPKTF LELMWEAQGV TLIILEMAVI ISLVLSFYRP
PGGENELCGQ IAQSAEDEGE AEAGWIEGAA ILFSVIIVVL VTAFNDWSKE KQFRGLQSRI
EQEQKFSVIR NGQLIQLPVA DIVVGDIAQI KYGDLLPADG VLIQGNDLKI DESSLMGQSY
HVPKSLDKDP MLLSGTHVME GSGRMVVTAV GVNSQAGIIF TLLGASEDDE EEKKKKGKKQ
GVPENHNKAK TQDGVALEIQ PLNSQEGADN EDKDKKASKV HKKEKSVLQG KLTRLAVQIG
KAGLIMSAVT VVILILYFVI DNFVIQGRPW LAECTPVYIQ YFVKFFIIGV TVLVVAVPEG
LPLAVTISLA YSVKKMMKDN ILVRHLDACE TMGNATAICS DKTGTLTMNR MTVVQAYVGG
THYHQVPSPN VFLPKVLDLI INGIAINSAY TSKILPPEKE GGLPRQVGNK TECALLGFVA
DLKQDYQAVR NEVSEEQLYK VYTFNSVRKS MSTVVRKPAG GFRMYSKGAS EIMLRKCNRI
LDKKGEAVPF KNKDRDDMVR SVIEPMACEG LRTICIAYRD FNNAEPSWDN ESQVLTELTC
IAVVGIEDPV RPEVPEAIAK CKRAGITVRM VTGDNVNTAR AIATKCGILT PGDDFLCLEG
GFACLAEPRC VWRWQVEQEK LDKIWPKLRV LARSSPTDKH TLVKGIIDST VGDQRQVVAV
TGDGTNDGPA LKKADVGFAM GIAGTDVAKE ASDIILTDDN FTSIVKAVMW GRNVYDSISK
FLQFQLTVNV VAVIVAFTGA CITQDSPLKA VQMLWVNLIM DTFASLALAT EPPTDALLRR
RPYGRNKPLI SRTMMKNILG HAVYQLTIIF FLVFAGEKFF HIDSGRKAPL HSPPSQHYTI
VFNTFVLMQL FNEINSRKIH GERNVFAGIY HNLIFCSVVL GTFISQIISA IPTQSLKFLK
EAGHGTTKEE ISKDAEGLDE IDHAEMELRR GQILWFRGLN RIQTQVLRSW SLLAPGEDTT
PCWERVAGGR PSKLALQLAQ RGPRCGPPPS RRKHPATHPA GPGLPRARRQ TGKWMRAGQG
SPAAALPSLE SSSQRGHPSG TRTGPWGCAR CPPQPPAAES VKCP
//
