ATC_ARTSF
ID ATC_ARTSF Reviewed; 1003 AA.
AC P35316;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type;
DE EC=7.2.2.10;
DE AltName: Full=Calcium pump;
OS Artemia franciscana (Brine shrimp) (Artemia sanfranciscana).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Anostraca; Artemiidae; Artemia.
OX NCBI_TaxID=6661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2533270; DOI=10.1016/0022-2836(89)90106-x;
RA Palmero I., Sastre L.;
RT "Complementary DNA cloning of a protein highly homologous to mammalian
RT sarcoplasmic reticulum Ca-ATPase from the crustacean Artemia.";
RL J. Mol. Biol. 210:737-748(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-1003.
RC TISSUE=Embryo;
RX PubMed=8314776; DOI=10.1016/s0021-9258(19)85212-2;
RA Escalante R., Sastre L.;
RT "Similar alternative splicing events generate two sarcoplasmic or
RT endoplasmic reticulum Ca-ATPase isoforms in the crustacean Artemia
RT franciscana and in vertebrates.";
RL J. Biol. Chem. 268:14090-14095(1993).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of the calcium.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
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 -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35316-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35316-2; Sequence=VSP_000412;
CC -!- DEVELOPMENTAL STAGE: Isoform 2 (long form) is expressed only in early
CC stages of embryonic development (cysts), while isoform 1 (short form)
CC is also found in later embryonic stages and adults.
CC -!- MISCELLANEOUS: [Isoform 2]: Presents an extension, a potential
CC transmembrane domain, which may have an important functional role.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; X51674; CAA35980.1; -; mRNA.
DR EMBL; X72713; CAA51262.1; -; Genomic_DNA.
DR PIR; S07526; S07526.
DR PIR; S32230; S32230.
DR AlphaFoldDB; P35316; -.
DR SMR; P35316; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; IPR005782; P-type_ATPase_IIA.
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 SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Ion transport; Magnesium; Membrane; Nucleotide-binding; Phosphoprotein;
KW Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1003
FT /note="Calcium-transporting ATPase sarcoplasmic/endoplasmic
FT reticulum type"
FT /id="PRO_0000046226"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 776..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..840
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 841..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 864..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..917
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 918..934
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 955..1003
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 354
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 998..1003
FT /note="EFSFIK -> GMPLSSYFVDAWGLVLAWALFFGVIFYSPL (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000412"
FT CONFLICT 481
FT /note="T -> A (in Ref. 2; CAA51262)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="P -> Q (in Ref. 2; CAA51262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 110344 MW; 908A036A19FAF03E CRC64;
MEDAHAKKWE EVVDYFGVDP ERGLALEQVK KNQEKYGPNE LPAEEGKSLL TLILEQFDDL
LVKILLLAAI ISLVLALFEE HDDEAEQLTA YVEPFVILLI LIANAVVGVW QEKNAESAIE
ALKEYEPEMG KVIRADKTGI QKIKARDLVP GDIVEISVGD KIPADLRLIS ILSTTLRIDQ
SILTGESVSV IKHTDPVPDP RAVNQDKKNM LFSGTNVSAG KARGVVMGTG LNTAIGSIRT
QMFETEEMKT PLQQKLDEFG EQLSKVISVI CVAVWAINIG HFNDPAHGGS WIKGAIYYFK
IAVALAVAAI PEGLPAVITT CLALGTRRMA KKNAIVRSLP SVETLGCTSV ICSDKTGTLT
TNQMSVSRMF VFKDIPDDAA PELYQFELTG STYEPIGETF MQGQKINAAD YDAVKEITTI
CMMCNDSAID FNEYKQAFEK VGEATETALI VLGEKLNPYN LSKAGKDRRS AALVVREDMD
TRWKKEFTLE FSRDRKSMSS YCVPLKAGLL SNGPKMFVKG APEGVLDRCT HVRVGTKKVP
MTPAIMDKIL EVTRAYGTGR DTLRCLALAT IDDPMDPKDM DIIDSTKFVK YEQNCTFVGV
VGMLDPPRKE VLDAIERCRA AGIRVIVITG DNKATAEAIC RRIGVFGEDE NTEGMAYTGR
EFDDLSVEGQ RDAVARSRLF ARVEPFHKSK IVEYLQGMGE ISAMTGDGVN DAPALKKAEI
GIAMGSGTAV AKSAAEMVLA DDNFSTIVAA VEEGRAIYNN MKQFIRYLIS SNIGEVVSIF
LTAALGLPEA LIPVQLLWVN LVTDGLPATA LGFNPPDLDI MNKPPRRADE GLITGWLFFR
YMAIGTYVGA ATVGAAAHWF MMSPTGPGLN FYQLSHHLQC TPENEYFEGI DCEIFSDPHP
MTMALSVLVT IEMLNAINSL SENQSLLVMP PWSNIWLISA ICLSMTLHFV ILYVEILSTV
FQICPLTLTE WIVVLKISFP VLLLDEVLKF VARKYTDEFS FIK
