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AT2A3_PIG
ID   AT2A3_PIG               Reviewed;         999 AA.
AC   O77696; A0A286ZW82; K9IW69;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 3;
DE            Short=SERCA3;
DE            Short=SR Ca(2+)-ATPase 3;
DE            EC=7.2.2.10;
DE   AltName: Full=Calcium pump 3;
GN   Name=ATP2A3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 773-907, AND TISSUE SPECIFICITY.
RC   TISSUE=Coronary artery;
RX   PubMed=10724327; DOI=10.1023/a:1007093516593;
RA   Khan I., Sandhu V., Misquitta C.M., Grover A.K.;
RT   "SERCA pump isoform expression in endothelium of veins and arteries: every
RT   endothelium is not the same.";
RL   Mol. Cell. Biochem. 203:11-15(2000).
RN   [2] {ECO:0000312|EMBL:JAA53532.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Dawson H.D., Chen C.T.;
RT   "Global Gene Expression Profiling of Alveolar Macrophages by Deep
RT   Sequencing.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000312|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:HDB02571.1}
RP   IDENTIFICATION.
RX   PubMed=30723633; DOI=10.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the transport of calcium. Transports calcium ions from
CC       the cytosol into the sarcoplasmic/endoplasmic reticulum lumen.
CC       Contributes to calcium sequestration involved in muscular
CC       excitation/contraction. {ECO:0000250|UniProtKB:Q93084}.
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         Evidence={ECO:0000250|UniProtKB:Q93084};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC         Evidence={ECO:0000250|UniProtKB:Q93084};
CC   -!- ACTIVITY REGULATION: Inhibited by sarcolipin (SLN), phospholamban (PLN)
CC       and myoregulin (MRLN) (By similarity). Enhanced by DWORF; DWORF
CC       increases activity by displacing sarcolipin (SLN), phospholamban (PLN)
CC       and myoregulin (MRLN) (By similarity). {ECO:0000250|UniProtKB:P04191,
CC       ECO:0000250|UniProtKB:Q8R429}.
CC   -!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity). Interacts
CC       with phospholamban (PLN) (By similarity). Interacts with myoregulin
CC       (MRLN). Interacts with DWORF (By similarity). Interacts VMP1 (By
CC       similarity). Interacts with TUNAR; the interaction occurs at low levels
CC       in low glucose conditions and is increased by high glucose levels (By
CC       similarity). {ECO:0000250|UniProtKB:P04191,
CC       ECO:0000250|UniProtKB:Q8R429, ECO:0000250|UniProtKB:Q93084}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q93084}. Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q93084}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q93084}.
CC   -!- TISSUE SPECIFICITY: Expressed in endothelial tissues.
CC       {ECO:0000269|PubMed:10724327}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000305}.
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DR   EMBL; AF084929; AAC33481.1; -; mRNA.
DR   EMBL; GACC01000275; JAA53532.1; -; mRNA.
DR   EMBL; AEMK02000082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQIR01197659; HDB53136.1; -; Transcribed_RNA.
DR   EMBL; DQIR01147094; HDB02571.1; -; Transcribed_RNA.
DR   EMBL; DQIR01162709; HDB18186.1; -; Transcribed_RNA.
DR   EMBL; DQIR01166546; HDB22023.1; -; Transcribed_RNA.
DR   AlphaFoldDB; O77696; -.
DR   SMR; O77696; -.
DR   STRING; 9823.ENSSSCP00000018933; -.
DR   PaxDb; O77696; -.
DR   Ensembl; ENSSSCT00000056237; ENSSSCP00000035943; ENSSSCG00000017874.
DR   Ensembl; ENSSSCT00055060309; ENSSSCP00055048321; ENSSSCG00055029890.
DR   VGNC; VGNC:85648; ATP2A3.
DR   eggNOG; KOG0202; Eukaryota.
DR   GeneTree; ENSGT00940000155668; -.
DR   InParanoid; O77696; -.
DR   OrthoDB; 100699at2759; -.
DR   Proteomes; UP000008227; Chromosome 12.
DR   Proteomes; UP000314985; Unplaced.
DR   Bgee; ENSSSCG00000017874; Expressed in blood and 42 other tissues.
DR   ExpressionAtlas; O77696; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR   GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
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   Acetylation; ATP-binding; Calcium; Calcium transport; Disulfide bond;
KW   Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..999
FT                   /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 3"
FT                   /id="PRO_0000046204"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        49..69
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        70..89
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        90..110
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        111..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        254..273
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        274..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        296..313
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        314..757
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        758..777
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        778..787
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        788..808
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        809..828
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        829..851
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        852..897
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        898..917
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        918..930
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        931..949
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        950..964
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        965..985
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   TOPO_DOM        986..999
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          370..400
FT                   /note="Interaction with phospholamban 1"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   REGION          788..808
FT                   /note="Interaction with phospholamban 2"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   ACT_SITE        351
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         305
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         307
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         309
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         351
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         353
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         703
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         768
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         771
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         796
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         799
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         800
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         800
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   BINDING         908
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93084"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64518"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64518"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64518"
FT   MOD_RES         415
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64518"
FT   MOD_RES         662
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93084"
FT   DISULFID        876..888
FT                   /evidence="ECO:0000250|UniProtKB:P11607"
FT   CONFLICT        205
FT                   /note="K -> E (in Ref. 2; JAA53532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        375
FT                   /note="G -> S (in Ref. 2; JAA53532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="D -> N (in Ref. 2; JAA53532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        585
FT                   /note="V -> A (in Ref. 2; JAA53532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        820
FT                   /note="R -> L (in Ref. 1; AAC33481)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        868
FT                   /note="Y -> H (in Ref. 1; AAC33481)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        884..886
FT                   /note="TGT -> AGI (in Ref. 1; AAC33481)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        907
FT                   /note="T -> I (in Ref. 1; AAC33481)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   999 AA;  109328 MW;  4D49EEE3510047E1 CRC64;
     MEEAHLLPAA DVLRRFSVTA EGGLSPAQVT RARERYGPNE LPTEEGKSLW ELVLEQFEDL
     LVRILLLAAL VSFVLACFEE GEETTTAFVE PLVIVLILVA NAVVGVWQER NAENAIEALK
     EYEPEMGKVI RSDRKGVQRI RARDIVPGDI VEVAVGDKVP ADLRLIEIKS TTLRVDQSIL
     TGESVSVTKH TDAIPDPRAV NQDKKNMLFS GTNIASGKAV GVAVATGLHT ELGKIRNQMA
     SVEPERTPLQ QKLDEFGRQL SRAISVICMA VWVINIGHFA DPAHGGSWLR GAVYYFKIAV
     ALAVAAIPEG LPAVITTCLA LGTRRMARKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
     MSVCRMFVVA EAEAGTCRLH EFTISGTTYA PEGEVRQGEQ PVRCGKFDGL VELATICALC
     NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTDLQ ALSRVERAGA CNAVIKQLMR
     KEFTLEFSRD RKSMSVYCTP TRPGLVAQGS KMFVKGAPES VIERCSSVRV GSRTVPLNTT
     SREQILAKVR DWGSGSDTLR CLALATRDAP PRKEAMQLDD CSKFVQYETD LTFVGCVGML
     DPPRPEVASC IARCRQAGIR VVMITGDNKG TAVAICRRLG ILEDTEDVVG KAYTGREFDD
     LSPEQQRHAC RTARCFARVE PAHKSRIVEN LQSFNEVTAM TGDGVNDAPA LKKAEIGIAM
     GSGTAVAKSA AEMVLSDDNF ASIVAAVEEG RAIYSNMKQF IRYLISSNVG EVVCIFLTAI
     LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKR PRNPREALIS GWLFFRYLAI
     GVYVGLATVA AATWWFLYDA EGPQVTFYQL RNFLKCSEDN PLFTGTDCEV FESRFPTTMA
     LSVLVTTEMC NALNSVSENQ SLLRMPPWLN PWLLAAVAMS MALHFLILLV PPLPLIFQVT
     PLSGRQWVVV LQISLPVILL DEALKYLSRK HVDEEKGRQ
 
 
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