LOCUS       NP_058025               1038 aa            linear   ROD 03-JUN-2024
DEFINITION  sarcoplasmic/endoplasmic reticulum calcium ATPase 3 isoform b [Mus
            musculus].
ACCESSION   NP_058025
VERSION     NP_058025.2
DBSOURCE    REFSEQ: accession NM_016745.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Feng,M., Elaib,Z., Borgel,D., Denis,C.V., Adam,F., Bryckaert,M.,
            Rosa,J.P. and Bobe,R.
  TITLE     NAADP/SERCA3-Dependent Ca2+ Stores Pathway Specifically Controls
            Early Autocrine ADP Secretion Potentiating Platelet Activation
  JOURNAL   Circ Res 127 (7), e166-e183 (2020)
   PUBMED   32588751
  REMARK    GeneRIF: NAADP/SERCA3-Dependent Ca(2+) Stores Pathway Specifically
            Controls Early Autocrine ADP Secretion Potentiating Platelet
            Activation.
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Fecher-Trost,C., Lux,F., Busch,K.M., Raza,A., Winter,M.,
            Hielscher,F., Belkacemi,T., van der Eerden,B., Boehm,U.,
            Freichel,M. and Weissgerber,P.
  TITLE     Maternal Transient Receptor Potential Vanilloid 6 (Trpv6) Is
            Involved In Offspring Bone Development
  JOURNAL   J Bone Miner Res 34 (4), 699-710 (2019)
   PUBMED   30786075
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Anderson,D.M., Makarewich,C.A., Anderson,K.M., Shelton,J.M.,
            Bezprozvannaya,S., Bassel-Duby,R. and Olson,E.N.
  TITLE     Widespread control of calcium signaling by a family of
            SERCA-inhibiting micropeptides
  JOURNAL   Sci Signal 9 (457), ra119 (2016)
   PUBMED   27923914
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1038)
  AUTHORS   Elaib,Z., Adam,F., Berrou,E., Bordet,J.C., Prevost,N., Bobe,R.,
            Bryckaert,M. and Rosa,J.P.
  TITLE     Full activation of mouse platelets requires ADP secretion regulated
            by SERCA3 ATPase-dependent calcium stores
  JOURNAL   Blood 128 (8), 1129-1138 (2016)
   PUBMED   27301859
  REMARK    GeneRIF: SERCA3-dependent Ca(2+) stores control a specific ADP
            secretion pathway.
REFERENCE   5  (residues 1 to 1038)
  AUTHORS   Anderson,D.M., Anderson,K.M., Chang,C.L., Makarewich,C.A.,
            Nelson,B.R., McAnally,J.R., Kasaragod,P., Shelton,J.M., Liou,J.,
            Bassel-Duby,R. and Olson,E.N.
  TITLE     A micropeptide encoded by a putative long noncoding RNA regulates
            muscle performance
  JOURNAL   Cell 160 (4), 595-606 (2015)
   PUBMED   25640239
REFERENCE   6  (residues 1 to 1038)
  AUTHORS   Paul,R.J.
  TITLE     The role of phospholamban and SERCA3 in regulation of smooth
            muscle-endothelial cell signalling mechanisms: evidence from
            gene-ablated mice
  JOURNAL   Acta Physiol Scand 164 (4), 589-597 (1998)
   PUBMED   9887981
  REMARK    Review article
REFERENCE   7  (residues 1 to 1038)
  AUTHORS   Dode,L., De Greef,C., Mountian,I., Attard,M., Town,M.M.,
            Casteels,R. and Wuytack,F.
  TITLE     Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3
            gene. Promoter analysis and alternative splicing of the SERCA3
            pre-mRNA
  JOURNAL   J Biol Chem 273 (22), 13982-13994 (1998)
   PUBMED   9593748
REFERENCE   8  (residues 1 to 1038)
  AUTHORS   Ozog,A., Pouzet,B., Bobe,R. and Lompre,A.M.
  TITLE     Characterization of the 3' end of the mouse SERCA 3 gene and tissue
            distribution of mRNA spliced variants
  JOURNAL   FEBS Lett 427 (3), 349-352 (1998)
   PUBMED   9637255
REFERENCE   9  (residues 1 to 1038)
  AUTHORS   Liu,L.H., Paul,R.J., Sutliff,R.L., Miller,M.L., Lorenz,J.N.,
            Pun,R.Y., Duffy,J.J., Doetschman,T., Kimura,Y., MacLennan,D.H.,
            Hoying,J.B. and Shull,G.E.
  TITLE     Defective endothelium-dependent relaxation of vascular smooth
            muscle and endothelial cell Ca2+ signaling in mice lacking
            sarco(endo)plasmic reticulum Ca2+-ATPase isoform 3
  JOURNAL   J Biol Chem 272 (48), 30538-30545 (1997)
   PUBMED   9374548
REFERENCE   10 (residues 1 to 1038)
  AUTHORS   Slack,J.P., Grupp,I.L., Ferguson,D.G., Rosenthal,N. and
            Kranias,E.G.
  TITLE     Ectopic expression of phospholamban in fast-twitch skeletal muscle
            alters sarcoplasmic reticulum Ca2+ transport and muscle relaxation
  JOURNAL   J Biol Chem 272 (30), 18862-18868 (1997)
   PUBMED   9228063
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK155904.1, AK089487.1, U49393.1, AK152999.1 and BY549777.1.
            
            On Jun 9, 2003 this sequence version replaced NP_058025.1.
            
            Transcript Variant: This variant (2) includes an additional exon in
            the 3' coding region resulting in a frameshift, compared to variant
            1. Variant 2 encodes isoform b, which is longer and has a distinct
            C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017639.1, U49393.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 45.0 cM"
     Protein         1..1038
                     /product="sarcoplasmic/endoplasmic reticulum calcium
                     ATPase 3 isoform b"
                     /EC_number="7.2.2.10"
                     /note="sarcoendoplasmic reticulum Ca2+ ATPase type 3;
                     sarcoplasmic/endoplasmic reticulum calcium ATPase 3;
                     calcium pump 3; SR Ca(2+)-ATPase 3; sarco /endoplasmic
                     reticulum Ca2+ -ATPase"
                     /calculated_mol_wt=113508
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q93084; propagated from
                     UniProtKB/Swiss-Prot (Q64518.4)"
     Region          5..989
                     /region_name="P-type_ATPase_SERCA"
                     /note="sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA),
                     similar to mammalian ATP2A1-3/SERCA1-3; cd02083"
                     /db_xref="CDD:319778"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q64518.4)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q64518.4)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q64518.4)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            254..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            296..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            order(309,796,800)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Site            order(351..353,442,487,489,492,494,515..517,560,562,
                     625..627,678,684,703,706)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:319778"
     Region          370..400
                     /region_name="Interaction with phospholamban 1.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q64518.4)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q93084; propagated from
                     UniProtKB/Swiss-Prot (Q64518.4)"
     Site            758..777
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            order(768,771,799..800,908)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Region          788..808
                     /region_name="Interaction with phospholamban 2.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            788..808
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            829..851
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            898..917
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            931..949
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     Site            965..985
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64518.4)"
     CDS             1..1038
                     /gene="Atp2a3"
                     /gene_synonym="Serca3; SERCA3b"
                     /coded_by="NM_016745.3:186..3302"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS24991.1"
                     /db_xref="GeneID:53313"
                     /db_xref="MGI:MGI:1194503"
ORIGIN      
        1 meeahllsaa dvlrrfsvta egglsleqvt darerygpne lpteegkslw elvveqfedl
       61 lvrilllaal vsfvlawfee geetttafve plvimlilva naivgvwqer naesaiealk
      121 eyepemgkvi rsdrkgvqri rardivpgdi vevavgdkvp adlrlieiks ttlrvdqsil
      181 tgesvsvtkh tdaipdprav nqdkknmlfs gtniasgkal gvavatglqt elgkirsqma
      241 avepertplq rkldefgrql shaisvicva vwvinighfa dpahggswlr gavyyfkiav
      301 alavaaipeg lpavittcla lgtrrmarkn aivrslpsve tlgctsvics dktgtlttnq
      361 msvcrmfvva eaeagtcrlh eftisgttyt pegevrqgeq pvrcgqfdgl velaticalc
      421 ndsaldynea kgvyekvgea tetaltclve kmnvfdtdlk glsrveraga cnsvikqlmr
      481 keftlefsrd rksmsvyctp tradpkvqgs kmfvkgapes viercssvrv gsrtaplstt
      541 srehilakir dwgsgsdtlr clalatrdtp prkedmhldd csrfvqyetd ltfvgcvgml
      601 dpprpevaac itrcsragir vvmitgdnkg tavaicrrlg ifgdtedvlg kaytgrefdd
      661 lspeqqrqac rtarcfarve pahksriven lqsfneitam tgdgvndapa lkkaeigiam
      721 gsgtavaksa aemvlsddnf asivaaveeg raiynnmkqf irylissnvg evvcifltai
      781 lglpealipv qllwvnlvtd glpatalgfn ppdldimekp prnprealis gwlffrylai
      841 gvyvglatva aatwwflydt egpqvtfyql rnflkcsedn plfagidckv fesrfpttma
      901 lsvlvtiemc nalnsvsenq sllrmppwln pwllgavvms malhflillv pplplifqvt
      961 plsgrqwgvv lqmslpvill dealkylsrn hmdgvlgtfm qarsrqlptt srtpyhtgkk
     1021 gpevnpgsrg espvwpsd
//
