LOCUS       NP_001033063             692 aa            linear   ROD 10-MAY-2024
DEFINITION  junctophilin-2 [Rattus norvegicus].
ACCESSION   NP_001033063 XP_006235588 XP_230853
VERSION     NP_001033063.1
DBSOURCE    REFSEQ: accession NM_001037974.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Zhou,J., Liu,H., Lin,Y. and Zhao,J.
  TITLE     Membrane occupation and recognition nexus (MORN) motif controls
            protein localization and function
  JOURNAL   FEBS Lett 596 (14), 1839-1850 (2022)
   PUBMED   35568981
  REMARK    Review article
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Poulet,C., Sanchez-Alonso,J., Swiatlowska,P., Mouy,F.,
            Lucarelli,C., Alvarez-Laviada,A., Gross,P., Terracciano,C.,
            Houser,S. and Gorelik,J.
  TITLE     Junctophilin-2 tethers T-tubules and recruits functional L-type
            calcium channels to lipid rafts in adult cardiomyocytes
  JOURNAL   Cardiovasc Res 117 (1), 149-161 (2021)
   PUBMED   32053184
  REMARK    GeneRIF: Junctophilin-2 tethers T-tubules and recruits functional
            L-type calcium channels to lipid rafts in adult cardiomyocytes.
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Luo,T., Li,L., Peng,Y., Xie,R., Yan,N., Fan,H. and Zhang,Q.
  TITLE     The MORN domain of Junctophilin2 regulates functional interactions
            with small-conductance Ca2+ -activated potassium channel subtype2
            (SK2)
  JOURNAL   Biofactors 47 (1), 69-79 (2021)
   PUBMED   31904168
  REMARK    GeneRIF: The MORN domain of Junctophilin2 regulates functional
            interactions with small-conductance Ca(2+) -activated potassium
            channel subtype2 (SK2).
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Chan,B.Y.H., Roczkowsky,A., Cho,W.J., Poirier,M., Lee,T.Y.T.,
            Mahmud,Z. and Schulz,R.
  TITLE     Junctophilin-2 is a target of matrix metalloproteinase-2 in
            myocardial ischemia-reperfusion injury
  JOURNAL   Basic Res Cardiol 114 (6), 42 (2019)
   PUBMED   31506724
  REMARK    GeneRIF: Degradation of junctophilin-2 by MMP-2 is an early
            consequence of myocardial IR injury which may initiate a cascade of
            sequelae leading to impaired contractile function.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Guo,A., Wang,Y., Chen,B., Wang,Y., Yuan,J., Zhang,L., Hall,D.,
            Wu,J., Shi,Y., Zhu,Q., Chen,C., Thiel,W.H., Zhan,X., Weiss,R.M.,
            Zhan,F., Musselman,C.A., Pufall,M., Zhu,W., Au,K.F., Hong,J.,
            Anderson,M.E., Grueter,C.E. and Song,L.S.
  TITLE     E-C coupling structural protein junctophilin-2 encodes a
            stress-adaptive transcription regulator
  JOURNAL   Science 362 (6421) (2018)
   PUBMED   30409805
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Jayasinghe,I., Baddeley,D., Kong,C.H., Wehrens,X.H., Cannell,M.B.
            and Soeller,C.
  TITLE     Nanoscale organization of junctophilin-2 and ryanodine receptors
            within peripheral couplings of rat ventricular cardiomyocytes
  JOURNAL   Biophys J 102 (5), L19-L21 (2012)
   PUBMED   22404946
  REMARK    GeneRIF: JPH2 is dispersed throughout RyR clusters and that the
            packing of JPH2 into junctions and the assembly of RyR clusters are
            tightly linked
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Wei,S., Guo,A., Chen,B., Kutschke,W., Xie,Y.P., Zimmerman,K.,
            Weiss,R.M., Anderson,M.E., Cheng,H. and Song,L.S.
  TITLE     T-tubule remodeling during transition from hypertrophy to heart
            failure
  JOURNAL   Circ Res 107 (4), 520-531 (2010)
   PUBMED   20576937
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Woo,J.S., Hwang,J.H., Ko,J.K., Weisleder,N., Kim,D.H., Ma,J. and
            Lee,E.H.
  TITLE     S165F mutation of junctophilin 2 affects Ca2+ signalling in
            skeletal muscle
  JOURNAL   Biochem J 427 (1), 125-134 (2010)
   PUBMED   20095964
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Minamisawa,S., Oshikawa,J., Takeshima,H., Hoshijima,M., Wang,Y.,
            Chien,K.R., Ishikawa,Y. and Matsuoka,R.
  TITLE     Junctophilin type 2 is associated with caveolin-3 and is
            down-regulated in the hypertrophic and dilated cardiomyopathies
  JOURNAL   Biochem Biophys Res Commun 325 (3), 852-856 (2004)
   PUBMED   15541368
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before May 7, 2024 this sequence version replaced
            XP_006235588.1, XP_230853.2.
            
            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 :: FQ223967.1, SRR26643285.14197.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..692
                     /product="junctophilin-2"
                     /note="JP-2; junctophilin type 2"
                     /calculated_mol_wt=74128
     Region          <2..143
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          14..36
                     /region_name="MORN 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          38..>328
                     /region_name="PLN03185"
                     /note="phosphatidylinositol phosphate kinase; Provisional"
                     /db_xref="CDD:215619"
     Region          38..59
                     /region_name="MORN 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          60..79
                     /region_name="MORN 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          82..104
                     /region_name="MORN 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          106..128
                     /region_name="MORN 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          129..151
                     /region_name="MORN 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            155..156
                     /site_type="cleavage"
                     /note="Cleavage, by calpain.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          164..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BR39; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            201..202
                     /site_type="cleavage"
                     /note="Cleavage, by calpain.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          246..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          285..307
                     /region_name="MORN 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          308..330
                     /region_name="MORN 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          345..359
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          439..661
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          <446..633
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Region          488..492
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            565..566
                     /site_type="cleavage"
                     /note="Cleavage, by calpain.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ET78; propagated from
                     UniProtKB/Swiss-Prot (Q2PS20.1)"
     Site            671..691
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PS20.1)"
     CDS             1..692
                     /gene="Jph2"
                     /coded_by="NM_001037974.2:437..2515"
                     /db_xref="GeneID:296345"
                     /db_xref="RGD:1305196"
ORIGIN      
        1 msggrfdfdd ggaycggweg gkahghglct gpkgqgeysg swnfgfevag vytwpsgntf
       61 egywsqgkrh glgietkgrw lykgewthgf kgrygirqst nsgakyegtw nnglqdgygt
      121 etyadggtyq gqftngmrhg ygvrqsvpyg mavvvrsplr tslsslrseh sngtvapdsp
      181 aadgptlplp pvprggfals llataeaarp pglftrgall grlrrsesrt slgsqrsrls
      241 flkselssga sdaastgsla egaegpddaa apfdadidat ttetymgewk ndkrsgfgvs
      301 erssglryeg ewldnlrhgy grttlpdghr eegkyrhnvl vkgtkrrvlp lksnkvrqkv
      361 ehgvegaqra aaiarqkaei aasrtshaka kaeaaeqaal aanqesniar tlakelapdf
      421 yqpgpeyqkr rllqeilens eslleprerg pgtglperpr espqlheret pqpeggppsp
      481 agtppqpkrp rpgsskdgll spgawngepg gegsrpatps dgagrrspar pasehmaiea
      541 lqpppapsre pevalyrgyh syavrtgppe pppledepep epevprsdse ppspvsatvq
      601 eeespaprsr vpakpatlep kpivpkaepk akarktearg lskagakkkg rkevaqeaea
      661 eveveevpnt vlicmvilln iglailfvhl lt
//
