LOCUS       NP_001020068             543 aa            linear   ROD 03-APR-2024
DEFINITION  EH domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001020068 XP_341795
VERSION     NP_001020068.1
DBSOURCE    REFSEQ: accession NM_001024897.1
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 543)
  AUTHORS   Yang,H.Q., Jana,K., Rindler,M.J. and Coetzee,W.A.
  TITLE     The trafficking protein, EHD2, positively regulates cardiac
            sarcolemmal KATP channel surface expression: role in
            cardioprotection
  JOURNAL   FASEB J 32 (3), 1613-1625 (2018)
   PUBMED   29133341
  REMARK    GeneRIF: EHD2 may be cardioprotective as a dominant-negative EHD2
            mutant sensitized cardiomyocytes to ischemic damage. Our findings
            highlight EHD2 as a potential pharmacologic target in the treatment
            of diseases with KATP channel trafficking defects
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Shah,C., Hegde,B.G., Moren,B., Behrmann,E., Mielke,T., Moenke,G.,
            Spahn,C.M.T., Lundmark,R., Daumke,O. and Langen,R.
  TITLE     Structural insights into membrane interaction and caveolar
            targeting of dynamin-like EHD2
  JOURNAL   Structure 22 (3), 409-420 (2014)
   PUBMED   24508342
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Ke,K., Rui,Y., Li,L., Zheng,H., Xu,W., Tan,X., Cao,J., Wu,X.,
            Cui,G. and Cao,M.
  TITLE     Upregulation of EHD2 after intracerebral hemorrhage in adult rats
  JOURNAL   J Mol Neurosci 54 (2), 171-180 (2014)
   PUBMED   24664435
  REMARK    GeneRIF: EHD2 expression was upregulated in the perihematomal
            caudate in adult rats after intracerebral hemorrhage.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Ludwig,A., Howard,G., Mendoza-Topaz,C., Deerinck,T., Mackey,M.,
            Sandin,S., Ellisman,M.H. and Nichols,B.J.
  TITLE     Molecular composition and ultrastructure of the caveolar coat
            complex
  JOURNAL   PLoS Biol 11 (8), e1001640 (2013)
   PUBMED   24013648
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Posey,A.D. Jr., Pytel,P., Gardikiotes,K., Demonbreun,A.R.,
            Rainey,M., George,M., Band,H. and McNally,E.M.
  TITLE     Endocytic recycling proteins EHD1 and EHD2 interact with
            fer-1-like-5 (Fer1L5) and mediate myoblast fusion
  JOURNAL   J Biol Chem 286 (9), 7379-7388 (2011)
   PUBMED   21177873
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Guilherme,A., Soriano,N.A., Furcinitti,P.S. and Czech,M.P.
  TITLE     Role of EHD1 and EHBP1 in perinuclear sorting and insulin-regulated
            GLUT4 recycling in 3T3-L1 adipocytes
  JOURNAL   J Biol Chem 279 (38), 40062-40075 (2004)
   PUBMED   15247266
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Park,S.Y., Ha,B.G., Choi,G.H., Ryu,J., Kim,B., Jung,C.Y. and Lee,W.
  TITLE     EHD2 interacts with the insulin-responsive glucose transporter
            (GLUT4) in rat adipocytes and may participate in insulin-induced
            GLUT4 recruitment
  JOURNAL   Biochemistry 43 (23), 7552-7562 (2004)
   PUBMED   15182197
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Guilherme,A., Soriano,N.A., Bose,S., Holik,J., Bose,A.,
            Pomerleau,D.P., Furcinitti,P., Leszyk,J., Corvera,S. and Czech,M.P.
  TITLE     EHD2 and the novel EH domain binding protein EHBP1 couple
            endocytosis to the actin cytoskeleton
  JOURNAL   J Biol Chem 279 (11), 10593-10605 (2004)
   PUBMED   14676205
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Rotem-Yehudar,R., Galperin,E. and Horowitz,M.
  TITLE     Association of insulin-like growth factor 1 receptor with EHD1 and
            SNAP29
  JOURNAL   J Biol Chem 276 (35), 33054-33060 (2001)
   PUBMED   11423532
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Suzuki,K., Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L9
  JOURNAL   Gene 93 (2), 297-300 (1990)
   PUBMED   2227441
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097385.1.
            
            On Jun 17, 2005 this sequence version replaced XP_341795.1.
            
            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 :: BC097385.1, SRR8487231.63233.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [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..543
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..543
                     /product="EH domain-containing protein 2"
                     /note="putative eps protein"
                     /calculated_mol_wt=61107
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          25..56
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BH64; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          60..300
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Region          65..72
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            65..72
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(70..73,153,220,222,256..258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Region          91..92
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            94
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            98..100
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Region          153..156
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            153..156
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(155..156,183..184)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Region          219..222
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            219..222
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Region          243
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            256..258
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     Region          288..394
                     /region_name="DUF5600"
                     /note="Domain of unknown function (DUF5600); pfam18150"
                     /db_xref="CDD:465667"
     Region          320..340
                     /region_name="Mediates membrane-binding.
                     /evidence=ECO:0000250|UniProtKB:Q8BH64"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          443..536
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZN4; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZN4; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          521..543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     CDS             1..543
                     /gene="Ehd2"
                     /gene_synonym="MGEPS"
                     /coded_by="NM_001024897.1:84..1715"
                     /db_xref="GeneID:361512"
                     /db_xref="RGD:1560856"
ORIGIN      
        1 mfswlkkgga rgqrseairt vtsslkelyr tkllpleehy rfgsfhspal edadfdgkpm
       61 vlvagqystg ktsfiqylle qevpgsrvgp epttdcfvav mhgetegtvp gnalvvdpek
      121 pfrklnpfgn tflnrfmcaq lpnqvlesis iidtpgilsg akqrvsrgyd fpavlrwfae
      181 rvdliillfd ahkleisdef seaigalrgh edkirvvlnk admvetqqlm rvygalmwal
      241 gkvvgtpevl rvyigsfwsq pllvpdnrrl feleeqdlfr diqglprhaa lrklndlvkr
      301 arlvrvhayi isylkkemps vfgkenkkkq lifklpvifa kiqlehhisp gdfpdcqkmq
      361 ellmahdftk fhslkpklle aldemlthdi aklmpllrqe elesveagvq ggafegtrmg
      421 pfvergpdea iedgeegsed daewvvtkdk skydeifynl apadgklsgs kaktwmvgtk
      481 lpnsvlgriw klsdvdrdgm lddeefalas hlieaklegh glptnlprrl vppskrrqkg
      541 sae
//
