GenomeNet

Database: RefSeq
Entry: NP_036831
LinkDB: NP_036831
Original site: NP_036831 
LOCUS       NP_036831                222 aa            linear   ROD 21-NOV-2023
DEFINITION  dnaJ homolog subfamily B member 9 precursor [Rattus norvegicus].
ACCESSION   NP_036831
VERSION     NP_036831.2
DBSOURCE    REFSEQ: accession NM_012699.3
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 222)
  AUTHORS   Fritz JM and Weaver TE.
  TITLE     The BiP cochaperone ERdj4 is required for B cell development and
            function
  JOURNAL   PLoS One 9 (9), e107473 (2014)
   PUBMED   25222125
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Lai CW, Otero JH, Hendershot LM and Snapp E.
  TITLE     ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family
            protein that interacts with ER-associated degradation machinery
  JOURNAL   J Biol Chem 287 (11), 7969-7978 (2012)
   PUBMED   22267725
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Hageman J, van Waarde MA, Zylicz A, Walerych D and Kampinga HH.
  TITLE     The diverse members of the mammalian HSP70 machine show distinct
            chaperone-like activities
  JOURNAL   Biochem J 435 (1), 127-142 (2011)
   PUBMED   21231916
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Gonzalez-Begne M, Lu B, Han X, Hagen FK, Hand AR, Melvin JE and
            Yates JR.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Dong M, Bridges JP, Apsley K, Xu Y and Weaver TE.
  TITLE     ERdj4 and ERdj5 are required for endoplasmic reticulum-associated
            protein degradation of misfolded surfactant protein C
  JOURNAL   Mol Biol Cell 19 (6), 2620-2630 (2008)
   PUBMED   18400946
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Berger BJ, Muller TS, Buschmann IR, Peters K, Kirsch M, Christ B
            and Prols F.
  TITLE     High levels of the molecular chaperone Mdg1/ERdj4 reflect the
            activation state of endothelial cells
  JOURNAL   Exp Cell Res 290 (1), 82-92 (2003)
   PUBMED   14516790
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Shen Y, Meunier L and Hendershot LM.
  TITLE     Identification and characterization of a novel endoplasmic
            reticulum (ER) DnaJ homologue, which stimulates ATPase activity of
            BiP in vitro and is induced by ER stress
  JOURNAL   J Biol Chem 277 (18), 15947-15956 (2002)
   PUBMED   11836248
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Prols F, Mayer MP, Renner O, Czarnecki PG, Ast M, Gassler C,
            Wilting J, Kurz H and Christ B.
  TITLE     Upregulation of the cochaperone Mdg1 in endothelial cells is
            induced by stress and during in vitro angiogenesis
  JOURNAL   Exp Cell Res 269 (1), 42-53 (2001)
   PUBMED   11525638
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JACYVU010000164.1.
            
            On Oct 10, 2000 this sequence version replaced NP_036831.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X98993.2, BC070915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..222
                     /product="dnaJ homolog subfamily B member 9 precursor"
                     /note="mdg-1; microvascular endothelial differentiation
                     gene 1 protein; dnaJ homolog, subfamily b, member 9; DnaJ
                     (Hsp40) homolog, subfamily B, member 9; ER-resident
                     protein ERdj4; endoplasmic reticulum DNA J
                     domain-containing protein 4"
                     /calculated_mol_wt=23210
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:4.0"
                     /calculated_mol_wt=2525
     mat_peptide     24..222
                     /product="DnaJ homolog subfamily B member 9.
                     /id=PRO_0000071034"
                     /note="propagated from UniProtKB/Swiss-Prot (P97554.2)"
                     /calculated_mol_wt=23210
     Region          27..>134
                     /region_name="DnaJ_bact"
                     /note="chaperone protein DnaJ; TIGR02349"
                     /db_xref="CDD:274090"
     Region          91..222
                     /region_name="Divergent targeting domain.
                     /evidence=ECO:0000250|UniProtKB:Q9QYI6"
                     /note="propagated from UniProtKB/Swiss-Prot (P97554.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBS3; propagated from
                     UniProtKB/Swiss-Prot (P97554.2)"
     CDS             1..222
                     /gene="Dnajb9"
                     /gene_synonym="ERdj4; Mdg1"
                     /coded_by="NM_012699.3:179..847"
                     /db_xref="GeneID:24908"
                     /db_xref="RGD:3070"
ORIGIN      
        1 matpqsvfvf aicilmitel ilasknyydi lgvpksaser qikkafhkla mkyhpdknks
       61 pdaeakfrei aeayetlsda nrrkeydiig hsaftngkgq rsngspfeqs fnfnfddlfk
      121 dfnlfgqnqn trskkhfenh fqtrqdgssr qrhhfqefsf ggglfddmfe dmekmfsfsg
      181 fdstnrrtvq tenrfhgssk hcrtvtqrrg nmvttytdcs gq
//
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