LOCUS       NP_001099402             182 aa            linear   ROD 01-JUN-2024
DEFINITION  vacuolar protein sorting-associated protein 29 [Rattus norvegicus].
ACCESSION   NP_001099402 XP_001079533 XP_213780
VERSION     NP_001099402.1
DBSOURCE    REFSEQ: accession NM_001105932.1
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 182)
  AUTHORS   McNally,K.E., Faulkner,R., Steinberg,F., Gallon,M., Ghai,R.,
            Pim,D., Langton,P., Pearson,N., Danson,C.M., Nagele,H.,
            Morris,L.L., Singla,A., Overlee,B.L., Heesom,K.J., Sessions,R.,
            Banks,L., Collins,B.M., Berger,I., Billadeau,D.D., Burstein,E. and
            Cullen,P.J.
  TITLE     Retriever is a multiprotein complex for retromer-independent
            endosomal cargo recycling
  JOURNAL   Nat Cell Biol 19 (10), 1214-1225 (2017)
   PUBMED   28892079
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Follett,J., Bugarcic,A., Yang,Z., Ariotti,N., Norwood,S.J.,
            Collins,B.M., Parton,R.G. and Teasdale,R.D.
  TITLE     Parkinson Disease-linked Vps35 R524W Mutation Impairs the Endosomal
            Association of Retromer and Induces alpha-Synuclein Aggregation
  JOURNAL   J Biol Chem 291 (35), 18283-18298 (2016)
   PUBMED   27385586
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Gallon,M. and Cullen,P.J.
  TITLE     Retromer and sorting nexins in endosomal sorting
  JOURNAL   Biochem Soc Trans 43 (1), 33-47 (2015)
   PUBMED   25619244
  REMARK    Review article
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Hesketh,G.G., Perez-Dorado,I., Jackson,L.P., Wartosch,L.,
            Schafer,I.B., Gray,S.R., McCoy,A.J., Zeldin,O.B., Garman,E.F.,
            Harbour,M.E., Evans,P.R., Seaman,M.N.J., Luzio,J.P. and Owen,D.J.
  TITLE     VARP is recruited on to endosomes by direct interaction with
            retromer, where together they function in export to the cell
            surface
  JOURNAL   Dev Cell 29 (5), 591-606 (2014)
   PUBMED   24856514
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Popovic,D. and Dikic,I.
  TITLE     TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation
            of autophagy
  JOURNAL   EMBO Rep 15 (4), 392-401 (2014)
   PUBMED   24603492
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Kim,E., Lee,Y., Lee,H.J., Kim,J.S., Song,B.S., Huh,J.W., Lee,S.R.,
            Kim,S.U., Kim,S.H., Hong,Y., Shim,I. and Chang,K.T.
  TITLE     Implication of mouse Vps26b-Vps29-Vps35 retromer complex in
            sortilin trafficking
  JOURNAL   Biochem Biophys Res Commun 403 (2), 167-171 (2010)
   PUBMED   21040701
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473973.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001079533.1, XP_213780.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB557496.1, FQ213481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..182
                     /product="vacuolar protein sorting-associated protein 29"
                     /EC_number="3.1.3.3"
                     /note="vacuolar protein sorting 29 homolog"
                     /calculated_mol_wt=20338
     Region          2..179
                     /region_name="MPP_Vps29"
                     /note="Homo sapiens Vps29 and related proteins,
                     metallophosphatase domain; cd07394"
                     /db_xref="CDD:163637"
     Site            order(8,10,39,62,86,115,117)
                     /site_type="active"
                     /db_xref="CDD:163637"
     Site            order(8,10,39,62,86,115,117)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:163637"
     Site            order(8,10,14,39,62..63,86,91,115)
                     /site_type="other"
                     /note="Vps29:Vps35 subcomplex [polypeptide binding]"
                     /db_xref="CDD:163637"
     Site            50
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBQ0; propagated from
                     UniProtKB/Swiss-Prot (B2RZ78.2)"
     CDS             1..182
                     /gene="Vps29"
                     /coded_by="NM_001105932.1:84..632"
                     /db_xref="GeneID:288666"
                     /db_xref="RGD:1308332"
ORIGIN      
        1 mlvlvlgdlh iphrcnslpa kfkkllvpgk iqhilctgnl ctkesydylk tlagdvhivr
       61 gdfdeslnyp eqkvvtvgqf kiglihghqv ipwgdmasla llqrqfdvdi lisghthkfe
      121 afehenkfyi npgsatgayn aletniipsf vlmdiqastv vtyvyqligd dvkverieyk
      181 ks
//
