LOCUS       NP_036400                490 aa            linear   PRI 28-APR-2025
DEFINITION  5'-3' exonuclease PLD3 [Homo sapiens].
ACCESSION   NP_036400
VERSION     NP_036400.2
DBSOURCE    REFSEQ: accession NM_012268.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Roske,Y., Cappel,C., Cremer,N., Hoffmann,P., Koudelka,T.,
            Tholey,A., Heinemann,U., Daumke,O. and Damme,M.
  TITLE     Structural analysis of PLD3 reveals insights into the mechanism of
            lysosomal 5' exonuclease-mediated nucleic acid degradation
  JOURNAL   Nucleic Acids Res 52 (1), 370-384 (2024)
   PUBMED   37994783
  REMARK    GeneRIF: Structural analysis of PLD3 reveals insights into the
            mechanism of lysosomal 5' exonuclease-mediated nucleic acid
            degradation.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Nackenoff,A.G., Hohman,T.J., Neuner,S.M., Akers,C.S., Weitzel,N.C.,
            Shostak,A., Ferguson,S.M., Mobley,B., Bennett,D.A., Schneider,J.A.,
            Jefferson,A.L., Kaczorowski,C.C. and Schrag,M.S.
  TITLE     PLD3 is a neuronal lysosomal phospholipase D associated with
            beta-amyloid plaques and cognitive function in Alzheimer's disease
  JOURNAL   PLoS Genet 17 (4), e1009406 (2021)
   PUBMED   33830999
  REMARK    GeneRIF: PLD3 is a neuronal lysosomal phospholipase D associated
            with beta-amyloid plaques and cognitive function in Alzheimer's
            disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Demirev,A.V., Song,H.L., Cho,M.H., Cho,K., Peak,J.J., Yoo,H.J.,
            Kim,D.H. and Yoon,S.Y.
  TITLE     V232M substitution restricts a distinct O-glycosylation of PLD3 and
            its neuroprotective function
  JOURNAL   Neurobiol Dis 129, 182-194 (2019)
   PUBMED   31121321
  REMARK    GeneRIF: the V232M mutation of PLD3 may affect Alzheimer's disease
            pathogenesis
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Gonzalez,A.C., Stroobants,S., Reisdorf,P., Gavin,A.L., Nemazee,D.,
            Schwudke,D., D'Hooge,R., Saftig,P. and Damme,M.
  TITLE     PLD3 and spinocerebellar ataxia
  JOURNAL   Brain 141 (11), e78 (2018)
   PUBMED   30312375
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Cheng,J., Kapranov,P., Drenkow,J., Dike,S., Brubaker,S., Patel,S.,
            Long,J., Stern,D., Tammana,H., Helt,G., Sementchenko,V.,
            Piccolboni,A., Bekiranov,S., Bailey,D.K., Ganesh,M., Ghosh,S.,
            Bell,I., Gerhard,D.S. and Gingeras,T.R.
  TITLE     Transcriptional maps of 10 human chromosomes at 5-nucleotide
            resolution
  JOURNAL   Science 308 (5725), 1149-1154 (2005)
   PUBMED   15790807
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 490)
  AUTHORS   Pedersen,K.M., Finsen,B., Celis,J.E. and Jensen,N.A.
  TITLE     Expression of a novel murine phospholipase D homolog coincides with
            late neuronal development in the forebrain
  JOURNAL   J Biol Chem 273 (47), 31494-31504 (1998)
   PUBMED   9813063
REFERENCE   9  (residues 1 to 490)
  AUTHORS   Cao,J.X., Koop,B.F. and Upton,C.
  TITLE     A human homolog of the vaccinia virus HindIII K4L gene is a member
            of the phospholipase D superfamily
  JOURNAL   Virus Res 48 (1), 11-18 (1997)
   PUBMED   9140189
REFERENCE   10 (residues 1 to 490)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX785201.1, BP304863.1,
            BC000553.1 and BQ640152.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 29, 2008 this sequence version replaced NP_036400.1.
            
            Summary: This gene encodes a member of the phospholipase D (PLD)
            family of enzymes that catalyze the hydrolysis of membrane
            phospholipids. The encoded protein is a single-pass type II
            membrane protein and contains two PLD phosphodiesterase domains.
            This protein influences processing of amyloid-beta precursor
            protein. Mutations in this gene are associated with Alzheimer
            disease risk. Alternatively spliced transcript variants encoding
            the same protein have been found for this gene. [provided by
            RefSeq, Apr 2014].
            
            Transcript Variant: This variant (2) represents the longer
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            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 :: SRR3476690.655781.1,
                                           SRR3476690.105080.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409735.9/ ENSP00000386938.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..490
                     /product="5'-3' exonuclease PLD3"
                     /EC_number="3.1.16.1"
                     /note="phosphatidylcholine-hydrolyzing phospholipase D3;
                     choline phosphatase 3; hindIII K4L homolog;
                     (S,S)-bis(monoacylglycero)phosphate synthase PLD3"
                     /calculated_mol_wt=54574
     Site            39..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IV08.1)"
     Site            71..72
                     /site_type="cleavage"
                     /note="Cleavage, by lysosomal cysteine proteases.
                     /evidence=ECO:0000305|PubMed:29386126,
                     ECO:0000305|PubMed:37994783; propagated from
                     UniProtKB/Swiss-Prot (Q8IV08.1)"
     Region          77..490
                     /region_name="PHA02820"
                     /note="phospholipase-D-like protein; Provisional"
                     /db_xref="CDD:222934"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:37994783; propagated from
                     UniProtKB/Swiss-Prot (Q8IV08.1)"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:37994783; propagated from
                     UniProtKB/Swiss-Prot (Q8IV08.1)"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:37994783; propagated from
                     UniProtKB/Swiss-Prot (Q8IV08.1)"
     Site            284
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:37994783; propagated from
                     UniProtKB/Swiss-Prot (Q8IV08.1)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:37994783; propagated from
                     UniProtKB/Swiss-Prot (Q8IV08.1)"
     CDS             1..490
                     /gene="PLD3"
                     /gene_synonym="AD19; HU-K4; HUK4; SCA46"
                     /coded_by="NM_012268.4:353..1825"
                     /db_xref="CCDS:CCDS33027.1"
                     /db_xref="GeneID:23646"
                     /db_xref="HGNC:HGNC:17158"
                     /db_xref="MIM:615698"
ORIGIN      
        1 mkpklmyqel kvpaeepane lpmneieawk aaekkarwvl lvlilavvgf galmtqlflw
       61 eygdlhlfgp nqrpapcydp ceavlvesip egldfpnast gnpstsqawl gllagahssl
      121 diasfywtlt nndthtqeps aqqgeevlrq lqtlapkgvn vriavskpsg pqpqadlqal
      181 lqsgaqvrmv dmqklthgvl htkfwvvdqt hfylgsanmd wrsltqvkel gvvmyncscl
      241 ardltkifea ywflgqagss ipstwprfyd trynqetpme iclngtpala ylasappplc
      301 psgrtpdlka llnvvdnars fiyvavmnyl ptlefshphr fwpaiddglr ratyergvkv
      361 rlliscwghs epsmraflls laalrdnhth sdiqvklfvv padeaqarip yarvnhnkym
      421 vteratyigt snwsgnyfte tagtsllvtq ngrgglrsql eaiflrdwds pyshdldtsa
      481 dsvgnacrll
//
