LOCUS       NM_001389466            1631 bp    mRNA    linear   PRI 24-JUN-2024
DEFINITION  Homo sapiens dipeptidase 1 (DPEP1), transcript variant 3, mRNA.
ACCESSION   NM_001389466 XM_005256285
VERSION     NM_001389466.1
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  (bases 1 to 1631)
  AUTHORS   Li,Y., Wang,X., Zhang,Q., Tian,D., Bai,Y., Feng,Y., Liu,W. and
            Diao,Z.
  TITLE     Dipeptidase 1 promotes ferroptosis in renal tubular epithelial
            cells in diabetic nephropathy via inhibition of the GSH/GPX4 axis
  JOURNAL   Int Immunopharmacol 133, 111955 (2024)
   PUBMED   38626544
  REMARK    GeneRIF: Dipeptidase 1 promotes ferroptosis in renal tubular
            epithelial cells in diabetic nephropathy via inhibition of the
            GSH/GPX4 axis.
REFERENCE   2  (bases 1 to 1631)
  AUTHORS   Zeng,C., Qi,G., Shen,Y., Li,W., Zhu,Q., Yang,C., Deng,J., Lu,W.,
            Liu,Q. and Jin,J.
  TITLE     DPEP1 promotes drug resistance in colon cancer cells by forming a
            positive feedback loop with ASCL2
  JOURNAL   Cancer Med 12 (1), 412-424 (2023)
   PUBMED   35670012
  REMARK    GeneRIF: DPEP1 promotes drug resistance in colon cancer cells by
            forming a positive feedback loop with ASCL2.
REFERENCE   3  (bases 1 to 1631)
  AUTHORS   Nitanai,Y., Satow,Y., Adachi,H. and Tsujimoto,M.
  TITLE     Crystal structure of human renal dipeptidase involved in
            beta-lactam hydrolysis
  JOURNAL   J Mol Biol 321 (2), 177-184 (2002)
   PUBMED   12144777
  REMARK    GeneRIF: Crystal structure of human renal dipeptidase involved in
            beta-lactam hydrolysis
REFERENCE   4  (bases 1 to 1631)
  AUTHORS   Kera,Y., Liu,Z., Matsumoto,T., Sorimachi,Y., Nagasaki,H. and
            Yamada,R.H.
  TITLE     Rat and human membrane dipeptidase: tissue distribution and
            developmental changes
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 123 (1), 53-58 (1999)
   PUBMED   10425712
REFERENCE   5  (bases 1 to 1631)
  AUTHORS   Satoh,S., Ohtsuka,K., Keida,Y., Kusunoki,C., Konta,Y., Niwa,M. and
            Kohsaka,M.
  TITLE     Gene structural analysis and expression of human renal dipeptidase
  JOURNAL   Biotechnol Prog 10 (2), 134-140 (1994)
   PUBMED   7764673
REFERENCE   6  (bases 1 to 1631)
  AUTHORS   Satoh,S., Kusunoki,C., Konta,Y., Niwa,M. and Kohsaka,M.
  TITLE     Cloning and structural analysis of genomic DNA for human renal
            dipeptidase
  JOURNAL   Biochim Biophys Acta 1172 (1-2), 181-183 (1993)
   PUBMED   8439558
REFERENCE   7  (bases 1 to 1631)
  AUTHORS   Adachi,H., Katayama,T., Inuzuka,C., Oikawa,S., Tsujimoto,M. and
            Nakazato,H.
  TITLE     Identification of membrane anchoring site of human renal
            dipeptidase and construction and expression of a cDNA for its
            secretory form
  JOURNAL   J Biol Chem 265 (25), 15341-15345 (1990)
   PUBMED   2168407
REFERENCE   8  (bases 1 to 1631)
  AUTHORS   Adachi,H., Tawaragi,Y., Inuzuka,C., Kubota,I., Tsujimoto,M.,
            Nishihara,T. and Nakazato,H.
  TITLE     Primary structure of human microsomal dipeptidase deduced from
            molecular cloning
  JOURNAL   J Biol Chem 265 (7), 3992-3995 (1990)
   PUBMED   2303490
REFERENCE   9  (bases 1 to 1631)
  AUTHORS   Hooper,N.M., Keen,J.N. and Turner,A.J.
  TITLE     Characterization of the glycosyl-phosphatidylinositol-anchored
            human renal dipeptidase reveals that it is more extensively
            glycosylated than the pig enzyme
  JOURNAL   Biochem J 265 (2), 429-433 (1990)
   PUBMED   2137335
REFERENCE   10 (bases 1 to 1631)
  AUTHORS   Adachi,H., Kubota,I., Okamura,N., Iwata,H., Tsujimoto,M.,
            Nakazato,H., Nishihara,T. and Noguchi,T.
  TITLE     Purification and characterization of human microsomal dipeptidase
  JOURNAL   J Biochem 105 (6), 957-961 (1989)
   PUBMED   2768222
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010538.9.
            
            On Dec 22, 2020 this sequence version replaced XM_005256285.5.
            
            Summary: The protein encoded by this gene is a kidney membrane
            enzyme involved in the metabolism of glutathione and other similar
            proteins by dipeptide hydrolysis. The encoded protein is known to
            regulate leukotriene activity by catalyzing the conversion of
            leukotriene D4 to leukotriene E4. This protein uses zinc as a
            cofactor and acts as a disulfide-linked homodimer. [provided by
            RefSeq, Dec 2020].
            
            Transcript Variant: This variant (3), as well as variants 1, 2, and
            4-6, encodes isoform a.
            
            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 :: SRR11853558.9748.1,
                                           SRR14038193.2173193.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000690203.1/ ENSP00000508584.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-78                AC010538.9         127955-128032       c
            79-288              AC010538.9         111160-111369       c
            289-421             AC010538.9         105634-105766       c
            422-554             AC010538.9         105278-105410       c
            555-705             AC010538.9         104991-105141       c
            706-775             AC010538.9         104739-104808       c
            776-952             AC010538.9         104294-104470       c
            953-1037            AC010538.9         104122-104206       c
            1038-1113           AC010538.9         103967-104042       c
            1114-1249           AC010538.9         103703-103838       c
            1250-1631           AC010538.9         103241-103622       c
FEATURES             Location/Qualifiers
     source          1..1631
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     gene            1..1631
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /note="dipeptidase 1"
                     /db_xref="GeneID:1800"
                     /db_xref="HGNC:HGNC:3002"
                     /db_xref="MIM:179780"
     exon            1..78
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            79..288
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     CDS             185..1420
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /EC_number="3.4.13.19"
                     /EC_number="3.5.2.6"
                     /note="isoform a precursor is encoded by transcript
                     variant 3; hRDP; renal dipeptidase; dehydropeptidase-I;
                     microsomal dipeptidase; testicular tissue protein Li 57;
                     dipeptidase 1 (renal); beta-lactamase"
                     /codon_start=1
                     /product="dipeptidase 1 isoform a precursor"
                     /protein_id="NP_001376395.1"
                     /db_xref="CCDS:CCDS10982.1"
                     /db_xref="GeneID:1800"
                     /db_xref="HGNC:HGNC:3002"
                     /db_xref="MIM:179780"
                     /translation="MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLL
                     DMFNNRLQDERANLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQM
                     DVVHRMCRMYPETFLYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLG
                     MRYLTLTHSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVA
                     TMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTN
                     KANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWT
                     EAEVKGALADNLLRVFEAVEQASNLTQAPEEEPIPLDQLGGSCRTHYGYSSGASSLHR
                     HWGLLLASLAPLVLCLSLL"
     exon            289..421
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            422..554
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            555..705
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            706..775
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            776..952
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            953..1037
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            1038..1113
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            1114..1249
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     exon            1250..1631
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1609..1614
                     /regulatory_class="polyA_signal_sequence"
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /note="hexamer: AATAAA"
     polyA_site      1631
                     /gene="DPEP1"
                     /gene_synonym="MBD1; MDP; RDP"
                     /note="major polyA site"
ORIGIN      
        1 agcccagctg tgagcctggc gtgggagctg cctaggccgg gccctgccag ggagcaagtc
       61 tgcatcgcag aggccagggc agagtggctc ctcacagcct gaagctcatc cttctgcacg
      121 ggccagccag gccagcacag aggcaccagg gcagcagtgc acacaggtcc ccggggaccc
      181 caccatgtgg agcggatggt ggctgtggcc ccttgtggcc gtctgcactg cagacttctt
      241 tcgggacgag gcagagagga tcatgaggga ctcccctgtc attgatgggc acaatgacct
      301 cccctggcag ctgctggata tgttcaacaa ccggctgcag gacgagaggg ccaacctgac
      361 caccttggcc ggcacacaca ccaacatccc caagctgagg gccggctttg tgggaggcca
      421 gttctggtcc gtgtacacgc cctgcgacac ccagaacaaa gacgccgtgc ggaggacgct
      481 ggagcagatg gacgtggtcc accgcatgtg ccggatgtac ccggagacct tcctgtatgt
      541 caccagcagt gcaggcattc ggcaggcctt ccgggaaggg aaggtggcca gcctgatcgg
      601 cgtggagggc ggccactcca ttgacagcag tttgggcgtc ctgcgggcac tctatcagct
      661 gggcatgcgg tacctgaccc tcacccacag ctgcaacacg ccctgggctg acaactggct
      721 ggtggacacg ggagacagcg agccccagag ccaaggcttg tcaccctttg ggcagcgtgt
      781 ggtgaaggag ctgaaccgtc tgggggtcct catcgacttg gctcacgtgt ctgtggccac
      841 catgaaggcc accctgcagc tgtccagagc cccggtcatc ttcagccact cctcggccta
      901 cagcgtgtgc gcaagccggc gcaacgtgcc tgacgacgtc ctgaggctgg tgaaacagac
      961 agacagcctg gtgatggtga acttctacaa caattacatt tcctgcacca acaaggccaa
     1021 cctgtcccaa gtggccgacc atctggatca catcaaggag gtggcaggag ccagagccgt
     1081 gggttttggt ggggactttg atggtgttcc aagggtccct gaggggctgg aggacgtctc
     1141 caagtatcca gacctgatcg ctgagctgct caggaggaac tggacggagg cggaggtcaa
     1201 gggcgcactg gctgacaacc tgctgagggt cttcgaggct gtggaacagg ccagcaacct
     1261 cacacaggct cccgaggagg agcccatccc gctggaccag ctgggtggct cctgcaggac
     1321 ccattacggc tactcctctg gggcttccag cctccatcgc cactgggggc tcctgctggc
     1381 ctccctcgct cccctggtcc tctgtctgtc tctcctgtga aacctgggag accagagtcc
     1441 cctttagggt tcccggagct ccgggaagac ccgcccatcc caggactcca gatgccagga
     1501 gccctgctgc ccacatgcaa ggaccagcat ctcctgagag gacgcctggg cttacctggg
     1561 gggcaggatg cctggggaca gttcaggaca cacacacagt aggcccgcaa taaaagcaac
     1621 accccttcac a
//
