LOCUS       NP_001012056             575 aa            linear   ROD 03-APR-2024
DEFINITION  carboxylesterase 5A precursor [Rattus norvegicus].
ACCESSION   NP_001012056 XP_226263
VERSION     NP_001012056.2
DBSOURCE    REFSEQ: accession NM_001012056.2
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 575)
  AUTHORS   Ru,Y.F., Xue,H.M., Ni,Z.M., Xia,D., Zhou,Y.C. and Zhang,Y.L.
  TITLE     An epididymis-specific carboxyl esterase CES5A is required for
            sperm capacitation and male fertility in the rat
  JOURNAL   Asian J Androl 17 (2), 292-297 (2015)
   PUBMED   25475668
  REMARK    GeneRIF: CES5A plays an important role in sperm maturation and male
            fertility in the rat.
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Holmes,R.S., Wright,M.W., Laulederkind,S.J., Cox,L.A., Hosokawa,M.,
            Imai,T., Ishibashi,S., Lehner,R., Miyazaki,M., Perkins,E.J.,
            Potter,P.M., Redinbo,M.R., Robert,J., Satoh,T., Yamashita,T.,
            Yan,B., Yokoi,T., Zechner,R. and Maltais,L.J.
  TITLE     Recommended nomenclature for five mammalian carboxylesterase gene
            families: human, mouse, and rat genes and proteins
  JOURNAL   Mamm Genome 21 (9-10), 427-441 (2010)
   PUBMED   20931200
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Zhang,L., Hu,Z., Zhu,C., Liu,Q., Zhou,Y. and Zhang,Y.
  TITLE     Identification and characterization of an epididymis-specific gene,
            Ces7
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 41 (10), 809-815 (2009)
   PUBMED   19779645
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Zhang,L., Liu,Q., Zhou,Y. and Zhang,Y.
  TITLE     Baculo-expression and enzymatic characterization of CES7 esterase
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 41 (9), 731-736 (2009)
   PUBMED   19727521
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Holmes,R.S., Cox,L.A. and Vandeberg,J.L.
  TITLE     Mammalian carboxylesterase 5: comparative biochemistry and genomics
  JOURNAL   Comp Biochem Physiol Part D Genomics Proteomics 3 (3), 195-204
            (2008)
   PUBMED   19727319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Mar 5, 2021 this sequence version replaced NP_001012056.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF479659.1, SRR26643297.50962.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..575
                     /product="carboxylesterase 5A precursor"
                     /EC_number="3.1.1.1"
                     /note="cauxin; epididymis-specific gene 615 protein;
                     carboxylesterase-like urinary excreted protein homolog;
                     carboxylesterase 7; carboxylesterase 615"
                     /calculated_mol_wt=61218
     sig_peptide     1..28
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5GRG2.1)"
                     /calculated_mol_wt=3129
     mat_peptide     29..575
                     /product="Carboxylesterase 5A. /id=PRO_0000308593"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GRG2.1)"
                     /calculated_mol_wt=61218
     Region          29..539
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(146..148,225..227,230,369,373..374,407,455,458)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(226,345,454)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5GRG2.1)"
     Site            363
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5GRG2.1)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5GRG2.1)"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5GRG2.1)"
     CDS             1..575
                     /gene="Ces5a"
                     /gene_synonym="Ces5; Ces7"
                     /coded_by="NM_001012056.2:142..1869"
                     /db_xref="GeneID:307660"
                     /db_xref="RGD:1549717"
ORIGIN      
        1 msgdwvhtgq aliwvlwifa aiirgsvtee phrytrlgwv qgkqatvlgr lepvnvflgi
       61 pfaapplgpl rfsnpqppip whdlreatty pnvcfqnlew lfiyqnllkv hypklgvsed
      121 clylniyapa yandgsrlpv mmwipgggfe tgsasifdgs alaayedvli vtiqyrlgif
      181 gffntqnqha pgnwafqdql aalqwvreni nyfggnpdsv tifggsagai sisslilspl
      241 saglfhraim qsgvaiipsl knfddelkhg lqvvadvckc nvsdskvllk clreksslel
      301 lslgqktkaf trvvdgsffp eepmellsqk tfktvpsiig vnnqecgyil pmreapeilf
      361 gsnestaltl ihvllhippq ymhivakdyf hgkhsltdir dtlldlfgdv ffvvpglvta
      421 rnhrdaggpv yfyefqhrpn cfqntrpafv kadhtdeirf vfggpflegd vvmfeeated
      481 ekllsrkmms ywanfarsgd pngddlplwp aydqnesylk ldvnistgwr lkdrrvefwt
      541 dtlplitsas kallsptfpl ilfsllppsl lsias
//
