LOCUS       NP_071587                945 aa            linear   ROD 02-JUN-2024
DEFINITION  glutamyl aminopeptidase [Rattus norvegicus].
ACCESSION   NP_071587 XP_578082
VERSION     NP_071587.2
DBSOURCE    REFSEQ: accession NM_022251.2
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 945)
  AUTHORS   Berillo,O., Ouerd,S., Idris-Khodja,N., Rehman,A., Richer,C.,
            Sinnett,D., Kwitek,A.E., Paradis,P. and Schiffrin,E.L.
  TITLE     Chromosome 2 Fragment Substitutions in Dahl Salt-Sensitive Rats and
            RNA Sequencing Identified Enpep and Hs2st1 as Vascular Inflammatory
            Modulators
  JOURNAL   Hypertension 77 (1), 178-189 (2021)
   PUBMED   33161775
  REMARK    GeneRIF: Chromosome 2 Fragment Substitutions in Dahl Salt-Sensitive
            Rats and RNA Sequencing Identified Enpep and Hs2st1 as Vascular
            Inflammatory Modulators.
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Wangensteen,R., Segarra,A.B., Ramirez-Sanchez,M., Gasparo,M.D.,
            Dominguez,G., Banegas,I., Vargas,F., Vives,F. and Prieto,I.
  TITLE     Influence of thyroid disorders on the kidney expression and plasma
            activity of aminopeptidase A
  JOURNAL   Endocr Regul 49 (2), 68-72 (2015)
   PUBMED   25960007
  REMARK    GeneRIF: A discrepancy between the high expression of AP-A in
            kidney of hyperthyroid rats and the low activity of AP-A measured
            in plasma and kidney of hyperthyroid animals was found.
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Yang,Y., Liu,C., Lin,Y.L. and Li,F.
  TITLE     Structural insights into central hypertension regulation by human
            aminopeptidase A
  JOURNAL   J Biol Chem 288 (35), 25638-25645 (2013)
   PUBMED   23888046
REFERENCE   4  (residues 1 to 945)
  AUTHORS   Ishii,M., Hattori,A., Numaguchi,Y., Ma,X., Nagasaka,T.,
            Tsujimoto,M., Murohara,T., Kobayashi,H. and Mizutani,S.
  TITLE     The effect of recombinant aminopeptidase A (APA) on hypertension in
            pregnant spontaneously hypertensive rats (SHRs)
  JOURNAL   Early Hum Dev 85 (9), 589-594 (2009)
   PUBMED   19608358
REFERENCE   5  (residues 1 to 945)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 945)
  AUTHORS   Troyanovskaya,M., Song,L., Jayaraman,G. and Healy,D.P.
  TITLE     Expression of aminopeptidase A, an angiotensinase, in glomerular
            mesangial cells
  JOURNAL   Hypertension 27 (3 Pt 2), 518-522 (1996)
   PUBMED   8613196
REFERENCE   7  (residues 1 to 945)
  AUTHORS   Wenger,R.H., Kopf,M., Nitschke,L., Lamers,M.C., Kohler,G. and
            Nielsen,P.J.
  TITLE     B-cell maturation in chimaeric mice deficient for the heat stable
            antigen (HSA/mouse CD24)
  JOURNAL   Transgenic Res 4 (3), 173-183 (1995)
   PUBMED   7795661
REFERENCE   8  (residues 1 to 945)
  AUTHORS   Song,L., Ye,M., Troyanovskaya,M., Wilk,E., Wilk,S. and Healy,D.P.
  TITLE     Rat kidney glutamyl aminopeptidase (aminopeptidase A): molecular
            identity and cellular localization
  JOURNAL   Am J Physiol 267 (4 Pt 2), F546-F557 (1994)
   PUBMED   7943354
REFERENCE   9  (residues 1 to 945)
  AUTHORS   Li,L., Wang,J. and Cooper,M.D.
  TITLE     cDNA cloning and expression of human glutamyl aminopeptidase
            (aminopeptidase A)
  JOURNAL   Genomics 17 (3), 657-664 (1993)
   PUBMED   8244382
REFERENCE   10 (residues 1 to 945)
  AUTHORS   Nanus,D.M., Engelstein,D., Gastl,G.A., Gluck,L., Vidal,M.J.,
            Morrison,M., Finstad,C.L., Bander,N.H. and Albino,A.P.
  TITLE     Molecular cloning of the human kidney differentiation antigen
            gp160: human aminopeptidase A
  JOURNAL   Proc Natl Acad Sci U S A 90 (15), 7069-7073 (1993)
   PUBMED   8346219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF146044.1, CK481363.1, BC066663.1, CB747518.1 and AF214568.1.
            
            On Apr 5, 2007 this sequence version replaced NP_071587.1.
            
            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 :: AF214568.1, BC066663.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..945
                     /product="glutamyl aminopeptidase"
                     /EC_number="3.4.11.7"
                     /note="EAP; AP-A; aminopeptidase A"
                     /calculated_mol_wt=107866
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50123.2)"
     Region          45..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50123.2)"
     Region          92..531
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            order(213,215,349..352,385..386,389,408,412,466,471)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Site            213
                     /site_type="other"
                     /note="Binds calcium which modulates its enzyme activity.
                     /evidence=ECO:0000250|UniProtKB:Q07075; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            471
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q07075; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            546
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            584
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            601
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Region          607..925
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
     Site            640
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            669
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            754
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            792
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     CDS             1..945
                     /gene="Enpep"
                     /coded_by="NM_022251.2:422..3259"
                     /db_xref="GeneID:64017"
                     /db_xref="RGD:621228"
ORIGIN      
        1 mnfaeeepsk kycikgkhva iicatvvavg livglsvglt rscepgttpa psnppphtst
       61 alppqdqnvc pdsddesgew knfrlpdfiq pvhydlevkv lmeedrytgi vsisvnlskd
      121 trdlwlhire tritklpelr rpsgeqvpir rcfeykkqey vviqaeedla atsgdsvyrl
      181 tiefegwlng slvgfyrtty tedgqtksia atdheptdar ksfpcfdepn kkatynisli
      241 hpkeysalsn mpvekeetld ndwkkttfmk svpmstylvc favhqftsiq rtsrsgkplt
      301 vyvqpnqkqt aeyaanitka vfdffedyfa meyslpkldk iaipdfgtga menwglvtyr
      361 etnllydpll sassnqqrva svvahelvhq wfgnivtmdw wddlwlnegf asffeflgvn
      421 haeadwqmls qvlledvlpv qeddslmssh pvvvtvstpa eitsvfdgis yskgasilrm
      481 lqdwitpekf qkgcqiylen fkfknaktsd fwdslekasn qpvkevmdtw tsqmgypvvt
      541 vsgkqnvtqk rflldykadp sqppsalgyt wnipikwten gnsnitvyyr snregitlna
      601 nlsgdgflki npdhigfyrv nyeaetwdwi aetlssnhmn fssadrssfi ddafalaraq
      661 lldyekalnl tryltsekdf lpwervisav syiismfedd relypliety frsqvkpiad
      721 slgwqdtgsh itkllrasvl gfackmgage algnasqlfe awlkgnesip vnlrllvyry
      781 gmqnsgneaa wnytleqyqk tslaqekekl lyglasvkdv tllaryleml kdpniiktqd
      841 vftviryisy nsygksmawn wiqlnwdylv nrftindryl grivtiaepf ntelqlwqmq
      901 sffakypnag agakpreqvl etvknniewl klnrksisew ftsmp
//
