LOCUS       NP_037132                976 aa            linear   ROD 01-APR-2024
DEFINITION  peptidylglycine alpha-amidating monooxygenase precursor [Rattus
            norvegicus].
ACCESSION   NP_037132
VERSION     NP_037132.2
DBSOURCE    REFSEQ: accession NM_013000.3
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 976)
  AUTHORS   Rao,V.K.S., Eipper,B.A. and Mains,R.E.
  TITLE     Multiple roles for peptidylglycine alpha-amidating monooxygenase in
            the response to hypoxia
  JOURNAL   J Cell Physiol 236 (11), 7745-7758 (2021)
   PUBMED   34061983
  REMARK    GeneRIF: Multiple roles for peptidylglycine alpha-amidating
            monooxygenase in the response to hypoxia.
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Bonnemaison,M.L., Back,N., Duffy,M.E., Ralle,M., Mains,R.E. and
            Eipper,B.A.
  TITLE     Adaptor Protein-1 Complex Affects the Endocytic Trafficking and
            Function of Peptidylglycine alpha-Amidating Monooxygenase, a
            Luminal Cuproenzyme
  JOURNAL   J Biol Chem 290 (35), 21264-21279 (2015)
   PUBMED   26170456
  REMARK    GeneRIF: Disruption of AP-1-dependent late endosomal trafficking
            diminishes the ability of PAM to retain copper and produce amidated
            peptides.
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Vishwanatha,K., Back,N., Mains,R.E. and Eipper,B.A.
  TITLE     A histidine-rich linker region in peptidylglycine alpha-amidating
            monooxygenase has the properties of a pH sensor
  JOURNAL   J Biol Chem 289 (18), 12404-12420 (2014)
   PUBMED   24627494
  REMARK    GeneRIF: Data indicate that H3A mutation eliminates the ability of
            internalized peptidylglycine alpha-amidating monooxygenase PAM-1 to
            return to secretory granules.
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Rudzka,K., Moreno,D.M., Eipper,B., Mains,R., Estrin,D.A. and
            Amzel,L.M.
  TITLE     Coordination of peroxide to the Cu(M) center of peptidylglycine
            alpha-hydroxylating monooxygenase (PHM): structural and
            computational study
  JOURNAL   J Biol Inorg Chem 18 (2), 223-232 (2013)
   PUBMED   23247335
  REMARK    GeneRIF: The crystal structure of the oxidized form of PHM
            complexed with hydrogen peroxide.
REFERENCE   5  (residues 1 to 976)
  AUTHORS   Francone,V.P., Ifrim,M.F., Rajagopal,C., Leddy,C.J., Wang,Y.,
            Carson,J.H., Mains,R.E. and Eipper,B.A.
  TITLE     Signaling from the secretory granule to the nucleus: Uhmk1 and PAM
  JOURNAL   Mol Endocrinol 24 (8), 1543-1558 (2010)
   PUBMED   20573687
REFERENCE   6  (residues 1 to 976)
  AUTHORS   Maltese,J.Y. and Eipper,B.A.
  TITLE     Developmental expression of peptidylglycine alpha-amidating
            monooxygenase (PAM) in primary cultures of neonatal rat
            cardiocytes: a model for studying regulation of PAM expression in
            the rat heart
  JOURNAL   Mol Endocrinol 6 (12), 1998-2008 (1992)
   PUBMED   1491686
REFERENCE   7  (residues 1 to 976)
  AUTHORS   Ouafik,L.H., Stoffers,D.A., Campbell,T.A., Johnson,R.C.,
            Bloomquist,B.T., Mains,R.E. and Eipper,B.A.
  TITLE     The multifunctional peptidylglycine alpha-amidating monooxygenase
            gene: exon/intron organization of catalytic, processing, and
            routing domains
  JOURNAL   Mol Endocrinol 6 (10), 1571-1584 (1992)
   PUBMED   1448112
REFERENCE   8  (residues 1 to 976)
  AUTHORS   Braas,K.M., Harakall,S.A., Ouafik,L., Eipper,B.A. and May,V.
  TITLE     Expression of peptidylglycine alpha-amidating monooxygenase: an in
            situ hybridization and immunocytochemical study
  JOURNAL   Endocrinology 130 (5), 2778-2788 (1992)
   PUBMED   1572293
REFERENCE   9  (residues 1 to 976)
  AUTHORS   Eipper,B.A., Green,C.B., Campbell,T.A., Stoffers,D.A.,
            Keutmann,H.T., Mains,R.E. and Ouafik,L.
  TITLE     Alternative splicing and endoproteolytic processing generate
            tissue-specific forms of pituitary peptidylglycine alpha-amidating
            monooxygenase (PAM)
  JOURNAL   J Biol Chem 267 (6), 4008-4015 (1992)
   PUBMED   1740449
REFERENCE   10 (residues 1 to 976)
  AUTHORS   Kato,I., Yonekura,H., Tajima,M., Yanagi,M., Yamamoto,H. and
            Okamoto,H.
  TITLE     Two enzymes concerned in peptide hormone alpha-amidation are
            synthesized from a single mRNA
  JOURNAL   Biochem Biophys Res Commun 172 (1), 197-203 (1990)
   PUBMED   1699535
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 4, 2002 this sequence version replaced NP_037132.1.
            
            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 :: M25732.1, SRR26643298.50329.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..976
                     /product="peptidylglycine alpha-amidating monooxygenase
                     precursor"
                     /EC_number="1.14.17.3"
                     /EC_number="4.3.2.5"
                     /note="peptidyl-glycine alpha-amidating monooxygenase;
                     basic salivary proline-rich protein 4-like"
                     /calculated_mol_wt=106153
     Region          1..497
                     /region_name="Peptidylglycine alpha-hydroxylating
                     monooxygenase"
                     /note="propagated from UniProtKB/Swiss-Prot (P14925.1)"
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2541
     mat_peptide     36..976
                     /product="Peptidylglycine alpha-amidating monooxygenase.
                     /id=PRO_0000006366"
                     /note="propagated from UniProtKB/Swiss-Prot (P14925.1)"
                     /calculated_mol_wt=104934
     Region          64..173
                     /region_name="Cu2_monooxygen"
                     /note="Copper type II ascorbate-dependent monooxygenase,
                     N-terminal domain; pfam01082"
                     /db_xref="CDD:460053"
     Region          201..347
                     /region_name="Cu2_monoox_C"
                     /note="Copper type II ascorbate-dependent monooxygenase,
                     C-terminal domain; pfam03712"
                     /db_xref="CDD:461021"
     Region          498..820
                     /region_name="Peptidyl-alpha-hydroxyglycine
                     alpha-amidating lyase.
                     /evidence=ECO:0000269|PubMed:19604476"
                     /note="propagated from UniProtKB/Swiss-Prot (P14925.1)"
     Region          503..810
                     /region_name="NHL_PAL_like"
                     /note="Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
                     (PAL, EC 4.3.2.5); cd14958"
                     /db_xref="CDD:271328"
     Region          517..578
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271328"
     Site            order(520,587,638,787)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:271328"
     Region          584..625
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271328"
     Region          636..674
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271328"
     Region          686..724
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271328"
     Region          732..777
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271328"
     Site            765
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:2211657; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     Site            774
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (P14925.1)"
     Region          783..809
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271328"
     Site            792
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (P14925.1)"
     Site            867..890
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14925.1)"
     Site            921
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19021; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     Region          928..945
                     /region_name="Interaction with RASSF9.
                     /evidence=ECO:0000269|PubMed:9837933"
                     /note="propagated from UniProtKB/Swiss-Prot (P14925.1)"
     Site            932
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19021; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     Region          940..976
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14925.1)"
     Site            945
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     Site            946
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P19021; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     Site            949
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     Site            959
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     Site            961
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P14925.1)"
     CDS             1..976
                     /gene="Pam"
                     /gene_synonym="PHM"
                     /coded_by="NM_013000.3:183..3113"
                     /db_xref="GeneID:25508"
                     /db_xref="RGD:3252"
ORIGIN      
        1 magrarsgll llllgllalq ssclafrspl svfkrfkett rsfsneclgt igpvtpldas
       61 dfaldirmpg vtpkesdtyf cmsmrlpvde eafvidfkpr asmdtvhhml lfgcnmpsst
      121 gsywfcdegt ctdkanilya warnapptrl pkgvgfrvgg etgskyfvlq vhygdisafr
      181 dnhkdcsgvs vhltrvpqpl iagmylmmsv dtvippgekv vnadiscqyk mypmhvfayr
      241 vhthhlgkvv sgyrvrngqw tligrqnpql pqafypvehp vdvtfgdila arcvftgegr
      301 teathiggts sdemcnlyim yymeakyals fmtctknvap dmfrtipaea nipipvkpdm
      361 vmmhghhkea enkeksalmq qpkqgeeevl eqgdfyslls kllgeredvh vhkynptekt
      421 esgsdlvaei anvvqkkdlg rsdaregaeh eewgnailvr drihrfhqle stlrpaesra
      481 fsfqqpgegp wepepsgdfh veeeldwpgv yllpgqvsgv aldsknnlvi fhrgdhvwdg
      541 nsfdskfvyq qrglgpieed tilvidpnna eilqssgknl fylphglsid tdgnywvtdv
      601 alhqvfkldp hskegpllil grsmqpgsdq nhfcqptdva vepstgavfv sdgycnsriv
      661 qfspsgkfvt qwgeessgss prpgqfsvph slalvphldq lcvadrengr iqcfktdtke
      721 fvreikhasf grnvfaisyi pgflfavngk pyfgdqepvq gfvmnfssge iidvfkpvrk
      781 hfdmphdiva sedgtvyigd ahtntvwkft ltekmehrsv kkagievqei keaeavvepk
      841 venkptssel qkmqekqkls tepgsgvsvv littllvipv lvllaivmfi rwkksrafgd
      901 hdrklesssg rvlgrfrgkg sgglnlgnff asrkgysrkg fdrvstegsd qekdeddgte
      961 seeeysaplp kpapss
//
