LOCUS NP_000910 974 aa linear PRI 24-OCT-2008
DEFINITION peptidylglycine alpha-amidating monooxygenase isoform a
preproprotein [Homo sapiens].
ACCESSION NP_000910
VERSION NP_000910.2 GI:21070984
DBSOURCE REFSEQ: accession NM_000919.2
KEYWORDS .
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 974)
AUTHORS Olsen,J.V., Blagoev,B., Gnad,F., Macek,B., Kumar,C., Mortensen,P.
and Mann,M.
TITLE Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks
JOURNAL Cell 127 (3), 635-648 (2006)
PUBMED 17081983
REFERENCE 2 (residues 1 to 974)
AUTHORS Brenet,F., Dussault,N., Borch,J., Ferracci,G., Delfino,C.,
Roepstorff,P., Miquelis,R. and Ouafik,L.
TITLE Mammalian peptidylglycine alpha-amidating monooxygenase mRNA
expression can be modulated by the La autoantigen
JOURNAL Mol. Cell. Biol. 25 (17), 7505-7521 (2005)
PUBMED 16107699
REMARK GeneRIF: nuclear retention of PAM mRNA is lost upon expressing the
La proteins that lack a conserved nuclear retention element,
suggesting a direct association between PAM mRNA and La protein in
vivo
REFERENCE 3 (residues 1 to 974)
AUTHORS Satani,M., Takahashi,K., Sakamoto,H., Harada,S., Kaida,Y. and
Noguchi,M.
TITLE Expression and characterization of human bifunctional
peptidylglycine alpha-amidating monooxygenase
JOURNAL Protein Expr. Purif. 28 (2), 293-302 (2003)
PUBMED 12699694
REFERENCE 4 (residues 1 to 974)
AUTHORS Garmendia,O., Rodriguez,M.P., Burrell,M.A. and Villaro,A.C.
TITLE Immunocytochemical finding of the amidating enzymes in mouse
pancreatic A-, B-, and D-cells: a comparison with human and rat
JOURNAL J. Histochem. Cytochem. 50 (10), 1401-1416 (2002)
PUBMED 12364573
REFERENCE 5 (residues 1 to 974)
AUTHORS Jimenez,N., Jongsma,J., Calvo,A., van der Kwast,T.H., Treston,A.M.,
Cuttitta,F., Schroder,F.H., Montuenga,L.M. and van Steenbrugge,G.J.
TITLE Peptidylglycine alpha-amidating monooxygenase- and
proadrenomedullin-derived peptide-associated neuroendocrine
differentiation are induced by androgen deprivation in the
neoplastic prostate
JOURNAL Int. J. Cancer 94 (1), 28-34 (2001)
PUBMED 11668475
REFERENCE 6 (sites)
AUTHORS Caldwell,B.D., Darlington,D.N., Penzes,P., Johnson,R.C.,
Eipper,B.A. and Mains,R.E.
TITLE The novel kinase peptidylglycine alpha-amidating monooxygenase
cytosolic interactor protein 2 interacts with the cytosolic routing
determinants of the peptide processing enzyme peptidylglycine
alpha-amidating monooxygenase
JOURNAL J. Biol. Chem. 274 (49), 34646-34656 (1999)
PUBMED 10574929
REFERENCE 7 (sites)
AUTHORS Yun,H.Y., Milgram,S.L., Keutmann,H.T. and Eipper,B.A.
TITLE Phosphorylation of the cytosolic domain of peptidylglycine
alpha-amidating monooxygenase
JOURNAL J. Biol. Chem. 270 (50), 30075-30083 (1995)
PUBMED 8530412
REFERENCE 8 (residues 1 to 974)
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 9 (residues 1 to 974)
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 10 (residues 1 to 974)
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 11 (residues 1 to 974)
AUTHORS Glauder,J., Ragg,H., Rauch,J. and Engels,J.W.
TITLE Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning
and functional expression of a truncated form in COS cells
JOURNAL Biochem. Biophys. Res. Commun. 169 (2), 551-558 (1990)
PUBMED 2357221
REFERENCE 12 (residues 1 to 974)
AUTHORS Roberts,A.N., Leighton,B., Todd,J.A., Cockburn,D., Schofield,P.N.,
Sutton,R., Holt,S., Boyd,Y., Day,A.J., Foot,E.A. et al.
TITLE Molecular and functional characterization of amylin, a peptide
associated with type 2 diabetes mellitus
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 86 (24), 9662-9666 (1989)
PUBMED 2690069
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from M37721.1 and BC018127.1.
On May 22, 2002 this sequence version replaced gi:4505603.
Summary: This gene encodes a multifunctional protein. It has two
enzymatically active domains with catalytic activities -
peptidylglycine alpha-hydroxylating monooxygenase (PHM) and
peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). These
catalytic domains work sequentially to catalyze neuroendocrine
peptides to active alpha-amidated products. Multiple alternatively
spliced transcript variants encoding different isoforms have been
described for this gene but some of their full length sequences are
not yet known. [provided by RefSeq].
Transcript Variant: This variant (1) encodes the longest isoform.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..974
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="5"
/map="5q14-q21"
Protein 1..974
/product="peptidylglycine alpha-amidating monooxygenase
isoform a preproprotein"
/EC_number="1.14.17.3"
/EC_number="4.3.2.5"
/note="peptidyl alpha-amidating enzyme; peptidylglycine
2-hydroxylase; peptidylglycine alpha-hydroxylating
monooxygenase; peptidyl-alpha-hydroxyglycine
alpha-amidating lyase; pancreatic peptidylglycine
alpha-amidating monooxygenase"
/calculated_mol_wt=108273
Site 930
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[7]
/db_xref="HPRD:01498"
Site 935
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[7]
/db_xref="HPRD:01498"
Site 947
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/citation=[6]
/db_xref="HPRD:12318"
CDS 1..974
/gene="PAM"
/gene_synonym="PAL"
/gene_synonym="PHM"
/coded_by="NM_000919.2:374..3298"
/note="isoform a preproprotein is encoded by transcript
variant 1"
/db_xref="CCDS:CCDS43348.1"
/db_xref="GeneID:5066"
/db_xref="HGNC:8596"
/db_xref="HPRD:01361"
/db_xref="MIM:170270"
ORIGIN
1 magrvpsllv llvfpsscla frsplsvfkr fkettrpfsn eclgttrpvv pidssdfald
61 irmpgvtpkq sdtyfcmsmr ipvdeeafvi dfkprasmdt vhhmllfgcn mpsstgsywf
121 cdegtctdka nilyawarna pptrlpkgvg frvggetgsk yfvlqvhygd isafrdnnkd
181 csgvslhltr lpqpliagmy lmmsvdtvip agekvvnsdi schyknypmh vfayrvhthh
241 lgkvvsgyrv rngqwtligr qspqlpqafy pvghpvdvsf gdllaarcvf tgegrteath
301 iggtssdemc nlyimyymea khavsfmtct qnvapdmfrt ippeanipip vksdmvmmhe
361 hhketeykdk ipllqqpkre eeevldqgdf ysllskllge redvvhvhky nptekaeses
421 dlvaeianvv qkkdlgrsda regaehergn ailvrdrihk fhrlvstlrp pesrvfslqq
481 pppgegtwep ehtgdfhmee aldwpgvyll pgqvsgvald pknnlvifhr gdhvwdgnsf
541 dskfvyqqig lgpieedtil vidpnnaavl qssgknlfyl phglsidkdg nywvtdvalh
601 qvfkldpnnk egpvlilgrs mqpgsdqnhf cqptdvavdp gtgaiyvsdg ycnsrivqfs
661 psgkfitqwg eessgssplp gqftvphsla lvpllgqlcv adrengriqc fktdtkefvr
721 eikhssfgrn vfaisyipgl lfavngkphf gdqepvqgfv mnfsngeiid ifkpvrkhfd
781 mphdivased gtvyigdaht ntvwkftlte klehrsvkka gievqeikea eavvetkmen
841 kptsselqkm qekqklikep gsgvpvvlit tllvipvvvl laiaifirwk ksrafgadse
901 hkletssgrv lgrfrgkgsg glnlgnffas rkgysrkgfd rlstegsdqe keddgsesee
961 eysaplpala psss
//