ID AMD_BOVIN STANDARD; PRT; 972 AA. AC P10731; DT 01-JUL-1989 (Rel. 11, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 07-FEB-2006 (Rel. 49, Last annotation update) DE Peptidyl-glycine alpha-amidating monooxygenase precursor DE (EC 1.14.17.3) (PAM). GN Name=PAM; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Pituitary; RX MEDLINE=91042563; PubMed=3153462; RA Eipper B.A., Park L.P., Dickerson I.M., Keutmann H.T., Thiele E.A., RA Rodriguez H., Schofield P.R., Mains R.E.; RT "Structure of the precursor to an enzyme mediating COOH-terminal RT amidation in peptide biosynthesis."; RL Mol. Endocrinol. 1:777-790(1987). RN [2] RP PROTEIN SEQUENCE OF 478-499; 544-575; 611-630 AND 665-695, FUNCTION, RP AND SUBCELLULAR LOCATION. RX MEDLINE=91283459; PubMed=2059626; RA Katopodis A.G., Ping D.S., Smith C.E., May S.W.; RT "Functional and structural characterization of peptidylamidoglycolate RT lyase, the enzyme catalyzing the second step in peptide amidation."; RL Biochemistry 30:6189-6194(1991). CC -!- FUNCTION: C-terminal alpha-amidation of peptides. The reaction CC produces a peptidyl(2-hydroxyglycine) intermediate is unstable and CC dismutates to glyoxylate and the corresponding desglycine peptide CC amide. CC -!- CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O(2) = CC peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. CC -!- COFACTOR: Binds 2 copper ions per subunit. CC -!- SUBCELLULAR LOCATION: Secretory granules. CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent CC monooxygenase family. CC -!- SIMILARITY: Contains 5 NHL repeats. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M18683; AAA30683.1; -; mRNA. DR PIR; A40063; URBOAP. DR HSSP; P14925; 3PHM. DR SMR; P10731; 40-351. DR InterPro; IPR000323; Cu2_ascorb_mOase. DR InterPro; IPR001258; NHL. DR InterPro; IPR013017; NHL_rep. DR InterPro; IPR000720; Pep_amidat_mOase. DR Pfam; PF03712; Cu2_monoox_C; 1. DR Pfam; PF01082; Cu2_monooxygen; 1. DR Pfam; PF01436; NHL; 4. DR PRINTS; PR00790; PAMONOXGNASE. DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1. DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1. DR PROSITE; PS51125; NHL; 5. KW Copper; Direct protein sequencing; Glycoprotein; Membrane; KW Metal-binding; Monooxygenase; Oxidoreductase; Phosphorylation; Repeat; KW Signal; Sulfation; Transmembrane; Vitamin C; Zinc. FT SIGNAL 1 20 Potential. FT PROPEP 21 30 Potential. FT /FTId=PRO_0000006359. FT CHAIN 31 972 Peptidyl-glycine alpha-amidating FT monooxygenase. FT /FTId=PRO_0000006360. FT TOPO_DOM 31 873 Intragranular (Potential). FT TRANSMEM 874 897 Potential. FT TOPO_DOM 898 972 Cytoplasmic (Potential). FT REPEAT 498 541 NHL 1. FT REPEAT 567 608 NHL 2. FT REPEAT 617 662 NHL 3. FT REPEAT 670 714 NHL 4. FT REPEAT 766 809 NHL 5. FT REGION 495 817 Catalytic core (By similarity). FT METAL 102 102 Copper A (By similarity). FT METAL 103 103 Copper A (By similarity). FT METAL 167 167 Copper A (By similarity). FT METAL 237 237 Copper B (By similarity). FT METAL 239 239 Copper B (By similarity). FT METAL 309 309 Copper B (By similarity). FT MOD_RES 961 961 Sulfotyrosine (By similarity). FT CARBOHYD 762 762 N-linked (GlcNAc...) (Potential). FT DISULFID 631 652 By similarity. FT DISULFID 699 710 By similarity. SQ SEQUENCE 972 AA; 108177 MW; EBD41F83E341BAF1 CRC64; MAGFRSLLVL LLVFPSGCVG FRSPLSVFKR FKETTRSFSN ECLGTTRPVI PIDSSDFALD IRMPGVTPKQ SDTYFCMSVR LPMDEEAFVI DFKPRASMDT VHHMLLFGCN MPASTGNYWF CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNHKD CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP PGGKVVNSDI SCHYKKYPMH VFAYRVHTHH LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVEHPVDVSF GDILAARCVF TGEGRTEVTH IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDIFRT IPPEANIPIP VKSDMVMMHG HHKETENKDK TSLLQQPKRE EEGVLEQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES DLVAEIANVV QKKDLGRSDT RESAEQERGN AILVRDRIHK FHRLVSTLRP AESRVLSLQQ PLPGEGTWEP EHTGDFHVEE ALDWPGVYLL PGQVSGVALD PQNNLVIFHR GDHVWDGNSF DSKFVYQQRG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH QVFKLDPKSK EGPLLTLGRS MQPGSDQNHF CQPTDVAVDP DTGTIYVSDG YCNSRLVQFS PSGKFITQWG EASLESSPKP GQFRVPHSLA LVPPLGQLCV ADRENGRIQC FKTDTKEFVR EIKHPSFGRN VFAISYIPGL LFAVNGKPYF EDQEPVQGFV MNFSSGEIID VFKPVRKHFD MPHDIAASED GTVYVGDAHT NTVWKFTSTE KMEHRSVKKA GIEVQEIKES EAVVETKMEN KPASSELQKI QEKQKLVKEP GSGVPAVLIT TLLVIPVVVL LAIALFIRWK KSRAFGDSER KLEASSGRVL GRLRGKGGGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK DEDASESEEE YSAPPPAPAP SS //