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 28-FEB-2003 (Rel. 41, Last annotation update) DE Peptidyl-glycine alpha-amidating monooxygenase precursor DE (EC 1.14.17.3) (PAM). GN PAM. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL 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). 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: Copper and ascorbate. CC -!- SUBCELLULAR LOCATION: Secretory granules. CC -!- SIMILARITY: Belongs to the copper type II, ascorbate-dependent CC monooxygenase family. 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; -. DR PIR; A40063; URBOAP. DR HSSP; P14925; 1PHM. DR InterPro; IPR000323; Cu2_monooxygnse. DR InterPro; IPR001258; NHL. DR InterPro; IPR000720; Pamonoxygenase. DR InterPro; IPR008977; PHM_PNGase_F. 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. KW Oxidoreductase; Monooxygenase; Copper; Vitamin C; Transmembrane; KW Glycoprotein; Phosphorylation; Sulfation; Signal; Zinc. FT SIGNAL 1 20 Potential. FT PROPEP 21 30 Potential. FT CHAIN 31 972 Peptidyl-glycine alpha-amidating FT monooxygenase. FT DOMAIN 31 873 INTRAGRANULAR (POTENTIAL). FT TRANSMEM 874 897 Potential. FT DOMAIN 898 972 Cytoplasmic (Potential). FT DOMAIN 495 817 CATALYTIC CORE (BY SIMILARITY). FT METAL 237 237 Copper (Potential). FT METAL 239 239 Copper (Potential). FT METAL 240 240 Copper (Potential). FT METAL 359 359 Copper (Potential). FT METAL 361 361 Copper (Potential). FT METAL 362 362 Copper (Potential). FT DISULFID 631 652 By similarity. FT DISULFID 699 710 By similarity. FT MOD_RES 961 961 SULFATION (BY SIMILARITY). FT CARBOHYD 762 762 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 972 AA; 108176 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 //