ID AMD_BOVIN Reviewed; 972 AA. AC P10731; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 16-MAY-2012, entry version 115. DE RecName: Full=Peptidyl-glycine alpha-amidating monooxygenase; DE Short=PAM; DE Includes: DE RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase; DE Short=PHM; DE EC=1.14.17.3; DE Includes: DE RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; DE EC=4.3.2.5; DE AltName: Full=Peptidylamidoglycolate lyase; DE Short=PAL; DE Flags: Precursor; 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; DOI=10.1021/bi00239a016; 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: Bifunctional enzyme that catalyzes 2 sequential steps in CC C-terminal alpha-amidation of peptides. The monooxygenase part CC produces an unstable peptidyl(2-hydroxyglycine) intermediate that CC is dismutated to glyoxylate and the corresponding desglycine CC peptide amide by the lyase part. C-terminal amidation of peptides CC such as neuropeptides is essential for full biological activity. CC -!- CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O(2) = CC peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. CC -!- CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide + CC glyoxylate. CC -!- COFACTOR: Zinc; for the lyase reaction (By similarity). CC -!- COFACTOR: Binds 2 copper ions per subunit; For the monoxygenase CC reaction (By similarity). CC -!- SUBUNIT: Monomer. Interacts with RASSF9 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle CC membrane; Single-pass membrane protein. Note=Secretory granules. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl- CC alpha-hydroxyglycine alpha-amidating lyase family. CC -!- SIMILARITY: In the N-terminal section; belongs to the copper type CC II ascorbate-dependent 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 IPI; IPI00842571; -. DR PIR; A40063; URBOAP. DR RefSeq; NP_776373.1; NM_173948.2. DR UniGene; Bt.12303; -. DR ProteinModelPortal; P10731; -. DR SMR; P10731; 40-351. DR MINT; MINT-1365422; -. DR STRING; P10731; -. DR PRIDE; P10731; -. DR GeneID; 280890; -. DR KEGG; bta:280890; -. DR CTD; 5066; -. DR eggNOG; COG3391; -. DR HOGENOM; HOG000293368; -. DR HOVERGEN; HBG004218; -. DR InParanoid; P10731; -. DR KO; K00504; -. DR OrthoDB; EOG46MBHT; -. DR NextBio; 20805024; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:EC. DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; IEA:EC. DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro. DR Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1. DR Gene3D; G3DSA:2.60.120.230; Cu2_ascorb_mOase_core; 1. DR Gene3D; G3DSA:2.60.120.310; Cu2_ascorb_mOase_core; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C. DR InterPro; IPR020611; Cu2_ascorb_mOase_CS-1. DR InterPro; IPR014783; Cu2_ascorb_mOase_CS-2. DR InterPro; IPR000323; Cu2_ascorb_mOase_N. DR InterPro; IPR001258; NHL_repeat. DR InterPro; IPR013017; NHL_repeat_subgr. DR InterPro; IPR000720; Pep_amidat_mOase. DR InterPro; IPR008977; PHM/PNGase_F_dom. DR Pfam; PF01082; Cu2_monooxygen; 1. DR Pfam; PF01436; NHL; 4. DR PRINTS; PR00790; PAMONOXGNASE. DR SUPFAM; SSF49742; PHM_PNGase_F; 2. DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1. DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1. DR PROSITE; PS51125; NHL; 5. PE 1: Evidence at protein level; KW Cleavage on pair of basic residues; Complete proteome; Copper; KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Lyase; Membrane; Metal-binding; Monooxygenase; KW Multifunctional enzyme; Oxidoreductase; Phosphoprotein; KW Reference proteome; Repeat; Signal; Sulfation; Transmembrane; KW Transmembrane helix; 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 Helical; (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 1 494 Peptidylglycine alpha-hydroxylating FT monooxygenase (By similarity). FT REGION 495 817 Peptidyl-alpha-hydroxyglycine alpha- FT amidating lyase (By similarity). FT REGION 925 942 Interaction with RASSF9 (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 929 929 Phosphoserine (By similarity). FT MOD_RES 942 942 Phosphoserine (By similarity). FT MOD_RES 946 946 Phosphoserine (By similarity). FT MOD_RES 955 955 Phosphoserine (By similarity). FT MOD_RES 957 957 Phosphoserine (By similarity). FT MOD_RES 961 961 Sulfotyrosine (By similarity). FT CARBOHYD 762 762 N-linked (GlcNAc...) (Potential). FT DISULFID 42 181 By similarity. FT DISULFID 76 121 By similarity. FT DISULFID 109 126 By similarity. FT DISULFID 222 329 By similarity. FT DISULFID 288 310 By similarity. 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 //