ID PGRP2_HUMAN Reviewed; 576 AA. AC Q96PD5; A8K050; A8K8C7; B2RMZ2; B7ZM33; Q68CK1; Q96N74; Q9UC60; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 182. DE RecName: Full=N-acetylmuramoyl-L-alanine amidase; DE EC=3.5.1.28; DE AltName: Full=Peptidoglycan recognition protein 2; DE AltName: Full=Peptidoglycan recognition protein long; DE Short=PGRP-L; DE Flags: Precursor; GN Name=PGLYRP2; Synonyms=PGLYRPL, PGRPL; ORFNames=UNQ3103/PRO10102; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=11461926; DOI=10.1074/jbc.m105566200; RA Liu C., Xu Z., Gupta D., Dziarski R.; RT "Peptidoglycan recognition proteins: a novel family of four human innate RT immunity pattern recognition molecules."; RL J. Biol. Chem. 276:34686-34694(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-394. RX PubMed=15221005; DOI=10.1038/sj.onc.1207782; RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.; RT "Expression profiling and differential screening between hepatoblastomas RT and the corresponding normal livers: identification of high expression of RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."; RL Oncogene 23:5901-5911(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-46; RP GLN-99; LYS-270 AND GLN-394. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver, Mammary gland, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 22-36. RX PubMed=7663175; DOI=10.1006/prep.1995.1049; RA De Pauw P., Neyt C., Vanderwinkel E., Wattiez R., Falmagne P.; RT "Characterization of human serum N-acetylmuramyl-L-alanine amidase purified RT by affinity chromatography."; RL Protein Expr. Purif. 6:371-378(1995). RN [8] RP PROTEIN SEQUENCE OF 22-36. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, PHOSPHORYLATION AT RP SER-239, DEAMIDATION AT ASN-274 AND ASN-322, AND DISULFIDE BONDS. RC TISSUE=Liver, and Serum; RX PubMed=16054449; DOI=10.1016/j.bbapap.2005.07.001; RA Zhang Y., van der Fits L., Voerman J.S., Melief M.-J., Laman J.D., Wang M., RA Wang H., Wang M., Li X., Walls C.D., Gupta D., Dziarski R.; RT "Identification of serum N-acetylmuramoyl-l-alanine amidase as liver RT peptidoglycan recognition protein 2."; RL Biochim. Biophys. Acta 1752:34-46(2005). RN [10] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF HIS-411; RP CYS-419; HIS-436; TRP-442 AND CYS-530. RX PubMed=14506276; DOI=10.1074/jbc.m307758200; RA Wang Z.-M., Li X., Cocklin R.R., Wang M., Wang M., Fukase K., Inamura S., RA Kusumoto S., Gupta D., Dziarski R.; RT "Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine RT amidase."; RL J. Biol. Chem. 278:49044-49052(2003). RN [11] RP GLYCOSYLATION AT ASN-485. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77; ASN-367 AND ASN-485. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367 AND ASN-485. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). CC -!- FUNCTION: May play a scavenger role by digesting biologically active CC peptidoglycan (PGN) into biologically inactive fragments. Has no direct CC bacteriolytic activity. {ECO:0000269|PubMed:14506276}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L- CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P00806}; CC -!- INTERACTION: CC Q96PD5-2; O43765: SGTA; NbExp=3; IntAct=EBI-12758027, EBI-347996; CC -!- SUBCELLULAR LOCATION: Secreted. Membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96PD5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96PD5-2; Sequence=VSP_008964; CC -!- TISSUE SPECIFICITY: Strongly expressed in liver and fetal liver, and CC secreted into serum. Expressed to a much lesser extent in transverse CC colon, lymph nodes, heart, thymus, pancreas, descending colon, stomach CC and testis. Isoform 2 is not detected in the liver or serum. CC {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:16054449}. CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. CC {ECO:0000305}. 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; AF384856; AAL05629.1; -; mRNA. DR EMBL; AB073610; BAD38647.1; -; mRNA. DR EMBL; AY358156; AAQ88523.1; -; mRNA. DR EMBL; AK055882; BAB71034.1; -; mRNA. DR EMBL; AK289415; BAF82104.1; -; mRNA. DR EMBL; AK292292; BAF84981.1; -; mRNA. DR EMBL; CH471106; EAW84482.1; -; Genomic_DNA. DR EMBL; CH471106; EAW84483.1; -; Genomic_DNA. DR EMBL; BC136551; AAI36552.1; -; mRNA. DR EMBL; BC136552; AAI36553.1; -; mRNA. DR EMBL; BC144238; AAI44239.1; -; mRNA. DR CCDS; CCDS12330.2; -. [Q96PD5-1] DR CCDS; CCDS86718.1; -. [Q96PD5-2] DR RefSeq; NP_443122.3; NM_052890.3. [Q96PD5-1] DR RefSeq; XP_006722696.1; XM_006722633.3. DR AlphaFoldDB; Q96PD5; -. DR SMR; Q96PD5; -. DR BioGRID; 125340; 2. DR IntAct; Q96PD5; 3. DR STRING; 9606.ENSP00000292609; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR GlyConnect; 784; 8 N-Linked glycans (3 sites), 1 O-Linked glycan (1 site). DR GlyCosmos; Q96PD5; 10 sites, 12 glycans. DR GlyGen; Q96PD5; 11 sites, 12 N-linked glycans (3 sites), 5 O-linked glycans (8 sites). DR iPTMnet; Q96PD5; -. DR PhosphoSitePlus; Q96PD5; -. DR BioMuta; PGLYRP2; -. DR DMDM; 38258222; -. DR jPOST; Q96PD5; -. DR MassIVE; Q96PD5; -. DR PaxDb; 9606-ENSP00000345968; -. DR PeptideAtlas; Q96PD5; -. DR ProteomicsDB; 77669; -. [Q96PD5-1] DR ProteomicsDB; 77670; -. [Q96PD5-2] DR Antibodypedia; 43600; 107 antibodies from 23 providers. DR DNASU; 114770; -. DR Ensembl; ENST00000292609.8; ENSP00000292609.3; ENSG00000161031.13. [Q96PD5-2] DR Ensembl; ENST00000340880.5; ENSP00000345968.4; ENSG00000161031.13. [Q96PD5-1] DR GeneID; 114770; -. DR KEGG; hsa:114770; -. DR MANE-Select; ENST00000340880.5; ENSP00000345968.4; NM_052890.4; NP_443122.3. DR UCSC; uc002nbf.5; human. [Q96PD5-1] DR AGR; HGNC:30013; -. DR CTD; 114770; -. DR DisGeNET; 114770; -. DR GeneCards; PGLYRP2; -. DR HGNC; HGNC:30013; PGLYRP2. DR HPA; ENSG00000161031; Tissue enriched (liver). DR MIM; 608199; gene. DR neXtProt; NX_Q96PD5; -. DR OpenTargets; ENSG00000161031; -. DR PharmGKB; PA134929965; -. DR VEuPathDB; HostDB:ENSG00000161031; -. DR eggNOG; ENOG502QR3D; Eukaryota. DR GeneTree; ENSGT00940000158718; -. DR HOGENOM; CLU_038892_0_0_1; -. DR InParanoid; Q96PD5; -. DR OMA; TLTQQVW; -. DR OrthoDB; 2282228at2759; -. DR PhylomeDB; Q96PD5; -. DR TreeFam; TF323898; -. DR BRENDA; 3.5.1.28; 2681. DR PathwayCommons; Q96PD5; -. DR Reactome; R-HSA-6803157; Antimicrobial peptides. DR SignaLink; Q96PD5; -. DR BioGRID-ORCS; 114770; 12 hits in 1143 CRISPR screens. DR ChiTaRS; PGLYRP2; human. DR GeneWiki; PGLYRP2; -. DR GenomeRNAi; 114770; -. DR Pharos; Q96PD5; Tbio. DR PRO; PR:Q96PD5; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q96PD5; Protein. DR Bgee; ENSG00000161031; Expressed in right lobe of liver and 42 other cell types or tissues. DR ExpressionAtlas; Q96PD5; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:CACAO. DR GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB. DR GO; GO:0016019; F:peptidoglycan immune receptor activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0051701; P:biological process involved in interaction with host; IEA:Ensembl. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB. DR GO; GO:0016045; P:detection of bacterium; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB. DR GO; GO:0032827; P:negative regulation of natural killer cell differentiation involved in immune response; IEA:Ensembl. DR GO; GO:0032689; P:negative regulation of type II interferon production; IEA:Ensembl. DR GO; GO:0001519; P:peptide amidation; NAS:UniProtKB. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl. DR CDD; cd06583; PGRP; 1. DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1. DR InterPro; IPR036505; Amidase/PGRP_sf. DR InterPro; IPR002502; Amidase_domain. DR InterPro; IPR015510; PGRP. DR InterPro; IPR006619; PGRP_domain_met/bac. DR PANTHER; PTHR11022:SF66; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1. DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1. DR Pfam; PF01510; Amidase_2; 1. DR SMART; SM00644; Ami_2; 1. DR SMART; SM00701; PGRP; 1. DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1. DR Genevisible; Q96PD5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Hydrolase; Immunity; Membrane; Metal-binding; Phosphoprotein; KW Reference proteome; Secreted; Signal; Zinc. FT SIGNAL 1..21 FT /evidence="ECO:0000269|PubMed:15340161, FT ECO:0000269|PubMed:7663175" FT CHAIN 22..576 FT /note="N-acetylmuramoyl-L-alanine amidase" FT /id="PRO_0000023920" FT DOMAIN 406..532 FT /note="N-acetylmuramoyl-L-alanine amidase" FT /evidence="ECO:0000255" FT REGION 550..576 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 410 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8INK6" FT BINDING 522 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8INK6" FT BINDING 530 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8INK6" FT SITE 447 FT /note="Important for catalytic activity; essential for FT amidase activity and zinc hydrate coordination" FT /evidence="ECO:0000250|UniProtKB:P00806" FT MOD_RES 239 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16054449" FT MOD_RES 274 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:16054449" FT MOD_RES 322 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:16054449" FT CARBOHYD 77 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 367 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 485 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218" FT DISULFID 419..425 FT /evidence="ECO:0000269|PubMed:16054449" FT VAR_SEQ 548..576 FT /note="TVKPRPARSVSKRSRREPPPRTLPATDLQ -> VSLRSLHYTARRPSVYTSS FT TRPLPPACNSCARTASARPPTSRRHVYSGNLGPAFAGHSAGNIPDPVTSAYAASAQPQT FT QPACPFPSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_008964" FT VARIANT 46 FT /note="T -> A (in dbSNP:rs3813135)" FT /evidence="ECO:0000269|PubMed:12975309" FT /id="VAR_050498" FT VARIANT 99 FT /note="R -> Q (in dbSNP:rs733731)" FT /evidence="ECO:0000269|PubMed:12975309" FT /id="VAR_050499" FT VARIANT 257 FT /note="T -> N (in dbSNP:rs28404490)" FT /id="VAR_050500" FT VARIANT 270 FT /note="M -> K (in dbSNP:rs892145)" FT /evidence="ECO:0000269|PubMed:12975309" FT /id="VAR_050501" FT VARIANT 394 FT /note="R -> Q (in dbSNP:rs34440547)" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:15221005" FT /id="VAR_055231" FT VARIANT 476 FT /note="R -> W (in dbSNP:rs2304200)" FT /id="VAR_050502" FT MUTAGEN 411 FT /note="H->A: No effect on amidase activity." FT /evidence="ECO:0000269|PubMed:14506276" FT MUTAGEN 419 FT /note="C->A: Abolishes amidase activity." FT /evidence="ECO:0000269|PubMed:14506276" FT MUTAGEN 436 FT /note="H->A: No effect on amidase activity." FT /evidence="ECO:0000269|PubMed:14506276" FT MUTAGEN 442 FT /note="W->A: Reduced amidase activity." FT /evidence="ECO:0000269|PubMed:14506276" FT MUTAGEN 447 FT /note="Y->A: Abolishes amidase activity." FT MUTAGEN 530 FT /note="C->S: Abolishes amidase activity." FT /evidence="ECO:0000269|PubMed:14506276" FT CONFLICT 124 FT /note="L -> P (in Ref. 6; AAI44239)" FT /evidence="ECO:0000305" FT CONFLICT 448 FT /note="S -> G (in Ref. 4; BAB71034)" FT /evidence="ECO:0000305" FT CONFLICT 562 FT /note="R -> G (in Ref. 4; BAF82104)" FT /evidence="ECO:0000305" SQ SEQUENCE 576 AA; 62217 MW; 73EA8713DC54F85A CRC64; MAQGVLWILL GLLLWSDPGT ASLPLLMDSV IQALAELEQK VPAAKTRHTA SAWLMSAPNS GPHNRLYHFL LGAWSLNATE LDPCPLSPEL LGLTKEVARH DVREGKEYGV VLAPDGSTVA VEPLLAGLEA GLQGRRVINL PLDSMAAPWE TGDTFPDVVA IAPDVRATSS PGLRDGSPDV TTADIGANTP DATKGCPDVQ ASLPDAKAKS PPTMVDSLLA VTLAGNLGLT FLRGSQTQSH PDLGTEGCWD QLSAPRTFTL LDPKASLLTM AFLNGALDGV ILGDYLSRTP EPRPSLSHLL SQYYGAGVAR DPGFRSNFRR QNGAALTSAS ILAQQVWGTL VLLQRLEPVH LQLQCMSQEQ LAQVAANATK EFTEAFLGCP AIHPRCRWGA APYRGRPKLL QLPLGFLYVH HTYVPAPPCT DFTRCAANMR SMQRYHQDTQ GWGDIGYSFV VGSDGYVYEG RGWHWVGAHT LGHNSRGFGV AIVGNYTAAL PTEAALRTVR DTLPSCAVRA GLLRPDYALL GHRQLVRTDC PGDALFDLLR TWPHFTATVK PRPARSVSKR SRREPPPRTL PATDLQ //