ID   PGRP2_PIG               Reviewed;         598 AA.
AC   Q866Y3; Q866Y4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 101.
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=PGRPL;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RA   Sang Y., Ross C.R., Blecha F.;
RT   "Characterization of porcine peptidoglycan recognition proteins: gene
RT   cloning and regulation on innate immunity.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a scavenger role by digesting biologically active
CC       peptidoglycan (PGN) into biologically inactive fragments. Has no direct
CC       bacteriolytic activity.
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   -!- SUBCELLULAR LOCATION: Secreted. Membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=Q866Y3-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q866Y3-2; Sequence=VSP_009082, VSP_009083;
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF541955; AAO41115.1; -; mRNA.
DR   EMBL; AF541956; AAO41116.1; -; mRNA.
DR   RefSeq; NP_998903.1; NM_213738.1. [Q866Y3-1]
DR   AlphaFoldDB; Q866Y3; -.
DR   SMR; Q866Y3; -.
DR   STRING; 9823.ENSSSCP00000028092; -.
DR   GlyCosmos; Q866Y3; 2 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000022015; -.
DR   PeptideAtlas; Q866Y3; -.
DR   GeneID; 396557; -.
DR   KEGG; ssc:396557; -.
DR   CTD; 114770; -.
DR   eggNOG; ENOG502QR3D; Eukaryota.
DR   InParanoid; Q866Y3; -.
DR   OrthoDB; 2282228at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042834; F:peptidoglycan binding; ISS:UniProtKB.
DR   GO; GO:0016019; F:peptidoglycan immune receptor activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
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.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Secreted;
KW   Signal; Zinc.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..598
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /id="PRO_0000023922"
FT   DOMAIN          428..554
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   REGION          172..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         544
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   BINDING         552
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT   SITE            469
FT                   /note="Important for catalytic activity; essential for
FT                   amidase activity and zinc hydrate coordination"
FT                   /evidence="ECO:0000250|UniProtKB:P00806"
FT   MOD_RES         261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PD5"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        441..447
FT                   /evidence="ECO:0000250|UniProtKB:Q96PD5"
FT   VAR_SEQ         1..346
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_009082"
FT   VAR_SEQ         347..356
FT                   /note="ALTLTPNLTQ -> MDCFCSRSQE (in isoform A)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_009083"
SQ   SEQUENCE   598 AA;  64594 MW;  FCDD237A9F105DDB CRC64;
     MSPGNWKTTM VVRGILLILY GLLLQPEPGT ATLPLLMDSV IQALAELERK SPATEAGHIA
     SMWLLSAQGS GAHNPLPRFL LEGQSLKTAK LAPPSLSPEF QGLIEEVARH GVQDGKEYGV
     VLAPDGSTVA VEPLLAGLEA GLQGHRVVNL PLDSTATFPD IGATVPDLKA TSSAHKDTSA
     DVNSADVGTL SPNVRDTDVD AEVTFLDVRP SSTGVQVTSP DVQVSSPDTK AKSPTTVDSL
     LMVTLARDLG LHFLQGAQTE SNSGLGTEGC WDQLSLPRTF TLLDPEASPL TMAFLNGALD
     GALLGDYLSK VPEPRPPLSH LLNQYYGAGV AGDPGLRSNF RRQNGAALTL TPNLTQQVWG
     TLILLQRLEP AHPQLQGMSQ EQLAQVATHA AKEFTEAFLG CPAIHPRCRW GAAPYRGSPK
     PLKLPLGFLY IHHTYVPARP CTDFALCAAN MRSMQRFHLD TQGWDDIGYS FVVGSDGYVY
     EGRGWHWVGA HTRDHNSRGF GVALIGNYTA ELPSEAALRA VRDELPHCAV RAGLLQPDYA
     LLGHRQLVRT DCPGDALFNM LRTWPRFNMN VKPRTARRAS GRSKRRLPLM IPLATDLQ
//