PGRP2_PIG
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 03-AUG-2022, entry version 96.
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.ENSSSCP00000022015; -.
DR PaxDb; Q866Y3; -.
DR PeptideAtlas; Q866Y3; -.
DR PRIDE; Q866Y3; -.
DR GeneID; 396557; -.
DR KEGG; ssc:396557; -.
DR CTD; 114770; -.
DR eggNOG; ENOG502QR3D; Eukaryota.
DR InParanoid; Q866Y3; -.
DR OrthoDB; 1110472at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; -; 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; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 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
