N-acetylmuramoyl-L-alanine amidase precursor

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Sites

Amino acid modifications

Natural variations

Preferred order of sections

Molecule processing

Sites

Amino acid modifications

Natural variations

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

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Q866Y3 (PGRP2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Protein names

Recommended name:
N-acetylmuramoyl-L-alanine amidase
EC=3.5.1.28

Alternative name(s):
Peptidoglycan recognition protein 2
Peptidoglycan recognition protein long
Short name=PGRP-L

Gene names

Name:	PGLYRP2
Synonyms:	PGRPL

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Sequence length	598 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

Function	May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity.
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Cofactor	Zinc By similarity.
Subcellular location	Secreted. Membrane.
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Keywords
Biological process	Immunity
Cellular component	Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to Gram-positive bacterium Inferred from sequence or structural similarity. Source: UniProtKB detection of bacterium Inferred from sequence or structural similarity. Source: UniProtKB peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC peptidoglycan binding Inferred from sequence or structural similarity. Source: UniProtKB peptidoglycan receptor activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Signal peptide

1 – 31

Potential

Chain

32 – 598

567

N-acetylmuramoyl-L-alanine amidase

PRO_0000023922

Metal binding

433

Zinc By similarity

Metal binding

469

Zinc By similarity

Metal binding

544

Zinc By similarity

Metal binding

552

Zinc By similarity

Modified residue

261

Phosphoserine By similarity

Glycosylation

353

N-linked (GlcNAc...) Potential

Glycosylation

507

N-linked (GlcNAc...) By similarity

Disulfide bond

441 ↔ 447

By similarity

Alternative sequence

1 – 346

346

Missing in isoform A.

VSP_009082

Alternative sequence

347 – 356

ALTLTPNLTQ → MDCFCSRSQE in isoform A.

VSP_009083

Sequence		Length	Mass (Da)
Isoform B [UniParc]. Last modified June 1, 2003. Version 1. Checksum: FCDD237A9F105DDB Show »	FASTA	598	64,594
10 20 30 40 50 60 MSPGNWKTTM VVRGILLILY GLLLQPEPGT ATLPLLMDSV IQALAELERK SPATEAGHIA 70 80 90 100 110 120 SMWLLSAQGS GAHNPLPRFL LEGQSLKTAK LAPPSLSPEF QGLIEEVARH GVQDGKEYGV 130 140 150 160 170 180 VLAPDGSTVA VEPLLAGLEA GLQGHRVVNL PLDSTATFPD IGATVPDLKA TSSAHKDTSA 190 200 210 220 230 240 DVNSADVGTL SPNVRDTDVD AEVTFLDVRP SSTGVQVTSP DVQVSSPDTK AKSPTTVDSL 250 260 270 280 290 300 LMVTLARDLG LHFLQGAQTE SNSGLGTEGC WDQLSLPRTF TLLDPEASPL TMAFLNGALD 310 320 330 340 350 360 GALLGDYLSK VPEPRPPLSH LLNQYYGAGV AGDPGLRSNF RRQNGAALTL TPNLTQQVWG 370 380 390 400 410 420 TLILLQRLEP AHPQLQGMSQ EQLAQVATHA AKEFTEAFLG CPAIHPRCRW GAAPYRGSPK 430 440 450 460 470 480 PLKLPLGFLY IHHTYVPARP CTDFALCAAN MRSMQRFHLD TQGWDDIGYS FVVGSDGYVY 490 500 510 520 530 540 EGRGWHWVGA HTRDHNSRGF GVALIGNYTA ELPSEAALRA VRDELPHCAV RAGLLQPDYA 550 560 570 580 590 LLGHRQLVRT DCPGDALFNM LRTWPRFNMN VKPRTARRAS GRSKRRLPLM IPLATDLQ « Hide
Isoform A [UniParc]. Checksum: 365F34308D2E3560 Show »	FASTA	252	28,393
10 20 30 40 50 60 MDCFCSRSQE QVWGTLILLQ RLEPAHPQLQ GMSQEQLAQV ATHAAKEFTE AFLGCPAIHP 70 80 90 100 110 120 RCRWGAAPYR GSPKPLKLPL GFLYIHHTYV PARPCTDFAL CAANMRSMQR FHLDTQGWDD 130 140 150 160 170 180 IGYSFVVGSD GYVYEGRGWH WVGAHTRDHN SRGFGVALIG NYTAELPSEA ALRAVRDELP 190 200 210 220 230 240 HCAVRAGLLQ PDYALLGHRQ LVRTDCPGDA LFNMLRTWPR FNMNVKPRTA RRASGRSKRR 250 LPLMIPLATD LQ « Hide

[1]	"Characterization of porcine peptidoglycan recognition proteins: gene cloning and regulation on innate immunity." Sang Y., Ross C.R., Blecha F. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).

Sequence databases
EMBL GenBank DDBJ	AF541955 mRNA. Translation: AAO41115.1. AF541956 mRNA. Translation: AAO41116.1.
RefSeq	NP_998903.1. NM_213738.1.
UniGene	Ssc.16628. Ssc.82572.
3D structure databases
ProteinModelPortal	Q866Y3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396557.
KEGG	ssc:396557.
Organism-specific databases
CTD	114770.
Phylogenomic databases
HOVERGEN	HBG053578.
KO	K01446.
Family and domain databases
Gene3D	3.40.80.10. 1 hit.
InterPro	IPR002502. Amidase_domain. IPR015510. PGRP. IPR006619. PGRP_domain_met/bac. [Graphical view]
PANTHER	PTHR11022. PTHR11022. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. SM00701. PGRP. 1 hit. [Graphical view]
SUPFAM	SSF55846. Amidase_2. 1 hit.
ProtoNet	Search...

Entry name

PGRP2_PIG

Accession

Primary (citable) accession number: Q866Y3
Secondary accession number(s): Q866Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	June 1, 2003
Last modified:	April 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform B (identifier: Q866Y3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform A (identifier: Q866Y3-2)

The sequence of this isoform differs from the canonical sequence as follows:
1-346: Missing.
347-356: ALTLTPNLTQ → MDCFCSRSQE

Note: No experimental confirmation available.