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Protein

Lactoperoxidase

Gene

LPO

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN). May protect the udder from infection and promote growth in newborn calves. Inhibits growth of the following bacterial species: E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis, and S.dysenteriae.By similarity

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 1 Ca2+ ion per heterodimer.
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251Heme (covalent; via 2 links)1 Publication
Active sitei226 – 2261Proton acceptorPROSITE-ProRule annotation
Metal bindingi227 – 2271CalciumPROSITE-ProRule annotation1 Publication
Metal bindingi301 – 3011CalciumPROSITE-ProRule annotation1 Publication
Metal bindingi303 – 3031Calcium; via carbonyl oxygenPROSITE-ProRule annotation1 Publication
Metal bindingi305 – 3051CalciumPROSITE-ProRule annotation1 Publication
Metal bindingi307 – 3071CalciumPROSITE-ProRule annotation1 Publication
Sitei372 – 3721Transition state stabilizerPROSITE-ProRule annotation
Binding sitei375 – 3751Heme (covalent; via 2 links)1 Publication
Metal bindingi468 – 4681Iron (heme axial ligand)

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • heme binding Source: InterPro
  • thiocyanate peroxidase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.11.1.7. 908.
SABIO-RKP80025.

Protein family/group databases

PeroxiBasei3331. BtLPO.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactoperoxidase (EC:1.11.1.7)
Short name:
LPO
Gene namesi
Name:LPO
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: Ensembl
  • cytoplasm Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi225 – 2251D → E: Partially bound heme and decrease in activity. Loss of heme binding and activity; when associated with D-375. 2 Publications
Mutagenesisi225 – 2251D → V: Partially bound heme. 2 Publications
Mutagenesisi375 – 3751E → D: Partially bound heme. Loss of heme binding and activity; when associated with E-225. 2 Publications
Mutagenesisi375 – 3751E → Q: Decrease in activity. 2 Publications

Chemistry

ChEMBLiCHEMBL2295561.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 100781 PublicationPRO_0000023647Add
BLAST
Chaini101 – 712612LactoperoxidasePRO_0000023648Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi132 ↔ 145
Glycosylationi212 – 2121N-linked (GlcNAc...)2 Publications
Disulfide bondi246 ↔ 256
Disulfide bondi250 ↔ 274
Modified residuei315 – 3151Phosphoserine2 Publications
Glycosylationi322 – 3221N-linked (GlcNAc...)2 Publications
Disulfide bondi354 ↔ 365
Glycosylationi358 – 3581N-linked (GlcNAc...)2 Publications
Glycosylationi449 – 4491N-linked (GlcNAc...)2 Publications
Disulfide bondi573 ↔ 630
Disulfide bondi671 ↔ 696

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP80025.
PeptideAtlasiP80025.
PRIDEiP80025.

PTM databases

iPTMnetiP80025.

Expressioni

Tissue specificityi

Mammary gland; milk.

Gene expression databases

BgeeiENSBTAG00000012780.
ExpressionAtlasiP80025. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016986.

Structurei

Secondary structure

1
712
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi125 – 1273Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi146 – 1505Combined sources
Turni151 – 1544Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi184 – 1874Combined sources
Helixi192 – 1998Combined sources
Beta strandi209 – 2146Combined sources
Helixi215 – 22814Combined sources
Beta strandi238 – 2414Combined sources
Helixi242 – 2498Combined sources
Beta strandi254 – 2563Combined sources
Helixi266 – 2705Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi286 – 2883Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi296 – 2983Combined sources
Beta strandi302 – 3054Combined sources
Helixi307 – 3104Combined sources
Helixi314 – 3196Combined sources
Beta strandi324 – 3274Combined sources
Beta strandi338 – 3414Combined sources
Helixi353 – 3564Combined sources
Turni359 – 3613Combined sources
Turni371 – 3744Combined sources
Helixi377 – 40024Combined sources
Helixi406 – 42722Combined sources
Helixi429 – 4346Combined sources
Helixi435 – 4373Combined sources
Helixi438 – 4414Combined sources
Beta strandi450 – 4523Combined sources
Helixi460 – 4634Combined sources
Helixi464 – 4707Combined sources
Beta strandi473 – 4764Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi486 – 4883Combined sources
Beta strandi490 – 4923Combined sources
Helixi493 – 4964Combined sources
Helixi501 – 5044Combined sources
Turni505 – 5073Combined sources
Helixi510 – 5189Combined sources
Beta strandi519 – 5224Combined sources
Beta strandi526 – 5283Combined sources
Helixi532 – 5354Combined sources
Beta strandi537 – 5393Combined sources
Turni541 – 5433Combined sources
Beta strandi545 – 5484Combined sources
Helixi550 – 56011Combined sources
Helixi566 – 5727Combined sources
Helixi581 – 5888Combined sources
Helixi591 – 60111Combined sources
Helixi604 – 6063Combined sources
Helixi609 – 6157Combined sources
Beta strandi622 – 6243Combined sources
Helixi626 – 64116Combined sources
Beta strandi647 – 6493Combined sources
Turni650 – 6523Combined sources
Helixi655 – 6617Combined sources
Helixi666 – 6738Combined sources
Beta strandi678 – 6825Combined sources
Turni689 – 6924Combined sources
Beta strandi693 – 6953Combined sources
Helixi696 – 6983Combined sources
Helixi705 – 7073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJ1X-ray2.30A130-712[»]
2IPSX-ray3.10A118-712[»]
2NQXX-ray2.95A118-712[»]
2PT3X-ray2.34A118-712[»]
2PUMX-ray2.70A118-712[»]
2QPKX-ray2.34A118-712[»]
2QQTX-ray2.50A118-712[»]
2QRBX-ray2.50A118-712[»]
3BXIX-ray2.30A118-712[»]
3ERIX-ray2.50A118-712[»]
3GC1X-ray2.50A118-712[»]
3GCJX-ray2.34A118-712[»]
3GCKX-ray2.90A118-712[»]
3GCLX-ray2.50A118-712[»]
3I6NX-ray2.70A118-712[»]
3KRQX-ray2.25A118-712[»]
3NYHX-ray1.77A118-712[»]
3OGWX-ray1.89A118-712[»]
3PY4X-ray2.42A118-712[»]
3Q9KX-ray1.70A118-712[»]
3QL6X-ray1.70A118-712[»]
3R4XX-ray2.01A118-712[»]
3R5OX-ray2.60A118-712[»]
3S4FX-ray2.00A118-712[»]
3TGYX-ray2.35A118-712[»]
3TUWX-ray2.20A118-712[»]
3UBAX-ray2.65A118-712[»]
3V6QX-ray2.00A118-712[»]
4GM7X-ray2.60A118-712[»]
4GN6X-ray2.42A118-712[»]
4KSZX-ray1.98A118-712[»]
4NJBX-ray2.31A118-712[»]
4NT3X-ray1.99A118-712[»]
4PNXX-ray2.41A118-712[»]
4S0YX-ray1.93A118-712[»]
5JT3X-ray2.30A118-712[»]
5K1EX-ray2.07A118-712[»]
ProteinModelPortaliP80025.
SMRiP80025. Positions 118-712.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80025.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP80025.
KOiK12550.
OMAiSPWASVK.
OrthoDBiEOG091G0236.
TreeFamiTF314316.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029587. LPO.
[Graphical view]
PANTHERiPTHR11475:SF67. PTHR11475:SF67. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80025-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWVCLQLPVF LASVTLFEVA ASDTIAQAAS TTTISDAVSK VKIQVNKAFL
60 70 80 90 100
DSRTRLKTTL SSEAPTTQQL SEYFKHAKGR TRTAIRNGQV WEESLKRLRR
110 120 130 140 150
DTTLTNVTDP SLDLTALSWE VGCGAPVPLV KCDENSPYRT ITGDCNNRRS
160 170 180 190 200
PALGAANRAL ARWLPAEYED GLALPFGWTQ RKTRNGFRVP LAREVSNKIV
210 220 230 240 250
GYLDEEGVLD QNRSLLFMQW GQIVDHDLDF APETELGSNE HSKTQCEEYC
260 270 280 290 300
IQGDNCFPIM FPKNDPKLKT QGKCMPFFRA GFVCPTPPYQ SLAREQINAV
310 320 330 340 350
TSFLDASLVY GSEPSLASRL RNLSSPLGLM AVNQEAWDHG LAYLPFNNKK
360 370 380 390 400
PSPCEFINTT ARVPCFLAGD FRASEQILLA TAHTLLLREH NRLARELKKL
410 420 430 440 450
NPHWNGEKLY QEARKILGAF IQIITFRDYL PIVLGSEMQK WIPPYQGYNN
460 470 480 490 500
SVDPRISNVF TFAFRFGHME VPSTVSRLDE NYQPWGPEAE LPLHTLFFNT
510 520 530 540 550
WRIIKDGGID PLVRGLLAKK SKLMNQDKMV TSELRNKLFQ PTHKIHGFDL
560 570 580 590 600
AAINLQRCRD HGMPGYNSWR GFCGLSQPKT LKGLQTVLKN KILAKKLMDL
610 620 630 640 650
YKTPDNIDIW IGGNAEPMVE RGRVGPLLAC LLGRQFQQIR DGDRFWWENP
660 670 680 690 700
GVFTEKQRDS LQKVSFSRLI CDNTHITKVP LHAFQANNYP HDFVDCSTVD
710
KLDLSPWASR EN
Length:712
Mass (Da):80,642
Last modified:August 1, 1991 - v1
Checksum:i28EED4C0C8420E6D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti449 – 4491N → R AA sequence (PubMed:2050150).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58150 mRNA. Translation: AAA62714.1.
PIRiA35828.
RefSeqiNP_776358.1. NM_173933.2.
XP_010814001.1. XM_010815699.2.
XP_010814003.1. XM_010815701.2.
XP_015313999.1. XM_015458513.1.
UniGeneiBt.4784.

Genome annotation databases

EnsembliENSBTAT00000016986; ENSBTAP00000016986; ENSBTAG00000012780.
GeneIDi280844.
KEGGibta:280844.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58150 mRNA. Translation: AAA62714.1.
PIRiA35828.
RefSeqiNP_776358.1. NM_173933.2.
XP_010814001.1. XM_010815699.2.
XP_010814003.1. XM_010815701.2.
XP_015313999.1. XM_015458513.1.
UniGeneiBt.4784.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJ1X-ray2.30A130-712[»]
2IPSX-ray3.10A118-712[»]
2NQXX-ray2.95A118-712[»]
2PT3X-ray2.34A118-712[»]
2PUMX-ray2.70A118-712[»]
2QPKX-ray2.34A118-712[»]
2QQTX-ray2.50A118-712[»]
2QRBX-ray2.50A118-712[»]
3BXIX-ray2.30A118-712[»]
3ERIX-ray2.50A118-712[»]
3GC1X-ray2.50A118-712[»]
3GCJX-ray2.34A118-712[»]
3GCKX-ray2.90A118-712[»]
3GCLX-ray2.50A118-712[»]
3I6NX-ray2.70A118-712[»]
3KRQX-ray2.25A118-712[»]
3NYHX-ray1.77A118-712[»]
3OGWX-ray1.89A118-712[»]
3PY4X-ray2.42A118-712[»]
3Q9KX-ray1.70A118-712[»]
3QL6X-ray1.70A118-712[»]
3R4XX-ray2.01A118-712[»]
3R5OX-ray2.60A118-712[»]
3S4FX-ray2.00A118-712[»]
3TGYX-ray2.35A118-712[»]
3TUWX-ray2.20A118-712[»]
3UBAX-ray2.65A118-712[»]
3V6QX-ray2.00A118-712[»]
4GM7X-ray2.60A118-712[»]
4GN6X-ray2.42A118-712[»]
4KSZX-ray1.98A118-712[»]
4NJBX-ray2.31A118-712[»]
4NT3X-ray1.99A118-712[»]
4PNXX-ray2.41A118-712[»]
4S0YX-ray1.93A118-712[»]
5JT3X-ray2.30A118-712[»]
5K1EX-ray2.07A118-712[»]
ProteinModelPortaliP80025.
SMRiP80025. Positions 118-712.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016986.

Chemistry

ChEMBLiCHEMBL2295561.

Protein family/group databases

PeroxiBasei3331. BtLPO.

PTM databases

iPTMnetiP80025.

Proteomic databases

PaxDbiP80025.
PeptideAtlasiP80025.
PRIDEiP80025.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016986; ENSBTAP00000016986; ENSBTAG00000012780.
GeneIDi280844.
KEGGibta:280844.

Organism-specific databases

CTDi4025.

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP80025.
KOiK12550.
OMAiSPWASVK.
OrthoDBiEOG091G0236.
TreeFamiTF314316.

Enzyme and pathway databases

BRENDAi1.11.1.7. 908.
SABIO-RKP80025.

Miscellaneous databases

EvolutionaryTraceiP80025.
PROiP80025.

Gene expression databases

BgeeiENSBTAG00000012780.
ExpressionAtlasiP80025. baseline and differential.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029587. LPO.
[Graphical view]
PANTHERiPTHR11475:SF67. PTHR11475:SF67. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPERL_BOVIN
AccessioniPrimary (citable) accession number: P80025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 7, 2016
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.