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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)DescriptionActionsGraphical viewLength
Binding sitei225Heme (covalent; via 2 links)1 Publication1
Active sitei226Proton acceptorPROSITE-ProRule annotation1
Metal bindingi227CalciumPROSITE-ProRule annotation1 Publication1
Metal bindingi301CalciumPROSITE-ProRule annotation1 Publication1
Metal bindingi303Calcium; via carbonyl oxygenPROSITE-ProRule annotation1 Publication1
Metal bindingi305CalciumPROSITE-ProRule annotation1 Publication1
Metal bindingi307CalciumPROSITE-ProRule annotation1 Publication1
Sitei372Transition state stabilizerPROSITE-ProRule annotation1
Binding sitei375Heme (covalent; via 2 links)1 Publication1
Metal bindingi468Iron (heme axial ligand)1

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: GO_Central
  • extracellular exosome Source: Ensembl
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi225D → E: Partially bound heme and decrease in activity. Loss of heme binding and activity; when associated with D-375. 2 Publications1
Mutagenesisi225D → V: Partially bound heme. 2 Publications1
Mutagenesisi375E → D: Partially bound heme. Loss of heme binding and activity; when associated with E-225. 2 Publications1
Mutagenesisi375E → Q: Decrease in activity. 2 Publications1

Chemistry databases

ChEMBLiCHEMBL2295561.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000002364723 – 1001 PublicationAdd BLAST78
ChainiPRO_0000023648101 – 712LactoperoxidaseAdd BLAST612

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi106N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi132 ↔ 145
Glycosylationi212N-linked (GlcNAc...)2 Publications1
Disulfide bondi246 ↔ 256
Disulfide bondi250 ↔ 274
Modified residuei315Phosphoserine2 Publications1
Glycosylationi322N-linked (GlcNAc...)2 Publications1
Disulfide bondi354 ↔ 365
Glycosylationi358N-linked (GlcNAc...)2 Publications1
Glycosylationi449N-linked (GlcNAc...)2 Publications1
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

1712
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi125 – 127Combined sources3
Beta strandi141 – 143Combined sources3
Beta strandi146 – 150Combined sources5
Turni151 – 154Combined sources4
Beta strandi156 – 159Combined sources4
Beta strandi171 – 173Combined sources3
Beta strandi178 – 181Combined sources4
Beta strandi184 – 187Combined sources4
Helixi192 – 199Combined sources8
Beta strandi209 – 214Combined sources6
Helixi215 – 228Combined sources14
Beta strandi238 – 241Combined sources4
Helixi242 – 249Combined sources8
Beta strandi254 – 256Combined sources3
Helixi266 – 270Combined sources5
Beta strandi273 – 275Combined sources3
Beta strandi282 – 284Combined sources3
Beta strandi286 – 288Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi296 – 298Combined sources3
Beta strandi302 – 305Combined sources4
Helixi307 – 310Combined sources4
Helixi314 – 319Combined sources6
Beta strandi323 – 325Combined sources3
Beta strandi338 – 341Combined sources4
Helixi353 – 356Combined sources4
Turni359 – 361Combined sources3
Turni371 – 374Combined sources4
Helixi377 – 400Combined sources24
Helixi406 – 427Combined sources22
Helixi429 – 434Combined sources6
Helixi435 – 437Combined sources3
Helixi438 – 441Combined sources4
Beta strandi450 – 452Combined sources3
Helixi460 – 463Combined sources4
Helixi464 – 470Combined sources7
Beta strandi473 – 476Combined sources4
Beta strandi482 – 484Combined sources3
Beta strandi486 – 488Combined sources3
Beta strandi490 – 492Combined sources3
Helixi493 – 496Combined sources4
Helixi501 – 504Combined sources4
Turni505 – 507Combined sources3
Helixi510 – 518Combined sources9
Beta strandi519 – 522Combined sources4
Beta strandi526 – 528Combined sources3
Helixi532 – 535Combined sources4
Beta strandi537 – 539Combined sources3
Turni541 – 543Combined sources3
Beta strandi545 – 548Combined sources4
Helixi550 – 560Combined sources11
Helixi566 – 572Combined sources7
Helixi581 – 588Combined sources8
Helixi591 – 601Combined sources11
Helixi604 – 606Combined sources3
Helixi609 – 615Combined sources7
Beta strandi622 – 624Combined sources3
Helixi626 – 641Combined sources16
Beta strandi647 – 649Combined sources3
Turni650 – 652Combined sources3
Helixi655 – 661Combined sources7
Helixi666 – 673Combined sources8
Beta strandi678 – 682Combined sources5
Turni689 – 692Combined sources4
Beta strandi693 – 695Combined sources3
Helixi696 – 698Combined sources3
Helixi705 – 707Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5B72X-ray1.98A118-712[»]
5GH0X-ray2.30A118-712[»]
5GLSX-ray1.93A118-712[»]
5K1EX-ray2.07A118-712[»]
ProteinModelPortaliP80025.
SMRiP80025.
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)DescriptionActionsGraphical viewLength
Sequence conflicti449N → R AA sequence (PubMed:2050150).Curated1

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
PDB 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[»]
5B72X-ray1.98A118-712[»]
5GH0X-ray2.30A118-712[»]
5GLSX-ray1.93A118-712[»]
5K1EX-ray2.07A118-712[»]
ProteinModelPortaliP80025.
SMRiP80025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016986.

Chemistry databases

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: November 2, 2016
This is version 163 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.