Q8R481

PR
Gene name
LPO
Protein name
Lactoperoxidase
Names
LPO, Lacrimal gland peroxidase
Species
Mesocricetus auratus (Golden hamster)
KEGG Pathway
EC number
1.11.1.7: Peroxidases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-63 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8R481

Entry ID Method Resolution Chain Position Source
AF-Q8R481-F1 Predicted AlphaFoldDB

No variants for Q8R481

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8R481

No associated diseases with Q8R481

No regional properties for Q8R481

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8R481

Functions

Description
EC Number 1.11.1.7 Peroxidases
Subcellular Localization
  • Secreted
  • Cytoplasm
  • Secreted by the lacrimal gland into tears
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
basolateral plasma membrane The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.

5 GO annotations of molecular function

Name Definition
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
lactoperoxidase activity Catalysis of the reaction: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O.
metal ion binding Binding to a metal ion.
peroxidase activity Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O.
thiocyanate peroxidase activity Catalysis of the reaction: thiocyanate (SCN-) + hydrogen peroxide (H2O2) = hypothiocyanite (OSCN-) + 2 H2O. Catalyzes the hydrogen peroxide oxidation of thiocyanate.

3 GO annotations of biological process

Name Definition
defense response to bacterium Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
detection of chemical stimulus involved in sensory perception of bitter taste The series of events required for a bitter taste stimulus to be received and converted to a molecular signal.
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKVLLRLPAL LASLTLLQMA ASTRNATRTA TIRETVDEVK VQVNKAFLDS RDRLKTDMSN
70 80 90 100 110 120
LAPTVRHLSG YLKQAKGRTR TAIRVGQVWE QSLKRLRRMV PLTNVTGQGL DLTSLSWEVG
130 140 150 160 170 180
CGHPAPTVTC NISNPYRTIT GDCNNRKNPE LGSANRALAR WLPAEYEDGL SLPFGWTPGK
190 200 210 220 230 240
TRNGFPLPQP RDVSNQVLDY LNEEEILDQN RSLLFMQWGQ IVDHDLDFAP ETEMGSDNYS
250 260 270 280 290 300
KAQCDELCIQ GDNCFPIMFP KGDPKLKTQG KCLPFFRAGF VCPTSPYQSL AREQINALTS
310 320 330 340 350 360
FMDASMVYGS EPSLANRLRN LSSPLGLMAV NEEVSDHGRP LLPFVNVKPS PCEVINRTAG
370 380 390 400 410 420
VPCFLAGDSR ASEQILLATS HTLFLREHNR LARELSRLNP QWDGEKLYQE ARRIMGALIQ
430 440 450 460 470 480
IITFRDYLPI LLGDELQKWI PPYQGYKETV DPRISNVFTF AFRFGHLEVP STVSRLDENY
490 500 510 520 530 540
QPWGSEPELP LHKLFFNTWR VVKDGGIDPL VRGLLAKKAK LAHQDKMMTG ELRNMLFQPN
550 560 570 580 590 600
HTVHGFDLAA INIQRCRDHG QPGYNSWRAF CGLSQPKTLE ELSAVLRNEV LAKKLMDLYG
610 620 630 640 650 660
TPDNIDIWLG AIAEPLVRRG RVGPLLTCLL GQQFQRIRDG DRFWWENPGV FTEKQRDSLQ
670 680 690 700
KMSFSRLVCD NTGINKVPLN PFQPNSYPHS FVDCSAIEKL DLTPWASVKK