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Q02401 (LPH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lactase-phlorizin hydrolase
Alternative name(s):
Lactase-glycosylceramidase

Including the following 2 domains:

  1. Lactase
    EC=3.2.1.108
  2. Phlorizin hydrolase
    EC=3.2.1.62
Gene names
Name:Lct
Synonyms:Lph
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1928 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

LPH splits lactose in the small intestine.

Catalytic activity

Lactose + H2O = D-galactose + D-glucose.

Glycosyl-N-acylsphingosine + H2O = N-acylsphingosine + a sugar.

Subcellular location

Apical cell membrane; Single-pass type I membrane protein. Note: Brush border.

Tissue specificity

Intestine.

Domain

The sequence exhibits 4 regions (I-IV) of internal homology; therefore LPH might have evolved by two cycles of partial gene duplication.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionGlycosidase
Hydrolase
   PTMZymogen
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

response to drug

Inferred from direct assay PubMed 17147060. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 16396664. Source: RGD

response to ethanol

Inferred from direct assay PubMed 15849819. Source: RGD

response to hormone

Inferred from expression pattern PubMed 17190105. Source: RGD

response to hypoxia

Inferred from direct assay PubMed 12773704. Source: RGD

response to iron(II) ion

Inferred from direct assay PubMed 16081762. Source: RGD

response to lead ion

Inferred from direct assay PubMed 16092086. Source: RGD

response to nickel cation

Inferred from direct assay PubMed 16819762. Source: RGD

response to nutrient

Inferred from direct assay PubMed 16497337. Source: RGD

response to organic substance

Inferred from direct assay PubMed 12428451. Source: RGD

response to starvation

Inferred from expression pattern PubMed 17190105. Source: RGD

response to sucrose

Inferred from expression pattern PubMed 17190105. Source: RGD

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

brush border

Inferred from direct assay PubMed 12023280. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglycosylceramidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

lactase activity

Inferred from direct assay PubMed 12023280. Source: RGD

transferase activity

Inferred from direct assay PubMed 12023280. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 867848Beta-glucosidase
PRO_0000011771
Chain868 – 19281061Lactase-phlorizin hydrolase
PRO_0000011772

Regions

Topological domain22 – 18831862Extracellular Potential
Transmembrane1884 – 190219Helical; Potential
Topological domain1903 – 192826Cytoplasmic Potential
Repeat89 – 175871
Repeat365 – 8494852
Repeat886 – 13664813
Repeat1371 – 18424724
Region89 – 184217544 X approximate repeats

Sites

Active site10671Proton donor Potential
Active site12741Nucleophile By similarity
Active site15391Proton donor Potential
Active site17501Nucleophile By similarity

Experimental info

Sequence conflict71A → R in AAA41539. Ref.1
Sequence conflict1131Q → E in AAA41539. Ref.1
Sequence conflict2071E → D in AAA41539. Ref.1
Sequence conflict13371Y → H Ref.3
Sequence conflict1357 – 13593PDL → AEV Ref.3
Sequence conflict1369 – 13702RE → GK Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q02401 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 56DDCAAC4ACAEA85

FASTA1,928217,268
        10         20         30         40         50         60 
MELPWTALFL STVLLGLSCQ GSDWESDRNF ISAAGPLTND LVLNLNYPPG KQGSDVVSGN 

        70         80         90        100        110        120 
TDHLLCQQPL PSFLSQYFSS LRASQVTHYK VLLSWAQLLP TGSSKNPDQE AVQCYRQLLQ 

       130        140        150        160        170        180 
SLKDAQLEPM VVLCHQTPPT SSAIQREGAF ADLFADYATL AFQSFGDLVE IWFTFSDLEK 

       190        200        210        220        230        240 
VIMDLPHKDL KASALQTLSN AHRRAFEIYH RKFSSQGGKL SVVLKAEDIP ELLPDPALAA 

       250        260        270        280        290        300 
LVQGSVDFLS LDLSYECQSV ATLPQKLSEL QNLEPKVKVF IYTLKLEDCP ATGTSPSSLL 

       310        320        330        340        350        360 
ISLLEAINKD QIQTVGFDVN AFLSCTSNSE ESPSCSLTDS LALQTEQQQE TAVPSSPGSA 

       370        380        390        400        410        420 
YQRVWAAFAN QSREERDAFL QDVFPEGFLW GISTGAFNVE GGWAEGGRGP SIWDHYGNLN 

       430        440        450        460        470        480 
AAEGQATAKV ASDSYHKPAS DVALLRGIRA QVYKFSISWS GLFPLGQKST PNRQGVAYYN 

       490        500        510        520        530        540 
KLIDRLLDSH IEPMATLFHW DLPQALQEQG GWQNESVVEA FLDYAAFCFS TFGDRVKLWV 

       550        560        570        580        590        600 
TFHEPWVMSY AGYGTGQHAP AISDPGMASF KVAHLILKAH ARTWHLYDLH HRLQQQGRVG 

       610        620        630        640        650        660 
IVLNSDLAEP LDRKSPQDLA AAERFLHFML GWFAHPIFVD GDYPTTSAQI QHINQQCGHP 

       670        680        690        700        710        720 
LAQLPEFTEA EKRLLKGSAD FLGLSHYTSR LISKAGRQTC TSSYDNIGGF SQHVDPEWPQ 

       730        740        750        760        770        780 
TASPWIRVVP WGIRRLLRFA SMEYTKGKLP IFLAGNGMPV GEEADLFDDS VRVNYFNWYI 

       790        800        810        820        830        840 
NEVLKAVKED LVDVRSYIVR SLIDGYEGPL GFSQRFGLYH VNFNDSSRPR TPRKSAYLFT 

       850        860        870        880        890        900 
SIIEKNGFSA KKVKRNPLPV RADFTSRARV TDSLPSEVPS KAKISVEKFS KQPRFERDLF 

       910        920        930        940        950        960 
YDGRFRDDFL WGVSSSPYQI EGGWNADGKG PSIWDNFTHT PGNGVKDNAT GDVACDSYHQ 

       970        980        990       1000       1010       1020 
LDADLNILRT LKVKSYRFSI SWSRIFPTGR NSTINKQGVD YYNRLIDSLV DNNIFPMVTL 

      1030       1040       1050       1060       1070       1080 
FHWDLPQALQ DIGGWENPSL IELFDSYADY CFKTFGDRVK FWMTFNEPWC HVVLGYSSGI 

      1090       1100       1110       1120       1130       1140 
FPPSVQEPGW LPYKVSHIVI KAHARVYHTY DEKYRSEQKG VISLSLNTHW AEPKDPGLQR 

      1150       1160       1170       1180       1190       1200 
DVEAADRMLQ FTMGWFAHPI FKNGDYPDVM KWTVGNRSEL QHLASSRLPT FTEEEKNYVR 

      1210       1220       1230       1240       1250       1260 
GTADVFCHNT YTSVFVQHST PRLNPPSYDD DMELKLIEMN SSTGVMHQDV PWGTRRLLNW 

      1270       1280       1290       1300       1310       1320 
IKEEYGNIPI YITENGQGLE NPTLDDTERI FYHKTYINEA LKAYKLDGVD LRGYSAWTLM 

      1330       1340       1350       1360       1370       1380 
DDFEWLLGYT MRFGLYYVDF NHVSRPRTAR ASARYYPDLI ANNGMPLARE DEFLYGEFPK 

      1390       1400       1410       1420       1430       1440 
GFIWSAASAS YQVEGAWRAD GKGLSIWDTF SHTPLRIGND DNGDVACDSY HKIAEDVVAL 

      1450       1460       1470       1480       1490       1500 
QNLGVSHYRF SIAWSRILPD GTTKFINEAG LSYYVRFIDA LLAAGITPQV TIYHWDLPQA 

      1510       1520       1530       1540       1550       1560 
LQDVGGWENE TIVQRFKEYA DVLFQRLGDR VKFWITLNEP FVIAAQGYGT GVSAPGISFR 

      1570       1580       1590       1600       1610       1620 
PGTAPYIAGH NLIKAHAEAW HLYNDVYRAR QGGTISITIS SDWGEPRDPT NREHVEAARS 

      1630       1640       1650       1660       1670       1680 
YVQFMGGWFA HPIFKNGDYP EVMKTRIRDR SLGAGLNKSR LPEFTESEKS RIKGTFDFFG 

      1690       1700       1710       1720       1730       1740 
FNHNTTVLAY NLDYPAAFSS FDADRGVASI ADSSWPVSGS FWLKVTPFGF RRILNWLKEE 

      1750       1760       1770       1780       1790       1800 
YNNPPIYVTE NGVSRRGEPE LNDTDRIYYL RSYINEALKA VHDKVDLRGY TVWSIMDNFE 

      1810       1820       1830       1840       1850       1860 
WATGFAERFG VHFVNRSDPS LPRIPRASAK FYATIVRCNG FPDPAQGPHP CLQQPEDAAP 

      1870       1880       1890       1900       1910       1920 
TASPVQSEVP FLGLMLGIAE AQTALYVLFA LLLLGACSLA FLTYNTGRRS KQGNAQPSQH 


QLSPISSF 

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References

[1]"Sequence of the precursor of intestinal lactase-phlorizin hydrolase from fetal rat."
Duluc I., Boukamel R., Mantei N., Semenza G., Raul F., Freund J.-N.
Gene 103:275-276(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Wistar.
Tissue: Intestine.
[2]"The rat LPH gene 5' region: comparative structure with the human gene."
Boukamel R., Freund J.-N.
DNA Seq. 3:119-121(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
Strain: Sprague-Dawley.
[3]"Coordinate expression of lactase-phlorizin hydrolase mRNA and enzyme levels in rat intestine during development."
Bueller H.A., Kothe M.J., Goldman D.A., Grubman S.A., Sasak W.V., Matsudaira P.T., Montgomery R.K., Grand R.J.
J. Biol. Chem. 265:6978-6983(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1288-1370.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56748 Genomic DNA. Translation: CAA40070.1.
X56747 mRNA. Translation: CAA40069.1.
L04635 Genomic DNA. Translation: AAA41539.1.
PIRJS0610.
UniGeneRn.92376.

3D structure databases

ProteinModelPortalQ02401.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ02401.
ChEMBLCHEMBL3389.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

PTM databases

PhosphoSiteQ02401.

Proteomic databases

PaxDbQ02401.
PRIDEQ02401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:620823. rat.

Organism-specific databases

RGD620823. Lct.

Phylogenomic databases

eggNOGCOG2723.
HOVERGENHBG006290.
InParanoidQ02401.
PhylomeDBQ02401.

Gene expression databases

GenevestigatorQ02401.

Family and domain databases

Gene3D3.20.20.80. 4 hits.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 4 hits.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 4 hits.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

PROQ02401.

Entry information

Entry nameLPH_RAT
AccessionPrimary (citable) accession number: Q02401
Secondary accession number(s): Q63712, Q63719
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries