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Reviewed, UniProtKB/Swiss-Prot P09849 (LPH_RABIT)

Last modified January 19, 2010. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Lactase-phlorizin hydrolase
Alternative name(s):
    Lactase-glycosylceramidase
Including the following 2 domains:
    1- Recommended name:
            Lactase
              EC=3.2.1.108
    2- Recommended name:
            Phlorizin hydrolase
              EC=3.2.1.62
Gene names
Name: LCT
Synonyms: LPH
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length1926 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Propeptide20 – 866847Beta-glucosidase
PRO_0000011769
Chain867 – 19261060Lactase-phlorizin hydrolase
PRO_0000011770

Regions

Topological domain20 – 18821863Extracellular Potential
Transmembrane1883 – 190119 Potential
Topological domain1902 – 192625Cytoplasmic Potential
Repeat79 – 172941
Repeat360 – 8454862
Repeat881 – 13674873
Repeat1375 – 18004264
Region79 – 180017224 X approximate repeats

Sites

Active site10631Proton donor Potential
Active site12711Nucleophile Ref.2
Active site15361Proton donor Potential
Active site17471Nucleophile Ref.2

Amino acid modifications

Modified residue13011Phosphotyrosine By similarity
Modified residue13111Phosphotyrosine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P09849-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 2A21A7370D0CFC7A

FASTA1,926217,849
        10         20         30         40         50         60 
MELFWSIVFT VLLSFSCRGS DWESDSNFIS AAGPLTTDLL LSLQYPQGNQ TSDFAAGGKD 

        70         80         90        100        110        120 
LYVCSQPLPA FLPEYFSSLR ASEITHYKVF LSWAQLLPAG HSGDPDGNAV RCYRQLLEAL 

       130        140        150        160        170        180 
RAAQLQPMVV LHHQHLPASS ALRSAVFADL FAEYATFAFH AFGDLVGVWL TFSDLEAAIR 

       190        200        210        220        230        240 
ELPQPESRAS RLQLLTEAHR KAYEIYHQKY AAQGGKVSVV LQAEEISELL LESSTSALAK 

       250        260        270        280        290        300 
DSIDFLSLDL SYECQSEMSL PEKLSKLQTI EPKVKVFIFT LRLQDCPSSR KSPASLLFSF 

       310        320        330        340        350        360 
IEAINKDQVL TLGFDVNAFL NCSSTSKKSI SCFLTDSLAL QTDHERAARN SAPVSTYQRV 

       370        380        390        400        410        420 
WEMFAHQPRA ERDAFLQDTF PQGFLWGVST GAFNVEGGWA EGGRGPSVWD QFGHLKAAQG 

       430        440        450        460        470        480 
QATPEVASDS YYKWASDVAL LRGLRAQVYK FSISWSRIFP MGRGSSPSPQ GVAYYNKLID 

       490        500        510        520        530        540 
SLLDSHIEPM ATLFHWDLPQ ALQDEGGWQN ESVVDAFVDY AAFCFSAFGN RVKLWVTFHE 

       550        560        570        580        590        600 
PWVMSYAGYG TGQHAPGISD PGIASFQVAH LVLKAHARTW HHYNSHHRPQ QQGRVGIVLN 

       610        620        630        640        650        660 
SDWAEPLSPE RPEDLAASER FLHFMLGWFA HPIFVDGDYP ATMKAQIQQR NEQCPSPVAQ 

       670        680        690        700        710        720 
LPEFTDTEKQ LLKGSADFLG LSHYTSRLIS KAPEDSCIPS YDTIGGFSQH TDPAWPQTSS 

       730        740        750        760        770        780 
PWIRVVPWGI RRLLQFVSLE YTKGKVPIYL AGNGMPIGES ENLLSDSLRV DYFNQYINEV 

       790        800        810        820        830        840 
LKAIKEDSVD VRSYIARSLM DGFEGPAGYS QRFGLYHVNF NESSKPRTPR KSAFLLTSII 

       850        860        870        880        890        900 
EKNGFLTKAV KQPLPPNSAH LPSKTRASAL PSEVPSKAKV VWEKFSNQTK FERDLFYHGT 

       910        920        930        940        950        960 
FRDDFLWGVS SSAYQIEGAW DADGKGPSIW DNFTHTPGNG VTDNSTGDIA CDSYNQLDAD 

       970        980        990       1000       1010       1020 
LNVLRALKVK AYRFSLSWSR IFPTGTNSSI NSHGVDYYNR LIDGLLASDI FPMVTLFHWD 

      1030       1040       1050       1060       1070       1080 
LPQALQDIGG WENPSLIDLF DSYADYCFQT FGDRVKFWIT FNEPTYYSWW SYGSGTFPPN 

      1090       1100       1110       1120       1130       1140 
VNDPGWAPYR ISHALIKAHA RVYHTYDEKY RQSQNGVISL SLVAQWAEPK SPDVLRDVEA 

      1150       1160       1170       1180       1190       1200 
ADRKMQFTLG WYAHPIFKTG DYPDAMKWKV GNRSELQHLA TSRLPSFTEE EKSYIRGTAD 

      1210       1220       1230       1240       1250       1260 
VFCLNTYSSK IVQHKTPALN PPSYEDDQEL AEEEDTSWPT TAMNRAASFG MRRLLNWIKE 

      1270       1280       1290       1300       1310       1320 
EYGDIPIYIT ENGVGLTNPR LEDIDRIFYY KTYINEALKA YRLDGVNLRG YFAWSLMDNF 

      1330       1340       1350       1360       1370       1380 
EWLQGYTIKF GLYHVDFENV NRPRTARISA SYYTELITNN GMPLPSEDEF VYGQFPEGFV 

      1390       1400       1410       1420       1430       1440 
WSTSTAAFQI EGAWRADGKG LGIWDTFTHT RLKIENDDIA DVACDSYHKI SEDVVALQNL 

      1450       1460       1470       1480       1490       1500 
AVTHYRFSIS WSRILPDGTT NYINEAGLNY YVRLIDALLA ANIKPQVTMY HFDLPQALQD 

      1510       1520       1530       1540       1550       1560 
VGGWENETIV QRFKEYADVL FQRLGDKVKF WITLNEPFVV AYHGYGTGLY APGIYFRPGT 

      1570       1580       1590       1600       1610       1620 
APYIVGHNLI KAHAEAWHLY NDVYRASQGG VISITISSDW AEPRDPSNQE DVEAAKRYVQ 

      1630       1640       1650       1660       1670       1680 
FMGGWFAHPI FKNGDYNEVM KTQIRERSLA AGLNESRLPE FTESEKRRIN GTYDFFGFNH 

      1690       1700       1710       1720       1730       1740 
YTTVLAYNFN YPSIMSTVDA DRGVASIVDR SWPGSGSYWL KMTPFGFRRI LNWIKEEYNN 

      1750       1760       1770       1780       1790       1800 
PPIYVTENGV SHRGDSYLND TTRIYYLRSY INEALKAVQQ DKVDLRGYTV WTLMDNFEWY 

      1810       1820       1830       1840       1850       1860 
TGFSDKFGLH FVNYSDPSLP RIPRESAKFY ASIVRCNGFP DPAEGPHPCL LQPEDTDPTM 

      1870       1880       1890       1900       1910       1920 
SPVSQEEVQF LGLSLGSTEA ETALYVLFSL MLLGVCGLAF LSYALCKSSK QRKKLSQQEL 


SPVSSF

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References

[1]"Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme."
Mantei N., Villa M., Enzler T., Wacker H., Boll W., James P., Hunziker W., Semenza G.
EMBO J. 7:2705-2713(1988) [PubMed: 2460343] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: New Zealand white.
[2]"Location of the two catalytic sites in intestinal lactase-phlorizin hydrolase. Comparison with sucrase-isomaltase and with other glycosidases, the membrane anchor of lactase-phlorizin hydrolase."
Wacker H., Keller P., Falchetto R., Legler G., Semenza G.
J. Biol. Chem. 267:18744-18752(1992) [PubMed: 1388157] [Abstract]
Cited for: ACTIVE SITES.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X07995 mRNA. Translation: CAA30802.1.
PIRS01169.
RefSeqNP_001095159.1.
UniGeneOcu.3264

3D structure databases

SMRP09849. Positions 377-840, 900-1362, 1374-1839.
ModBaseSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Genome annotation databases

GeneID100009256.

Organism-specific databases

CTD100009256.

Phylogenomic databases

eggNOGmaNOG07993.
HOVERGENP09849.

Enzyme and pathway databases

BRENDA3.2.1.108. 255.
3.2.1.62. 255.

Family and domain databases

InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 4 hits.
PANTHERPTHR10353. Glyco_hydro_1. 1 hit.
PfamPF00232. Glyco_hydro_1. 4 hits.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 2 hits.
PS00653. GLYCOSYL_HYDROL_F1_2. 3 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLPH_RABIT
AccessionPrimary (citable) accession number: P09849
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 19, 2010
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents