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P07768 (SUIS_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. Feed History...

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

Names and origin

Protein namesRecommended name:
Sucrase-isomaltase, intestinal

Cleaved into the following 2 chains:

  1. Sucrase
    EC=3.2.1.48
  2. Isomaltase
    EC=3.2.1.10
Gene names
Name:SI
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length1827 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.

Catalytic activity

Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

Subunit structure

The resulting sucrase and isomaltase subunits stay associated with one another in a complex by non-covalent linkages.

Subcellular location

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

Post-translational modification

The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.

N- and O-glycosylated.

Sulfated By similarity.

Miscellaneous

There is a high degree of homology between the isomaltase and sucrase portions (41% of amino acid identity) indicating that this protein is evolved by partial gene duplication.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Contains 2 P-type (trefoil) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 18271826Sucrase-isomaltase, intestinal
PRO_0000018556
Chain2 – 10071006Isomaltase
PRO_0000018557
Chain1008 – 1827820Sucrase
PRO_0000018558

Regions

Topological domain2 – 1211Cytoplasmic Potential
Transmembrane13 – 3220Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 18271795Lumenal Potential
Domain61 – 11050P-type 1
Domain932 – 97847P-type 2
Region110 – 1007898Isomaltase
Region1008 – 1827820Sucrase
Compositional bias43 – 6018Ser/Thr-rich

Sites

Active site5051Nucleophile; for isomaltase activity
Active site6041For isomaltase activity By similarity
Active site13941Nucleophile; for sucrase activity
Active site13971For sucrase activity
Active site15001Proton donor; for sucrase activity By similarity
Binding site2641Substrate By similarity
Binding site3881Substrate By similarity
Binding site5881Substrate By similarity
Binding site6621Substrate By similarity

Amino acid modifications

Modified residue71Phosphoserine; by PKA By similarity
Modified residue3911Sulfotyrosine Potential
Modified residue4001Sulfotyrosine Potential
Modified residue13821Sulfotyrosine Potential
Modified residue13851Sulfotyrosine Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation8591N-linked (GlcNAc...) Potential
Glycosylation8961N-linked (GlcNAc...) Potential
Glycosylation9041N-linked (GlcNAc...) Potential
Glycosylation10021N-linked (GlcNAc...) Potential
Glycosylation12351N-linked (GlcNAc...) Potential
Glycosylation13031N-linked (GlcNAc...) Potential
Glycosylation13251N-linked (GlcNAc...) Potential
Glycosylation13401N-linked (GlcNAc...) Potential
Glycosylation13541N-linked (GlcNAc...) Potential
Glycosylation13681N-linked (GlcNAc...) Potential
Glycosylation14031N-linked (GlcNAc...) Potential
Glycosylation15351N-linked (GlcNAc...) Potential
Glycosylation15721N-linked (GlcNAc...) Potential
Glycosylation17481N-linked (GlcNAc...) Potential
Glycosylation17631N-linked (GlcNAc...) Potential
Glycosylation17991N-linked (GlcNAc...) Potential
Disulfide bond63 ↔ 94 By similarity
Disulfide bond77 ↔ 93 By similarity
Disulfide bond88 ↔ 106 By similarity
Disulfide bond520 ↔ 545 By similarity
Disulfide bond635 ↔ 646 By similarity

Sequences

Sequence LengthMass (Da)Tools
P07768 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2CEFFE3109AC8917

FASTA1,827210,140
        10         20         30         40         50         60 
MAKRKFSGLE ITLIVLFVIV FIIAIALIAV LATKTPAVEE VNPSSSTPTT TSTTTSTSGS 

        70         80         90        100        110        120 
VSCPSELNEV VNERINCIPE QSPTQAICAQ RNCCWRPWNN SDIPWCFFVD NHGYNVEGMT 

       130        140        150        160        170        180 
TTSTGLEARL NRKSTPTLFG NDINNVLLTT ESQTANRLRF KLTDPNNKRY EVPHQFVTEF 

       190        200        210        220        230        240 
AGPAATETLY DVQVTENPFS IKVIRKSNNR ILFDSSIGPL VYSDQYLQIS TRLPSEYMYG 

       250        260        270        280        290        300 
FGEHVHKRFR HDLYWKTWPI FTRDQHTDDN NNNLYGHQTF FMCIEDTTGK SFGVFLMNSN 

       310        320        330        340        350        360 
AMEIFIQPTP IVTYRVIGGI LDFYIFLGDT PEQVVQQYQE LIGRPAMPAY WSLGFQLSRW 

       370        380        390        400        410        420 
NYNSLDVVKE VVRRNREALI PFDTQVSDID YMEDKKDFTY DRVAYNGLPD FVQDLHDHGQ 

       430        440        450        460        470        480 
KYVIILDPAI SINRRASGEA YESYDRGNAQ NVWVNESDGT TPIVGEVWPG DTVYPDFTSP 

       490        500        510        520        530        540 
NCIEWWANEC NIFHQEVNYD GLWIDMNEVS SFVQGSNKGC NDNTLNYPPY IPDIVDKLMY 

       550        560        570        580        590        600 
SKTLCMDSVQ YWGKQYDVHS LYGYSMAIAT ERAVERVFPN KRSFILTRST FAGSGRHAAH 

       610        620        630        640        650        660 
WLGDNTATWE QMEWSITGML EFGLFGMPLV GADICGFLAE TTEELCRRWM QLGAFYPFSR 

       670        680        690        700        710        720 
NHNADGFEHQ DPAFFGQDSL LVKSSRHYLN IRYTLLPFLY TLFYKAHAFG ETVARPVLHE 

       730        740        750        760        770        780 
FYEDTNSWVE DREFLWGPAL LITPVLTQGA ETVSAYIPDA VWYDYETGAK RPWRKQRVEM 

       790        800        810        820        830        840 
SLPADKIGLH LRGGYIIPIQ QPAVTTTASR MNPLGLIIAL NDDNTAVGDF FWDDGETKDT 

       850        860        870        880        890        900 
VQNDNYILYT FAVSNNNLNI TCTHELYSEG TTLAFQTIKI LGVTETVTQV TVAENNQSMS 

       910        920        930        940        950        960 
THSNFTYDPS NQVLLIENLN FNLGRNFRVQ WDQTFLESEK ITCYPDADIA TQEKCTQRGC 

       970        980        990       1000       1010       1020 
IWDTNTVNPR APECYFPKTD NPYSVSSTQY SPTGITADLQ LNPTRTRITL PSEPITNLRV 

      1030       1040       1050       1060       1070       1080 
EVKYHKNDMV QFKIFDPQNK RYEVPVPLDI PATPTSTQEN RLYDVEIKEN PFGIQIRRRS 

      1090       1100       1110       1120       1130       1140 
TGKVIWDSCL PGFAFNDQFI QISTRLPSEY IYGFGEAEHT AFKRDLNWHT WGMFTRDQPP 

      1150       1160       1170       1180       1190       1200 
GYKLNSYGFH PYYMALEDEG NAHGVLLLNS NAMDVTFMPT PALTYRVIGG ILDFYMFLGP 

      1210       1220       1230       1240       1250       1260 
TPEVATQQYH EVIGHPVMPP YWSLGFQLCR YGYRNTSEII ELYEGMVAAD IPYDVQYTDI 

      1270       1280       1290       1300       1310       1320 
DYMERQLDFT IDENFRELPQ FVDRIRGEGM RYIIILDPAI SGNETRPYPA FDRGEAKDVF 

      1330       1340       1350       1360       1370       1380 
VKWPNTSDIC WAKVWPDLPN ITIDESLTED EAVNASRAHA AFPDFFRNST AEWWTREILD 

      1390       1400       1410       1420       1430       1440 
FYNNYMKFDG LWIDMNEPSS FVNGTTTNVC RNTELNYPPY FPELTKRTDG LHFRTMCMET 

      1450       1460       1470       1480       1490       1500 
EHILSDGSSV LHYDVHNLYG WSQAKPTYDA LQKTTGKRGI VISRSTYPTA GRWAGHWLGD 

      1510       1520       1530       1540       1550       1560 
NYARWDNMDK SIIGMMEFSL FGISYTGADI CGFFNDSEYH LCTRWTQLGA FYPFARNHNI 

      1570       1580       1590       1600       1610       1620 
QFTRRQDPVS WNQTFVEMTR NVLNIRYTLL PYFYTQLHEI HAHGGTVIRP LMHEFFDDRT 

      1630       1640       1650       1660       1670       1680 
TWDIFLQFLW GPAFMVTPVL EPYTTVVRGY VPNARWFDYH TGEDIGIRGQ VQDLTLLMNA 

      1690       1700       1710       1720       1730       1740 
INLHVRGGHI LPCQEPARTT FLSRQKYMKL IVAADDNHMA QGSLFWDDGD TIDTYERDLY 

      1750       1760       1770       1780       1790       1800 
LSVQFNLNKT TLTSTLLKTG YINKTEIRLG YVHVWGIGNT LINEVNLMYN EINYPLIFNQ 

      1810       1820 
TQAQEILNID LTAHEVTLDD PIEISWS

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References

[1]"The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein."
Hunziker W., Spiess M., Semenza G., Lodish H.F.
Cell 46:227-234(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"N-terminal sequences of pig intestinal sucrase-isomaltase and pro-sucrase-isomaltase. Implications for the biosynthesis and membrane insertion of pro-sucrase-isomaltase."
Sjoestroem H., Noren O., Christiansen L.A., Wacker H., Spiess M., Bigler-Meier B., Rickli E.E., Semenza G.
FEBS Lett. 148:321-325(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-38 AND 1008-1015.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M14046 mRNA. Translation: AAA31459.1.
PIRA23945.
RefSeqNP_001075735.1. NM_001082266.1.
UniGeneOcu.1958.

3D structure databases

ProteinModelPortalP07768.
SMRP07768. Positions 73-931.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000003372.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009093.

Organism-specific databases

CTD6476.

Phylogenomic databases

eggNOGCOG1501.
HOGENOMHOG000067936.
HOVERGENHBG080721.
OrthoDBEOG4K6G3B.

Enzyme and pathway databases

BRENDA3.2.1.10. 1749.

Family and domain databases

Gene3D4.10.110.10. 2 hits.
InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]
PANTHERPTHR22762. PTHR22762. 1 hit.
PfamPF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]
SMARTSM00018. PD. 2 hits.
[Graphical view]
SUPFAMSSF74650. Gal_mut_like. 2 hits.
SSF51445. Glyco_hydro_cat. 2 hits.
SSF57492. P_trefoil. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
PS00707. GLYCOSYL_HYDROL_F31_2. 2 hits.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSUIS_RABIT
AccessionPrimary (citable) accession number: P07768
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents