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P07768

- SUIS_RABIT

UniProt

P07768 - SUIS_RABIT

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Protein

Sucrase-isomaltase, intestinal

Gene
SI
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei264 – 2641Substrate By similarity
Binding sitei388 – 3881Substrate By similarity
Active sitei505 – 5051Nucleophile; for isomaltase activity
Binding sitei588 – 5881Substrate By similarity
Active sitei604 – 6041For isomaltase activity By similarity
Binding sitei662 – 6621Substrate By similarity
Active sitei1394 – 13941Nucleophile; for sucrase activity
Active sitei1397 – 13971For sucrase activity
Active sitei1500 – 15001Proton donor; for sucrase activity By similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. oligo-1,6-glucosidase activity Source: UniProtKB-EC
  3. sucrose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.10. 1749.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrase-isomaltase, intestinal
Cleaved into the following 2 chains:
Gene namesi
Name:SI
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini33 – 18271795Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 18271826Sucrase-isomaltase, intestinalPRO_0000018556Add
BLAST
Chaini2 – 10071006IsomaltasePRO_0000018557Add
BLAST
Chaini1008 – 1827820SucrasePRO_0000018558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by PKA By similarity
Glycosylationi42 – 421N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi63 ↔ 94 By similarity
Disulfide bondi77 ↔ 93 By similarity
Disulfide bondi88 ↔ 106 By similarity
Glycosylationi99 – 991N-linked (GlcNAc...) Reviewed prediction
Modified residuei391 – 3911Sulfotyrosine Reviewed prediction
Modified residuei400 – 4001Sulfotyrosine Reviewed prediction
Glycosylationi455 – 4551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi520 ↔ 545 By similarity
Disulfide bondi635 ↔ 646 By similarity
Glycosylationi859 – 8591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi896 – 8961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi904 – 9041N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1002 – 10021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1235 – 12351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1303 – 13031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1325 – 13251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1340 – 13401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1354 – 13541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1368 – 13681N-linked (GlcNAc...) Reviewed prediction
Modified residuei1382 – 13821Sulfotyrosine Reviewed prediction
Modified residuei1385 – 13851Sulfotyrosine Reviewed prediction
Glycosylationi1403 – 14031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1535 – 15351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1572 – 15721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1748 – 17481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1763 – 17631N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1799 – 17991N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.
N- and O-glycosylated.
Sulfated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000003372.

Structurei

3D structure databases

ProteinModelPortaliP07768.
SMRiP07768. Positions 73-931.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 11050P-type 1Add
BLAST
Domaini932 – 97847P-type 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 1007898IsomaltaseAdd
BLAST
Regioni1008 – 1827820SucraseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi43 – 6018Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1501.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.

Family and domain databases

Gene3Di4.10.110.10. 2 hits.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]
SMARTiSM00018. PD. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 4 hits.
SSF57492. SSF57492. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEiPS00129. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07768-1 [UniParc]FASTAAdd to Basket

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MAKRKFSGLE ITLIVLFVIV FIIAIALIAV LATKTPAVEE VNPSSSTPTT     50
TSTTTSTSGS VSCPSELNEV VNERINCIPE QSPTQAICAQ RNCCWRPWNN 100
SDIPWCFFVD NHGYNVEGMT TTSTGLEARL NRKSTPTLFG NDINNVLLTT 150
ESQTANRLRF KLTDPNNKRY EVPHQFVTEF AGPAATETLY DVQVTENPFS 200
IKVIRKSNNR ILFDSSIGPL VYSDQYLQIS TRLPSEYMYG FGEHVHKRFR 250
HDLYWKTWPI FTRDQHTDDN NNNLYGHQTF FMCIEDTTGK SFGVFLMNSN 300
AMEIFIQPTP IVTYRVIGGI LDFYIFLGDT PEQVVQQYQE LIGRPAMPAY 350
WSLGFQLSRW NYNSLDVVKE VVRRNREALI PFDTQVSDID YMEDKKDFTY 400
DRVAYNGLPD FVQDLHDHGQ KYVIILDPAI SINRRASGEA YESYDRGNAQ 450
NVWVNESDGT TPIVGEVWPG DTVYPDFTSP NCIEWWANEC NIFHQEVNYD 500
GLWIDMNEVS SFVQGSNKGC NDNTLNYPPY IPDIVDKLMY SKTLCMDSVQ 550
YWGKQYDVHS LYGYSMAIAT ERAVERVFPN KRSFILTRST FAGSGRHAAH 600
WLGDNTATWE QMEWSITGML EFGLFGMPLV GADICGFLAE TTEELCRRWM 650
QLGAFYPFSR NHNADGFEHQ DPAFFGQDSL LVKSSRHYLN IRYTLLPFLY 700
TLFYKAHAFG ETVARPVLHE FYEDTNSWVE DREFLWGPAL LITPVLTQGA 750
ETVSAYIPDA VWYDYETGAK RPWRKQRVEM SLPADKIGLH LRGGYIIPIQ 800
QPAVTTTASR MNPLGLIIAL NDDNTAVGDF FWDDGETKDT VQNDNYILYT 850
FAVSNNNLNI TCTHELYSEG TTLAFQTIKI LGVTETVTQV TVAENNQSMS 900
THSNFTYDPS NQVLLIENLN FNLGRNFRVQ WDQTFLESEK ITCYPDADIA 950
TQEKCTQRGC IWDTNTVNPR APECYFPKTD NPYSVSSTQY SPTGITADLQ 1000
LNPTRTRITL PSEPITNLRV EVKYHKNDMV QFKIFDPQNK RYEVPVPLDI 1050
PATPTSTQEN RLYDVEIKEN PFGIQIRRRS TGKVIWDSCL PGFAFNDQFI 1100
QISTRLPSEY IYGFGEAEHT AFKRDLNWHT WGMFTRDQPP GYKLNSYGFH 1150
PYYMALEDEG NAHGVLLLNS NAMDVTFMPT PALTYRVIGG ILDFYMFLGP 1200
TPEVATQQYH EVIGHPVMPP YWSLGFQLCR YGYRNTSEII ELYEGMVAAD 1250
IPYDVQYTDI DYMERQLDFT IDENFRELPQ FVDRIRGEGM RYIIILDPAI 1300
SGNETRPYPA FDRGEAKDVF VKWPNTSDIC WAKVWPDLPN ITIDESLTED 1350
EAVNASRAHA AFPDFFRNST AEWWTREILD FYNNYMKFDG LWIDMNEPSS 1400
FVNGTTTNVC RNTELNYPPY FPELTKRTDG LHFRTMCMET EHILSDGSSV 1450
LHYDVHNLYG WSQAKPTYDA LQKTTGKRGI VISRSTYPTA GRWAGHWLGD 1500
NYARWDNMDK SIIGMMEFSL FGISYTGADI CGFFNDSEYH LCTRWTQLGA 1550
FYPFARNHNI QFTRRQDPVS WNQTFVEMTR NVLNIRYTLL PYFYTQLHEI 1600
HAHGGTVIRP LMHEFFDDRT TWDIFLQFLW GPAFMVTPVL EPYTTVVRGY 1650
VPNARWFDYH TGEDIGIRGQ VQDLTLLMNA INLHVRGGHI LPCQEPARTT 1700
FLSRQKYMKL IVAADDNHMA QGSLFWDDGD TIDTYERDLY LSVQFNLNKT 1750
TLTSTLLKTG YINKTEIRLG YVHVWGIGNT LINEVNLMYN EINYPLIFNQ 1800
TQAQEILNID LTAHEVTLDD PIEISWS 1827
Length:1,827
Mass (Da):210,140
Last modified:January 23, 2007 - v3
Checksum:i2CEFFE3109AC8917
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14046 mRNA. Translation: AAA31459.1.
PIRiA23945.
RefSeqiNP_001075735.1. NM_001082266.1.
UniGeneiOcu.1958.

Genome annotation databases

GeneIDi100009093.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14046 mRNA. Translation: AAA31459.1 .
PIRi A23945.
RefSeqi NP_001075735.1. NM_001082266.1.
UniGenei Ocu.1958.

3D structure databases

ProteinModelPortali P07768.
SMRi P07768. Positions 73-931.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000003372.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009093.

Organism-specific databases

CTDi 6476.

Phylogenomic databases

eggNOGi COG1501.
HOGENOMi HOG000067936.
HOVERGENi HBG080721.

Enzyme and pathway databases

BRENDAi 3.2.1.10. 1749.

Family and domain databases

Gene3Di 4.10.110.10. 2 hits.
InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view ]
Pfami PF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view ]
SMARTi SM00018. PD. 2 hits.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 4 hits.
SSF57492. SSF57492. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEi PS00129. 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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiSUIS_RABIT
AccessioniPrimary (citable) accession number: P07768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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