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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 – 2641SubstrateBy similarity
Binding sitei388 – 3881SubstrateBy similarity
Active sitei505 – 5051Nucleophile; for isomaltase activity
Binding sitei588 – 5881SubstrateBy similarity
Active sitei604 – 6041For isomaltase activityBy similarity
Binding sitei662 – 6621SubstrateBy similarity
Active sitei1394 – 13941Nucleophile; for sucrase activity
Active sitei1397 – 13971For sucrase activity
Active sitei1500 – 15001Proton donor; for sucrase activityBy 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 – 1211CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 18271795LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma 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 – 11Removed
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 PKABy similarity
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi63 ↔ 94PROSITE-ProRule annotation
Disulfide bondi77 ↔ 93PROSITE-ProRule annotation
Disulfide bondi88 ↔ 106PROSITE-ProRule annotation
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Modified residuei391 – 3911SulfotyrosineSequence Analysis
Modified residuei400 – 4001SulfotyrosineSequence Analysis
Glycosylationi455 – 4551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi520 ↔ 545PROSITE-ProRule annotation
Disulfide bondi635 ↔ 646PROSITE-ProRule annotation
Glycosylationi859 – 8591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi896 – 8961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi904 – 9041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1002 – 10021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1235 – 12351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1303 – 13031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1325 – 13251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1368 – 13681N-linked (GlcNAc...)Sequence Analysis
Modified residuei1382 – 13821SulfotyrosineSequence Analysis
Modified residuei1385 – 13851SulfotyrosineSequence Analysis
Glycosylationi1403 – 14031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1535 – 15351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1572 – 15721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1748 – 17481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1799 – 17991N-linked (GlcNAc...)Sequence Analysis

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Belongs to the glycosyl hydrolase 31 family.Curated
Contains 2 P-type (trefoil) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1501.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.
InParanoidiP07768.

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

« Hide

        10         20         30         40         50
MAKRKFSGLE ITLIVLFVIV FIIAIALIAV LATKTPAVEE VNPSSSTPTT
60 70 80 90 100
TSTTTSTSGS VSCPSELNEV VNERINCIPE QSPTQAICAQ RNCCWRPWNN
110 120 130 140 150
SDIPWCFFVD NHGYNVEGMT TTSTGLEARL NRKSTPTLFG NDINNVLLTT
160 170 180 190 200
ESQTANRLRF KLTDPNNKRY EVPHQFVTEF AGPAATETLY DVQVTENPFS
210 220 230 240 250
IKVIRKSNNR ILFDSSIGPL VYSDQYLQIS TRLPSEYMYG FGEHVHKRFR
260 270 280 290 300
HDLYWKTWPI FTRDQHTDDN NNNLYGHQTF FMCIEDTTGK SFGVFLMNSN
310 320 330 340 350
AMEIFIQPTP IVTYRVIGGI LDFYIFLGDT PEQVVQQYQE LIGRPAMPAY
360 370 380 390 400
WSLGFQLSRW NYNSLDVVKE VVRRNREALI PFDTQVSDID YMEDKKDFTY
410 420 430 440 450
DRVAYNGLPD FVQDLHDHGQ KYVIILDPAI SINRRASGEA YESYDRGNAQ
460 470 480 490 500
NVWVNESDGT TPIVGEVWPG DTVYPDFTSP NCIEWWANEC NIFHQEVNYD
510 520 530 540 550
GLWIDMNEVS SFVQGSNKGC NDNTLNYPPY IPDIVDKLMY SKTLCMDSVQ
560 570 580 590 600
YWGKQYDVHS LYGYSMAIAT ERAVERVFPN KRSFILTRST FAGSGRHAAH
610 620 630 640 650
WLGDNTATWE QMEWSITGML EFGLFGMPLV GADICGFLAE TTEELCRRWM
660 670 680 690 700
QLGAFYPFSR NHNADGFEHQ DPAFFGQDSL LVKSSRHYLN IRYTLLPFLY
710 720 730 740 750
TLFYKAHAFG ETVARPVLHE FYEDTNSWVE DREFLWGPAL LITPVLTQGA
760 770 780 790 800
ETVSAYIPDA VWYDYETGAK RPWRKQRVEM SLPADKIGLH LRGGYIIPIQ
810 820 830 840 850
QPAVTTTASR MNPLGLIIAL NDDNTAVGDF FWDDGETKDT VQNDNYILYT
860 870 880 890 900
FAVSNNNLNI TCTHELYSEG TTLAFQTIKI LGVTETVTQV TVAENNQSMS
910 920 930 940 950
THSNFTYDPS NQVLLIENLN FNLGRNFRVQ WDQTFLESEK ITCYPDADIA
960 970 980 990 1000
TQEKCTQRGC IWDTNTVNPR APECYFPKTD NPYSVSSTQY SPTGITADLQ
1010 1020 1030 1040 1050
LNPTRTRITL PSEPITNLRV EVKYHKNDMV QFKIFDPQNK RYEVPVPLDI
1060 1070 1080 1090 1100
PATPTSTQEN RLYDVEIKEN PFGIQIRRRS TGKVIWDSCL PGFAFNDQFI
1110 1120 1130 1140 1150
QISTRLPSEY IYGFGEAEHT AFKRDLNWHT WGMFTRDQPP GYKLNSYGFH
1160 1170 1180 1190 1200
PYYMALEDEG NAHGVLLLNS NAMDVTFMPT PALTYRVIGG ILDFYMFLGP
1210 1220 1230 1240 1250
TPEVATQQYH EVIGHPVMPP YWSLGFQLCR YGYRNTSEII ELYEGMVAAD
1260 1270 1280 1290 1300
IPYDVQYTDI DYMERQLDFT IDENFRELPQ FVDRIRGEGM RYIIILDPAI
1310 1320 1330 1340 1350
SGNETRPYPA FDRGEAKDVF VKWPNTSDIC WAKVWPDLPN ITIDESLTED
1360 1370 1380 1390 1400
EAVNASRAHA AFPDFFRNST AEWWTREILD FYNNYMKFDG LWIDMNEPSS
1410 1420 1430 1440 1450
FVNGTTTNVC RNTELNYPPY FPELTKRTDG LHFRTMCMET EHILSDGSSV
1460 1470 1480 1490 1500
LHYDVHNLYG WSQAKPTYDA LQKTTGKRGI VISRSTYPTA GRWAGHWLGD
1510 1520 1530 1540 1550
NYARWDNMDK SIIGMMEFSL FGISYTGADI CGFFNDSEYH LCTRWTQLGA
1560 1570 1580 1590 1600
FYPFARNHNI QFTRRQDPVS WNQTFVEMTR NVLNIRYTLL PYFYTQLHEI
1610 1620 1630 1640 1650
HAHGGTVIRP LMHEFFDDRT TWDIFLQFLW GPAFMVTPVL EPYTTVVRGY
1660 1670 1680 1690 1700
VPNARWFDYH TGEDIGIRGQ VQDLTLLMNA INLHVRGGHI LPCQEPARTT
1710 1720 1730 1740 1750
FLSRQKYMKL IVAADDNHMA QGSLFWDDGD TIDTYERDLY LSVQFNLNKT
1760 1770 1780 1790 1800
TLTSTLLKTG YINKTEIRLG YVHVWGIGNT LINEVNLMYN EINYPLIFNQ
1810 1820
TQAQEILNID LTAHEVTLDD PIEISWS
Length:1,827
Mass (Da):210,140
Last modified:January 23, 2007 - v3
Checksum:i2CEFFE3109AC8917
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P07768.

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: October 29, 2014
This is version 115 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