P14410 (SUIS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1827 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.7
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.
Tissue specificity	Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon. Ref.5
Post-translational modification	The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen. Sulfated By similarity.
Involvement in disease	Congenital sucrase-isomaltase deficiency (CSID) [MIM:222900]: Autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Repeat Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein Sulfation
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome polysaccharide digestion Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Traceable author statement PubMed 1717481. Source: ProtInc apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell brush border Traceable author statement PubMed 1717481. Source: ProtInc integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro oligo-1,6-glucosidase activity Inferred from electronic annotation. Source: EC sucrose alpha-glucosidase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 1827

1826

Sucrase-isomaltase, intestinal

PRO_0000018551

Chain

2 – 1007

1006

Isomaltase

PRO_0000018552

Chain

1008 – 1827

820

Sucrase

PRO_0000018553

Regions

Topological domain

2 – 12

11

Cytoplasmic

Transmembrane

13 – 32

20

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

33 – 1827

1795

Lumenal

Domain

61 – 110

50

P-type 1

Domain

932 – 978

47

P-type 2

Region

110 – 1007

898

Isomaltase

Region

1008 – 1827

820

Sucrase

Compositional bias

43 – 60

18

Ser/Thr-rich

Sites

Active site

505

1

Nucleophile; for isomaltase activity Ref.7

Active site

604

1

For isomaltase activity Ref.7

Active site

1394

1

Nucleophile; for sucrase activity Ref.7

Active site

1397

1

For sucrase activity By similarity

Active site

1500

1

Proton donor; for isomaltase activity By similarity

Binding site

264

1

Substrate

Binding site

388

1

Substrate

Binding site

588

1

Substrate

Binding site

662

1

Substrate

Amino acid modifications

Modified residue

7

1

Phosphoserine; by PKA Ref.6

Modified residue

237

1

Sulfotyrosine Potential

Modified residue

239

1

Sulfotyrosine Potential

Modified residue

391

1

Sulfotyrosine Potential

Modified residue

400

1

Sulfotyrosine Potential

Modified residue

667

1

Sulfotyrosine Potential

Modified residue

763

1

Sulfotyrosine Potential

Modified residue

765

1

Sulfotyrosine Potential

Glycosylation

99

1

N-linked (GlcNAc...) Ref.7

Glycosylation

437

1

N-linked (GlcNAc...) Potential

Glycosylation

455

1

N-linked (GlcNAc...) Ref.7

Glycosylation

823

1

N-linked (GlcNAc...) Potential

Glycosylation

855

1

N-linked (GlcNAc...) Ref.7

Glycosylation

904

1

N-linked (GlcNAc...) Ref.7

Glycosylation

926

1

N-linked (GlcNAc...) Potential

Glycosylation

1235

1

N-linked (GlcNAc...) Potential

Glycosylation

1303

1

N-linked (GlcNAc...) Potential

Glycosylation

1340

1

N-linked (GlcNAc...) Potential

Glycosylation

1354

1

N-linked (GlcNAc...) Potential

Glycosylation

1403

1

N-linked (GlcNAc...) Potential

Glycosylation

1535

1

N-linked (GlcNAc...) Potential

Glycosylation

1572

1

N-linked (GlcNAc...) Potential

Glycosylation

1675

1

N-linked (GlcNAc...) Potential

Glycosylation

1748

1

N-linked (GlcNAc...) Potential

Glycosylation

1763

1

N-linked (GlcNAc...) Potential

Glycosylation

1815

1

N-linked (GlcNAc...) Potential

Disulfide bond

63 ↔ 94

Ref.7

Disulfide bond

77 ↔ 93

Ref.7

Disulfide bond

88 ↔ 106

Ref.7

Disulfide bond

520 ↔ 545

Ref.7

Disulfide bond

635 ↔ 646

Ref.7

Natural variations

Natural variant

15

1

V → F. Ref.3 Ref.5 Ref.11 Ref.12
Corresponds to variant rs9290264 [ dbSNP | Ensembl ].

VAR_025367

Natural variant

117

1

Q → R in CSID; missorting of the enzyme to the basolateral membrane. Ref.10

VAR_025368

Natural variant

231

1

T → A. Ref.1 Ref.3 Ref.4 Ref.11 Ref.12
Corresponds to variant rs9283633 [ dbSNP | Ensembl ].

VAR_025369

Natural variant

341

1

L → P in CSID; causes loss of anchored SI from the membrane. Ref.9

VAR_025370

Natural variant

577

1

V → G in CSID. Ref.12

VAR_025371

Natural variant

594

1

S → P in CSID. Ref.12

VAR_025372

Natural variant

620

1

L → P in CSID; SI accumulates predominantly in the ER. Ref.11

VAR_025373

Natural variant

694

1

T → P in CSID. Ref.12

VAR_025374

Natural variant

1073

1

G → D in CSID. Ref.12

VAR_025375

Natural variant

1098

1

Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. Ref.8

VAR_007854

Natural variant

1229

1

C → Y in CSID. Ref.12

VAR_025376

Natural variant

1367

1

R → G in CSID. Ref.12

VAR_025377

Natural variant

1523

1

M → I. Ref.1 Ref.3 Ref.12
Corresponds to variant rs4855271 [ dbSNP | Ensembl ].

VAR_025378

Natural variant

1745

1

F → C in CSID. Ref.12

VAR_025379

Natural variant

1802

1

T → S.
Corresponds to variant rs9917722 [ dbSNP | Ensembl ].

VAR_034522

Experimental info

Sequence conflict

300

1

N → D in AAI16453. Ref.3

Sequence conflict

460

1

S → I in AAI15035. Ref.3

Sequence conflict

475

1

P → S in AAI15035. Ref.3

Sequence conflict

548

1

A → V in AAI16453. Ref.3

Sequence conflict

584

1

F → L in AAI15035. Ref.3

Sequence conflict

588

1

R → C in AAI15035. Ref.3

Sequence conflict

633

1

D → A in AAI15035. Ref.3

Sequence conflict

687

1

Q → R in AAI16453. Ref.3

Sequence conflict

884

1

T → A in AAI15035. Ref.3

Sequence conflict

1016

1

S → E AA sequence Ref.5

Sequence conflict

1022

1

V → T AA sequence Ref.5

Sequence conflict

1155

1

A → V in AAI15035. Ref.3

Sequence conflict

1203

1

E → Q in CAA45140. Ref.1

Sequence conflict

1782

1

V → I in AAI15035. Ref.3

Sequence conflict

1825

1

N → S in AAI16453. Ref.3

Secondary structure

1

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1827

Helix Strand Turn

Details...

Beta strand

65 – 68

4

Helix

71 – 73

3

Beta strand

75 – 77

3

Helix

85 – 91

7

Beta strand

99 – 103

5

Beta strand

105 – 107

3

Beta strand

114 – 121

8

Beta strand

123 – 132

10

Beta strand

138 – 140

3

Beta strand

144 – 154

11

Beta strand

157 – 163

7

Beta strand

175 – 177

3

Beta strand

189 – 195

7

Turn

196 – 199

4

Beta strand

200 – 205

6

Turn

206 – 209

4

Beta strand

210 – 214

5

Helix

215 – 217

3

Beta strand

221 – 223

3

Beta strand

226 – 232

7

Beta strand

234 – 236

3

Beta strand

238 – 244

7

Beta strand

247 – 250

4

Beta strand

254 – 261

8

Beta strand

278 – 284

7

Beta strand

291 – 296

6

Beta strand

302 – 307

6

Turn

308 – 310

3

Beta strand

311 – 319

9

Beta strand

321 – 330

10

Helix

331 – 342

12

Helix

350 – 353

4

Helix

365 – 377

13

Beta strand

384 – 387

4

Helix

389 – 391

3

Helix

393 – 395

3

Turn

402 – 407

6

Helix

408 – 417

10

Beta strand

421 – 426

6

Helix

442 – 450

9

Beta strand

459 – 462

4

Beta strand

465 – 467

3

Beta strand

470 – 473

4

Helix

480 – 496

17

Beta strand

500 – 504

5

Turn

507 – 509

3

Beta strand

512 – 515

4

Turn

524 – 526

3

Helix

535 – 537

3

Turn

539 – 542

4

Helix

555 – 558

4

Helix

559 – 561

3

Helix

562 – 577

16

Beta strand

585 – 588

4

Helix

594 – 596

3

Beta strand

599 – 601

3

Beta strand

606 – 608

3

Helix

609 – 624

16

Beta strand

629 – 631

3

Beta strand

637 – 639

3

Helix

643 – 653

11

Beta strand

656 – 658

3

Helix

672 – 675

4

Helix

680 – 694

15

Helix

696 – 709

14

Beta strand

713 – 715

3

Helix

718 – 721

4

Helix

725 – 729

5

Beta strand

732 – 736

5

Turn

737 – 739

3

Beta strand

740 – 743

4

Beta strand

751 – 757

7

Beta strand

762 – 764

3

Turn

765 – 767

3

Beta strand

775 – 781

7

Beta strand

788 – 792

5

Beta strand

795 – 800

6

Helix

806 – 809

4

Beta strand

814 – 819

6

Beta strand

824 – 832

9

Beta strand

835 – 837

3

Helix

840 – 843

4

Beta strand

846 – 854

9

Beta strand

857 – 865

9

Helix

868 – 872

5

Beta strand

874 – 882

9

Beta strand

890 – 894

5

Beta strand

900 – 902

3

Beta strand

905 – 908

4

Turn

909 – 912

4

Beta strand

913 – 916

4

Beta strand

927 – 930

4

Sequences

	Sequence		Length	Mass (Da)
	P14410 [UniParc]. Last modified January 11, 2011. Version 6. Checksum: DCB93F068AEEF83E	FASTA	1,827	209,453
	10 20 30 40 50 60 MARKKFSGLE ISLIVLFVIV TIIAIALIVV LATKTPAVDE ISDSTSTPAT TRVTTNPSDS 70 80 90 100 110 120 GKCPNVLNDP VNVRINCIPE QFPTEGICAQ RGCCWRPWND SLIPWCFFVD NHGYNVQDMT 130 140 150 160 170 180 TTSIGVEAKL NRIPSPTLFG NDINSVLFTT QNQTPNRFRF KITDPNNRRY EVPHQYVKEF 190 200 210 220 230 240 TGPTVSDTLY DVKVAQNPFS IQVIRKSNGK TLFDTSIGPL VYSDQYLQIS TRLPSDYIYG 250 260 270 280 290 300 IGEQVHKRFR HDLSWKTWPI FTRDQLPGDN NNNLYGHQTF FMCIEDTSGK SFGVFLMNSN 310 320 330 340 350 360 AMEIFIQPTP IVTYRVTGGI LDFYILLGDT PEQVVQQYQQ LVGLPAMPAY WNLGFQLSRW 370 380 390 400 410 420 NYKSLDVVKE VVRRNREAGI PFDTQVTDID YMEDKKDFTY DQVAFNGLPQ FVQDLHDHGQ 430 440 450 460 470 480 KYVIILDPAI SIGRRANGTT YATYERGNTQ HVWINESDGS TPIIGEVWPG LTVYPDFTNP 490 500 510 520 530 540 NCIDWWANEC SIFHQEVQYD GLWIDMNEVS SFIQGSTKGC NVNKLNYPPF TPDILDKLMY 550 560 570 580 590 600 SKTICMDAVQ NWGKQYDVHS LYGYSMAIAT EQAVQKVFPN KRSFILTRST FAGSGRHAAH 610 620 630 640 650 660 WLGDNTASWE QMEWSITGML EFSLFGIPLV GADICGFVAE TTEELCRRWM QLGAFYPFSR 670 680 690 700 710 720 NHNSDGYEHQ DPAFFGQNSL LVKSSRQYLT IRYTLLPFLY TLFYKAHVFG ETVARPVLHE 730 740 750 760 770 780 FYEDTNSWIE DTEFLWGPAL LITPVLKQGA DTVSAYIPDA IWYDYESGAK RPWRKQRVDM 790 800 810 820 830 840 YLPADKIGLH LRGGYIIPIQ EPDVTTTASR KNPLGLIVAL GENNTAKGDF FWDDGETKDT 850 860 870 880 890 900 IQNGNYILYT FSVSNNTLDI VCTHSSYQEG TTLAFQTVKI LGLTDSVTEV RVAENNQPMN 910 920 930 940 950 960 AHSNFTYDAS NQVLLIADLK LNLGRNFSVQ WNQIFSENER FNCYPDADLA TEQKCTQRGC 970 980 990 1000 1010 1020 VWRTGSSLSK APECYFPRQD NSYSVNSARY SSMGITADLQ LNTANARIKL PSDPISTLRV 1030 1040 1050 1060 1070 1080 EVKYHKNDML QFKIYDPQKK RYEVPVPLNI PTTPISTYED RLYDVEIKEN PFGIQIRRRS 1090 1100 1110 1120 1130 1140 SGRVIWDSWL PGFAFNDQFI QISTRLPSEY IYGFGEVEHT AFKRDLNWNT WGMFTRDQPP 1150 1160 1170 1180 1190 1200 GYKLNSYGFH PYYMALEEEG NAHGVFLLNS NAMDVTFQPT PALTYRTVGG ILDFYMFLGP 1210 1220 1230 1240 1250 1260 TPEVATKQYH EVIGHPVMPA YWALGFQLCR YGYANTSEVR ELYDAMVAAN IPYDVQYTDI 1270 1280 1290 1300 1310 1320 DYMERQLDFT IGEAFQDLPQ FVDKIRGEGM RYIIILDPAI SGNETKTYPA FERGQQNDVF 1330 1340 1350 1360 1370 1380 VKWPNTNDIC WAKVWPDLPN ITIDKTLTED EAVNASRAHV AFPDFFRTST AEWWAREIVD 1390 1400 1410 1420 1430 1440 FYNEKMKFDG LWIDMNEPSS FVNGTTTNQC RNDELNYPPY FPELTKRTDG LHFRTICMEA 1450 1460 1470 1480 1490 1500 EQILSDGTSV LHYDVHNLYG WSQMKPTHDA LQKTTGKRGI VISRSTYPTS GRWGGHWLGD 1510 1520 1530 1540 1550 1560 NYARWDNMDK SIIGMMEFSL FGMSYTGADI CGFFNNSEYH LCTRWMQLGA FYPYSRNHNI 1570 1580 1590 1600 1610 1620 ANTRRQDPAS WNETFAEMSR NILNIRYTLL PYFYTQMHEI HANGGTVIRP LLHEFFDEKP 1630 1640 1650 1660 1670 1680 TWDIFKQFLW GPAFMVTPVL EPYVQTVNAY VPNARWFDYH TGKDIGVRGQ FQTFNASYDT 1690 1700 1710 1720 1730 1740 INLHVRGGHI LPCQEPAQNT FYSRQKHMKL IVAADDNQMA QGSLFWDDGE SIDTYERDLY 1750 1760 1770 1780 1790 1800 LSVQFNLNQT TLTSTILKRG YINKSETRLG SLHVWGKGTT PVNAVTLTYN GNKNSLPFNE 1810 1820 DTTNMILRID LTTHNVTLEE PIEINWS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase." Chantret I., Lacasa M., Chevalier G., Ruf J., Islam I., Mantei N., Edwards Y., Swallow D., Rousset M. Biochem. J. 285:915-923(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-231 AND ILE-1523. Tissue: Intestine.
[2]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PHE-15; ALA-231 AND ILE-1523.
[4]	"Isolation of a cDNA probe for a human jejunal brush-border hydrolase, sucrase-isomaltase, and assignment of the gene locus to chromosome 3." Green F., Edwards Y., Hauri H.-P., Povey S., Ho M.W., Pinto M., Swallow D. Gene 57:101-110(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-679, VARIANT ALA-231.
[5]	"Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon." Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S. Gastroenterology 101:618-625(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20 AND 1008-1024, TISSUE SPECIFICITY, VARIANT PHE-15.
[6]	"Phosphorylation of the N-terminal intracellular tail of sucrase-isomaltase by cAMP-dependent protein kinase." Keller P., Semenza G., Shaltiel S. Eur. J. Biochem. 233:963-968(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-7.
[7]	"Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains." Sim L., Willemsma C., Mohan S., Naim H.Y., Pinto B.M., Rose D.R. J. Biol. Chem. 285:17763-17770(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 62-931 ALONE AND IN COMPLEX WITH INHIBITOR, GLYCOSYLATION AT ASN-99; ASN-455; ASN-855 AND ASN-904, FUNCTION, ACTIVE SITE, SUBSTRATE-BINDING SITES, DISULFIDE BONDS.
[8]	"Congenital sucrase-isomaltase deficiency: identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment." Ouwendijk J., Moolenaar C.E.C., Peters W.J., Hollenberg C.P., Ginsel L.A., Fransen J.A.M., Naim H.Y. J. Clin. Invest. 97:633-641(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSID PRO-1098.
[9]	"Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme." Jacob R., Zimmer K.P., Schmitz J., Naim H.Y. J. Clin. Invest. 106:281-287(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSID PRO-341, CHARACTERIZATION OF VARIANT CSID PRO-341.
[10]	"Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder." Spodsberg N., Jacob R., Alfalah M., Zimmer K.P., Naim H.Y. J. Biol. Chem. 276:23506-23510(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSID ARG-117, CHARACTERIZATION OF VARIANT CSID ARG-117.
[11]	"Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum." Ritz V., Alfalah M., Zimmer K.P., Schmitz J., Jacob R., Naim H.Y. Gastroenterology 125:1678-1685(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-15 AND ALA-231, VARIANT CSID PRO-620.
[12]	"Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption." Sander P., Alfalah M., Keiser M., Korponay-Szabo I., Kovacs J.B., Leeb T., Naim H.Y. Hum. Mutat. 27:119-119(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CSID GLY-577; PRO-594; PRO-694; ASP-1073; TYR-1229; GLY-1367 AND CYS-1745, VARIANTS PHE-15; ALA-231 AND ILE-1523.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X63597 mRNA. Translation: CAA45140.1.
AC092695 Genomic DNA. No translation available.
AC140119 Genomic DNA. No translation available.
AC144561 Genomic DNA. No translation available.
BC115034 mRNA. Translation: AAI15035.1.
BC116452 mRNA. Translation: AAI16453.1.
BC132834 mRNA. Translation: AAI32835.1.
BC132860 mRNA. Translation: AAI32861.1.
M22616 mRNA. Translation: AAA60551.1.

IPI

IPI00221101.

PIR

UUHU. S36082.

RefSeq

NP_001032.2. NM_001041.3.

UniGene

Hs.429596.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LPO	X-ray	3.20	A/B/C/D	62-931	[»]
3LPP	X-ray	2.15	A/B/C/D	62-931	[»]

ProteinModelPortal

P14410.

SMR

P14410. Positions 62-931, 937-1818.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000264382.

Protein family/group databases

CAZy

GH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSite

P14410.

Polymorphism databases

DMDM

229463051.

Proteomic databases

PaxDb

P14410.

PRIDE

P14410.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264382; ENSP00000264382; ENSG00000090402.

GeneID

6476.

KEGG

hsa:6476.

UCSC

uc003fei.3. human.

Organism-specific databases

CTD

6476.

GeneCards

GC03M164696.

H-InvDB

HIX0030867.

HGNC

HGNC:10856. SI.

HPA

HPA011897.

MIM

222900. phenotype.
609845. gene.

neXtProt

NX_P14410.

Orphanet

35122. Congenital sucrase-isomaltase deficiency.

PharmGKB

PA35758.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1501.

HOGENOM

HOG000067936.

HOVERGEN

HBG080721.

InParanoid

P14410.

KO

K01203.

OMA

AKGDFFW.

OrthoDB

EOG4K6G3B.

PhylomeDB

P14410.

Enzyme and pathway databases

BioCyc

MetaCyc:HS01688-MONOMER.

BRENDA

3.2.1.10. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P14410.

Bgee

P14410.

CleanEx

HS_SI.

Genevestigator

P14410.

GermOnline

ENSG00000090402. Homo sapiens.

Family and domain databases

Gene3D

4.10.110.10. 2 hits.

InterPro

IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]

PANTHER

PTHR22762. PTHR22762. 1 hit.

Pfam

PF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]

SMART

SM00018. PD. 2 hits.
[Graphical view]

SUPFAM

SSF74650. Gal_mut_like. 2 hits.
SSF51445. Glyco_hydro_cat. 2 hits.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

P14410.

ChEMBL

CHEMBL2748.

DrugBank

DB00284. Acarbose.

EvolutionaryTrace

P14410.

GenomeRNAi

6476.

NextBio

25157.

SOURCE

Search...

Entry information

Entry name

SUIS_HUMAN

Accession

Primary (citable) accession number: P14410
Secondary accession number(s): A2RUC3, Q1JQ80, Q1RMC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 142 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.