SUIS_HUMAN
ID SUIS_HUMAN Reviewed; 1827 AA.
AC P14410; A2RUC3; Q1JQ80; Q1RMC2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 6.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Sucrase-isomaltase, intestinal;
DE Contains:
DE RecName: Full=Sucrase;
DE EC=3.2.1.48;
DE Contains:
DE RecName: Full=Isomaltase;
DE EC=3.2.1.10;
GN Name=SI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-231 AND ILE-1523.
RC TISSUE=Intestine;
RX PubMed=1353958; DOI=10.1042/bj2850915;
RA Chantret I., Lacasa M., Chevalier G., Ruf J., Islam I., Mantei N.,
RA Edwards Y., Swallow D., Rousset M.;
RT "Sequence of the complete cDNA and the 5' structure of the human sucrase-
RT isomaltase gene. Possible homology with a yeast glucoamylase.";
RL Biochem. J. 285:915-923(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PHE-15; ALA-231 AND
RP ILE-1523.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-679, AND VARIANT ALA-231.
RX PubMed=2962903; DOI=10.1016/0378-1119(87)90181-8;
RA Green F., Edwards Y., Hauri H.-P., Povey S., Ho M.W., Pinto M., Swallow D.;
RT "Isolation of a cDNA probe for a human jejunal brush-border hydrolase,
RT sucrase-isomaltase, and assignment of the gene locus to chromosome 3.";
RL Gene 57:101-110(1987).
RN [5]
RP PROTEIN SEQUENCE OF 2-20 AND 1008-1024, TISSUE SPECIFICITY, AND VARIANT
RP PHE-15.
RX PubMed=1677636; DOI=10.1016/0016-5085(91)90517-o;
RA Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S.;
RT "Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small
RT intestine and colon.";
RL Gastroenterology 101:618-625(1991).
RN [6]
RP PHOSPHORYLATION AT SER-7.
RX PubMed=8521865; DOI=10.1111/j.1432-1033.1995.963_3.x;
RA Keller P., Semenza G., Shaltiel S.;
RT "Phosphorylation of the N-terminal intracellular tail of sucrase-isomaltase
RT by cAMP-dependent protein kinase.";
RL Eur. J. Biochem. 233:963-968(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 62-931 ALONE AND IN COMPLEX WITH
RP INHIBITOR, GLYCOSYLATION AT ASN-99; ASN-455; ASN-855 AND ASN-904, FUNCTION,
RP ACTIVE SITE, SUBSTRATE-BINDING SITES, AND DISULFIDE BONDS.
RX PubMed=20356844; DOI=10.1074/jbc.m109.078980;
RA Sim L., Willemsma C., Mohan S., Naim H.Y., Pinto B.M., Rose D.R.;
RT "Structural basis for substrate selectivity in human maltase-glucoamylase
RT and sucrase-isomaltase N-terminal domains.";
RL J. Biol. Chem. 285:17763-17770(2010).
RN [8]
RP VARIANT CSID PRO-1098.
RX PubMed=8609217; DOI=10.1172/jci118459;
RA Ouwendijk J., Moolenaar C.E.C., Peters W.J., Hollenberg C.P., Ginsel L.A.,
RA Fransen J.A.M., Naim H.Y.;
RT "Congenital sucrase-isomaltase deficiency: identification of a glutamine to
RT proline substitution that leads to a transport block of sucrase-isomaltase
RT in a pre-Golgi compartment.";
RL J. Clin. Invest. 97:633-641(1996).
RN [9]
RP VARIANT CSID PRO-341, AND CHARACTERIZATION OF VARIANT CSID PRO-341.
RX PubMed=10903344; DOI=10.1172/jci9677;
RA Jacob R., Zimmer K.P., Schmitz J., Naim H.Y.;
RT "Congenital sucrase-isomaltase deficiency arising from cleavage and
RT secretion of a mutant form of the enzyme.";
RL J. Clin. Invest. 106:281-287(2000).
RN [10]
RP VARIANT CSID ARG-117, AND CHARACTERIZATION OF VARIANT CSID ARG-117.
RX PubMed=11340066; DOI=10.1074/jbc.c100219200;
RA Spodsberg N., Jacob R., Alfalah M., Zimmer K.P., Naim H.Y.;
RT "Molecular basis of aberrant apical protein transport in an intestinal
RT enzyme disorder.";
RL J. Biol. Chem. 276:23506-23510(2001).
RN [11]
RP VARIANTS PHE-15 AND ALA-231, AND VARIANT CSID PRO-620.
RX PubMed=14724820; DOI=10.1053/j.gastro.2003.09.022;
RA Ritz V., Alfalah M., Zimmer K.P., Schmitz J., Jacob R., Naim H.Y.;
RT "Congenital sucrase-isomaltase deficiency because of an accumulation of the
RT mutant enzyme in the endoplasmic reticulum.";
RL Gastroenterology 125:1678-1685(2003).
RN [12]
RP VARIANTS CSID GLY-577; PRO-594; PRO-694; ASP-1073; TYR-1229; GLY-1367 AND
RP CYS-1745, AND VARIANTS PHE-15; ALA-231 AND ILE-1523.
RX PubMed=16329100; DOI=10.1002/humu.9392;
RA Sander P., Alfalah M., Keiser M., Korponay-Szabo I., Kovacs J.B., Leeb T.,
RA Naim H.Y.;
RT "Novel mutations in the human sucrase-isomaltase gene (SI) that cause
RT congenital carbohydrate malabsorption.";
RL Hum. Mutat. 27:119-119(2006).
CC -!- FUNCTION: Plays an important role in the final stage of carbohydrate
CC digestion. Isomaltase activity is specific for both alpha-1,4- and
CC alpha-1,6-oligosaccharides. {ECO:0000269|PubMed:20356844}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-
CC type action.; EC=3.2.1.48;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some
CC oligosaccharides produced from starch and glycogen by alpha-amylase,
CC and in isomaltose.; EC=3.2.1.10;
CC -!- SUBUNIT: The resulting sucrase and isomaltase subunits stay associated
CC with one another in a complex by non-covalent linkages.
CC {ECO:0000269|PubMed:20356844}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II
CC membrane protein. Note=Brush border.
CC -!- TISSUE SPECIFICITY: Expressed in the poorly differentiated crypt cells
CC of the small intestine as well as in the mature villous cells.
CC Expressed at very low levels in the colon.
CC {ECO:0000269|PubMed:1677636}.
CC -!- PTM: The precursor is proteolytically cleaved when exposed to
CC pancreatic proteases in the intestinal lumen.
CC -!- PTM: Sulfated. {ECO:0000250}.
CC -!- DISEASE: Congenital sucrase-isomaltase deficiency (CSID) [MIM:222900]:
CC Autosomal recessive intestinal disorder that is clinically
CC characterized by fermentative diarrhea, abdominal pain, and cramps upon
CC ingestion of sugar. The symptoms are the consequence of absent or
CC drastically reduced enzymatic activities of sucrase and isomaltase. The
CC prevalence of CSID is 0.02 % in individuals of European descent and
CC appears to be much higher in Greenland, Alaskan, and Canadian native
CC people. CSID arises due to post-translational perturbations in the
CC intracellular transport, polarized sorting, aberrant processing, and
CC defective function of SI. {ECO:0000269|PubMed:10903344,
CC ECO:0000269|PubMed:11340066, ECO:0000269|PubMed:14724820,
CC ECO:0000269|PubMed:16329100, ECO:0000269|PubMed:8609217}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: There is a high degree of homology between the
CC isomaltase and sucrase portions (41% of amino acid identity) indicating
CC that this protein is evolved by partial gene duplication.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; X63597; CAA45140.1; -; mRNA.
DR EMBL; AC092695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115034; AAI15035.1; -; mRNA.
DR EMBL; BC116452; AAI16453.1; -; mRNA.
DR EMBL; BC132834; AAI32835.1; -; mRNA.
DR EMBL; BC132860; AAI32861.1; -; mRNA.
DR EMBL; M22616; AAA60551.1; -; mRNA.
DR CCDS; CCDS3196.1; -.
DR PIR; S36082; UUHU.
DR RefSeq; NP_001032.2; NM_001041.3.
DR PDB; 3LPO; X-ray; 3.20 A; A/B/C/D=62-931.
DR PDB; 3LPP; X-ray; 2.15 A; A/B/C/D=62-931.
DR PDBsum; 3LPO; -.
DR PDBsum; 3LPP; -.
DR AlphaFoldDB; P14410; -.
DR SMR; P14410; -.
DR BioGRID; 112371; 2.
DR IntAct; P14410; 2.
DR MINT; P14410; -.
DR STRING; 9606.ENSP00000264382; -.
DR BindingDB; P14410; -.
DR ChEMBL; CHEMBL2748; -.
DR DrugBank; DB00284; Acarbose.
DR DrugBank; DB00747; Scopolamine.
DR DrugCentral; P14410; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GlyGen; P14410; 18 sites.
DR iPTMnet; P14410; -.
DR PhosphoSitePlus; P14410; -.
DR BioMuta; SI; -.
DR DMDM; 317373594; -.
DR jPOST; P14410; -.
DR MassIVE; P14410; -.
DR MaxQB; P14410; -.
DR PaxDb; P14410; -.
DR PeptideAtlas; P14410; -.
DR PRIDE; P14410; -.
DR ProteomicsDB; 53051; -.
DR Antibodypedia; 2270; 102 antibodies from 22 providers.
DR DNASU; 6476; -.
DR Ensembl; ENST00000264382.8; ENSP00000264382.3; ENSG00000090402.8.
DR GeneID; 6476; -.
DR KEGG; hsa:6476; -.
DR MANE-Select; ENST00000264382.8; ENSP00000264382.3; NM_001041.4; NP_001032.2.
DR UCSC; uc003fei.3; human.
DR CTD; 6476; -.
DR DisGeNET; 6476; -.
DR GeneCards; SI; -.
DR HGNC; HGNC:10856; SI.
DR HPA; ENSG00000090402; Tissue enriched (intestine).
DR MalaCards; SI; -.
DR MIM; 222900; phenotype.
DR MIM; 609845; gene.
DR neXtProt; NX_P14410; -.
DR OpenTargets; ENSG00000090402; -.
DR Orphanet; 35122; Congenital sucrase-isomaltase deficiency.
DR PharmGKB; PA35758; -.
DR VEuPathDB; HostDB:ENSG00000090402; -.
DR eggNOG; KOG1065; Eukaryota.
DR GeneTree; ENSGT00940000161633; -.
DR HOGENOM; CLU_000631_3_1_1; -.
DR InParanoid; P14410; -.
DR OMA; WDNMDKS; -.
DR OrthoDB; 151244at2759; -.
DR PhylomeDB; P14410; -.
DR TreeFam; TF314577; -.
DR BioCyc; MetaCyc:HS01688-MON; -.
DR BRENDA; 3.2.1.10; 2681.
DR BRENDA; 3.2.1.48; 2681.
DR PathwayCommons; P14410; -.
DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
DR Reactome; R-HSA-5659898; Intestinal saccharidase deficiencies.
DR SignaLink; P14410; -.
DR SIGNOR; P14410; -.
DR BioGRID-ORCS; 6476; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; SI; human.
DR EvolutionaryTrace; P14410; -.
DR GenomeRNAi; 6476; -.
DR Pharos; P14410; Tchem.
DR PRO; PR:P14410; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P14410; protein.
DR Bgee; ENSG00000090402; Expressed in jejunal mucosa and 47 other tissues.
DR ExpressionAtlas; P14410; baseline and differential.
DR Genevisible; P14410; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0004574; F:oligo-1,6-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; TAS:Reactome.
DR GO; GO:0044245; P:polysaccharide digestion; TAS:Reactome.
DR GO; GO:0005987; P:sucrose catabolic process; IDA:UniProtKB.
DR CDD; cd00111; Trefoil; 2.
DR Gene3D; 2.60.40.1180; -; 4.
DR Gene3D; 4.10.110.10; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR017957; P_trefoil_CS.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR Pfam; PF01055; Glyco_hydro_31; 2.
DR Pfam; PF16863; NtCtMGAM_N; 2.
DR Pfam; PF00088; Trefoil; 2.
DR SMART; SM00018; PD; 2.
DR SUPFAM; SSF51445; SSF51445; 2.
DR SUPFAM; SSF57492; SSF57492; 1.
DR SUPFAM; SSF74650; SSF74650; 2.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 2.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 2.
DR PROSITE; PS00025; P_TREFOIL_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Multifunctional enzyme; Phosphoprotein; Reference proteome; Repeat;
KW Signal-anchor; Sulfation; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1677636"
FT CHAIN 2..1827
FT /note="Sucrase-isomaltase, intestinal"
FT /id="PRO_0000018551"
FT CHAIN 2..1007
FT /note="Isomaltase"
FT /id="PRO_0000018552"
FT CHAIN 1008..1827
FT /note="Sucrase"
FT /id="PRO_0000018553"
FT TOPO_DOM 2..12
FT /note="Cytoplasmic"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..1827
FT /note="Lumenal"
FT DOMAIN 61..110
FT /note="P-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 932..978
FT /note="P-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..1007
FT /note="Isomaltase"
FT REGION 1008..1827
FT /note="Sucrase"
FT ACT_SITE 505
FT /note="Nucleophile; for isomaltase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066,
FT ECO:0000269|PubMed:20356844"
FT ACT_SITE 604
FT /note="For isomaltase activity"
FT /evidence="ECO:0000269|PubMed:20356844"
FT ACT_SITE 1394
FT /note="Nucleophile; for sucrase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066,
FT ECO:0000269|PubMed:20356844"
FT ACT_SITE 1397
FT /note="For sucrase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 1500
FT /note="Proton donor; for isomaltase activity"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT BINDING 388
FT /ligand="substrate"
FT BINDING 588
FT /ligand="substrate"
FT BINDING 662
FT /ligand="substrate"
FT MOD_RES 7
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:8521865"
FT MOD_RES 237
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 239
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 391
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 400
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 667
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 763
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 765
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20356844"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20356844"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20356844"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20356844"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:20356844"
FT DISULFID 77..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:20356844"
FT DISULFID 88..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:20356844"
FT DISULFID 520..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:20356844"
FT DISULFID 635..646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:20356844"
FT VARIANT 15
FT /note="V -> F (in dbSNP:rs9290264)"
FT /evidence="ECO:0000269|PubMed:14724820,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16329100,
FT ECO:0000269|PubMed:1677636"
FT /id="VAR_025367"
FT VARIANT 117
FT /note="Q -> R (in CSID; missorting of the enzyme to the
FT basolateral membrane; dbSNP:rs121912612)"
FT /evidence="ECO:0000269|PubMed:11340066"
FT /id="VAR_025368"
FT VARIANT 231
FT /note="T -> A (in dbSNP:rs9283633)"
FT /evidence="ECO:0000269|PubMed:1353958,
FT ECO:0000269|PubMed:14724820, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16329100, ECO:0000269|PubMed:2962903"
FT /id="VAR_025369"
FT VARIANT 341
FT /note="L -> P (in CSID; causes loss of anchored SI from the
FT membrane; dbSNP:rs267607049)"
FT /evidence="ECO:0000269|PubMed:10903344"
FT /id="VAR_025370"
FT VARIANT 577
FT /note="V -> G (in CSID; dbSNP:rs121912615)"
FT /evidence="ECO:0000269|PubMed:16329100"
FT /id="VAR_025371"
FT VARIANT 594
FT /note="S -> P (in CSID; dbSNP:rs765433197)"
FT /evidence="ECO:0000269|PubMed:16329100"
FT /id="VAR_025372"
FT VARIANT 620
FT /note="L -> P (in CSID; SI accumulates predominantly in the
FT ER; dbSNP:rs121912613)"
FT /evidence="ECO:0000269|PubMed:14724820"
FT /id="VAR_025373"
FT VARIANT 694
FT /note="T -> P (in CSID)"
FT /evidence="ECO:0000269|PubMed:16329100"
FT /id="VAR_025374"
FT VARIANT 1073
FT /note="G -> D (in CSID; dbSNP:rs121912616)"
FT /evidence="ECO:0000269|PubMed:16329100"
FT /id="VAR_025375"
FT VARIANT 1098
FT /note="Q -> P (in CSID; exhibits intracellular accumulation
FT of mannose-rich SI in the Golgi; dbSNP:rs121912611)"
FT /evidence="ECO:0000269|PubMed:8609217"
FT /id="VAR_007854"
FT VARIANT 1229
FT /note="C -> Y (in CSID; dbSNP:rs121912614)"
FT /evidence="ECO:0000269|PubMed:16329100"
FT /id="VAR_025376"
FT VARIANT 1367
FT /note="R -> G (in CSID; dbSNP:rs143388292)"
FT /evidence="ECO:0000269|PubMed:16329100"
FT /id="VAR_025377"
FT VARIANT 1523
FT /note="M -> I (in dbSNP:rs4855271)"
FT /evidence="ECO:0000269|PubMed:1353958,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16329100"
FT /id="VAR_025378"
FT VARIANT 1745
FT /note="F -> C (in CSID; dbSNP:rs79717168)"
FT /evidence="ECO:0000269|PubMed:16329100"
FT /id="VAR_025379"
FT VARIANT 1802
FT /note="T -> S (in dbSNP:rs9917722)"
FT /id="VAR_034522"
FT CONFLICT 300
FT /note="N -> D (in Ref. 3; AAI16453)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="S -> I (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="P -> S (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="A -> V (in Ref. 3; AAI16453)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="F -> L (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="R -> C (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="D -> A (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="Q -> R (in Ref. 3; AAI16453)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="T -> A (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="S -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="V -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="A -> V (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="E -> Q (in Ref. 1; CAA45140)"
FT /evidence="ECO:0000305"
FT CONFLICT 1782
FT /note="V -> I (in Ref. 3; AAI15035)"
FT /evidence="ECO:0000305"
FT CONFLICT 1825
FT /note="N -> S (in Ref. 3; AAI16453)"
FT /evidence="ECO:0000305"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3LPO"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 321..330
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:3LPO"
FT TURN 402..407
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 480..496
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 539..542
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 562..577
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 609..624
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 643..653
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 672..675
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 680..694
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 696..709
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 718..721
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 725..729
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 732..736
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 737..739
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 751..757
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 765..767
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 775..781
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 788..792
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 795..800
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 806..809
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 814..819
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 824..832
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 835..837
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 840..843
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 846..854
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 857..865
FT /evidence="ECO:0007829|PDB:3LPP"
FT HELIX 868..872
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 874..882
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 890..894
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 900..902
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:3LPP"
FT TURN 909..912
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 913..916
FT /evidence="ECO:0007829|PDB:3LPP"
FT STRAND 927..930
FT /evidence="ECO:0007829|PDB:3LPP"
SQ SEQUENCE 1827 AA; 209453 MW; DCB93F068AEEF83E CRC64;
MARKKFSGLE ISLIVLFVIV TIIAIALIVV LATKTPAVDE ISDSTSTPAT TRVTTNPSDS
GKCPNVLNDP VNVRINCIPE QFPTEGICAQ RGCCWRPWND SLIPWCFFVD NHGYNVQDMT
TTSIGVEAKL NRIPSPTLFG NDINSVLFTT QNQTPNRFRF KITDPNNRRY EVPHQYVKEF
TGPTVSDTLY DVKVAQNPFS IQVIRKSNGK TLFDTSIGPL VYSDQYLQIS TRLPSDYIYG
IGEQVHKRFR HDLSWKTWPI FTRDQLPGDN NNNLYGHQTF FMCIEDTSGK SFGVFLMNSN
AMEIFIQPTP IVTYRVTGGI LDFYILLGDT PEQVVQQYQQ LVGLPAMPAY WNLGFQLSRW
NYKSLDVVKE VVRRNREAGI PFDTQVTDID YMEDKKDFTY DQVAFNGLPQ FVQDLHDHGQ
KYVIILDPAI SIGRRANGTT YATYERGNTQ HVWINESDGS TPIIGEVWPG LTVYPDFTNP
NCIDWWANEC SIFHQEVQYD GLWIDMNEVS SFIQGSTKGC NVNKLNYPPF TPDILDKLMY
SKTICMDAVQ NWGKQYDVHS LYGYSMAIAT EQAVQKVFPN KRSFILTRST FAGSGRHAAH
WLGDNTASWE QMEWSITGML EFSLFGIPLV GADICGFVAE TTEELCRRWM QLGAFYPFSR
NHNSDGYEHQ DPAFFGQNSL LVKSSRQYLT IRYTLLPFLY TLFYKAHVFG ETVARPVLHE
FYEDTNSWIE DTEFLWGPAL LITPVLKQGA DTVSAYIPDA IWYDYESGAK RPWRKQRVDM
YLPADKIGLH LRGGYIIPIQ EPDVTTTASR KNPLGLIVAL GENNTAKGDF FWDDGETKDT
IQNGNYILYT FSVSNNTLDI VCTHSSYQEG TTLAFQTVKI LGLTDSVTEV RVAENNQPMN
AHSNFTYDAS NQVLLIADLK LNLGRNFSVQ WNQIFSENER FNCYPDADLA TEQKCTQRGC
VWRTGSSLSK APECYFPRQD NSYSVNSARY SSMGITADLQ LNTANARIKL PSDPISTLRV
EVKYHKNDML QFKIYDPQKK RYEVPVPLNI PTTPISTYED RLYDVEIKEN PFGIQIRRRS
SGRVIWDSWL PGFAFNDQFI QISTRLPSEY IYGFGEVEHT AFKRDLNWNT WGMFTRDQPP
GYKLNSYGFH PYYMALEEEG NAHGVFLLNS NAMDVTFQPT PALTYRTVGG ILDFYMFLGP
TPEVATKQYH EVIGHPVMPA YWALGFQLCR YGYANTSEVR ELYDAMVAAN IPYDVQYTDI
DYMERQLDFT IGEAFQDLPQ FVDKIRGEGM RYIIILDPAI SGNETKTYPA FERGQQNDVF
VKWPNTNDIC WAKVWPDLPN ITIDKTLTED EAVNASRAHV AFPDFFRTST AEWWAREIVD
FYNEKMKFDG LWIDMNEPSS FVNGTTTNQC RNDELNYPPY FPELTKRTDG LHFRTICMEA
EQILSDGTSV LHYDVHNLYG WSQMKPTHDA LQKTTGKRGI VISRSTYPTS GRWGGHWLGD
NYARWDNMDK SIIGMMEFSL FGMSYTGADI CGFFNNSEYH LCTRWMQLGA FYPYSRNHNI
ANTRRQDPAS WNETFAEMSR NILNIRYTLL PYFYTQMHEI HANGGTVIRP LLHEFFDEKP
TWDIFKQFLW GPAFMVTPVL EPYVQTVNAY VPNARWFDYH TGKDIGVRGQ FQTFNASYDT
INLHVRGGHI LPCQEPAQNT FYSRQKHMKL IVAADDNQMA QGSLFWDDGE SIDTYERDLY
LSVQFNLNQT TLTSTILKRG YINKSETRLG SLHVWGKGTT PVNAVTLTYN GNKNSLPFNE
DTTNMILRID LTTHNVTLEE PIEINWS
