AMY1C_HUMAN
ID AMY1C_HUMAN Reviewed; 511 AA.
AC P0DTE8; A6NJS5; A8K8H6; P04745; Q13763; Q5T083;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Alpha-amylase 1C;
DE EC=3.2.1.1 {ECO:0000269|PubMed:12527308};
DE Flags: Precursor;
GN Name=AMY1C {ECO:0000312|HGNC:HGNC:476}; Synonyms=AMY1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP GLYCOSYLATION AT ASN-427, AND DEAMIDATION AT ASN-365; ASN-427 AND ASN-474.
RX PubMed=1710976; DOI=10.1002/elps.1150120114;
RA Bank R.A., Hettema E.H., Arwert F., Amerongen A.V., Pronk J.C.;
RT "Electrophoretic characterization of posttranslational modifications of
RT human parotid salivary alpha-amylase.";
RL Electrophoresis 12:74-79(1991).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM
RP AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=15299664; DOI=10.1107/s0907444995014119;
RA Ramasubbu N., Paloth V., Luo Y., Brayer G.D., Levine M.J.;
RT "Structure of human salivary alpha-amylase at 1.6-A resolution:
RT implications for its role in the oral cavity.";
RL Acta Crystallogr. D 52:435-446(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 16-511 OF WILD-TYPE AND MUTANT
RP 321-GLY--ALA-325 DEL IN COMPLEX WITH CALCIUM AND CHLORIDE, CATALYTIC
RP ACTIVITY, AND DISULFIDE BONDS.
RX PubMed=12527308; DOI=10.1016/s0022-2836(02)01326-8;
RA Ramasubbu N., Ragunath C., Mishra P.J.;
RT "Probing the role of a mobile loop in substrate binding and enzyme activity
RT of human salivary amylase.";
RL J. Mol. Biol. 325:1061-1076(2003).
CC -!- FUNCTION: Calcium-binding enzyme that initiates starch digestion in the
CC oral cavity (PubMed:12527308). Catalyzes the hydrolysis of internal
CC (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose,
CC isomaltose, small amounts of glucose as well as small linear and
CC branched oligosaccharides called dextrins (PubMed:12527308).
CC {ECO:0000269|PubMed:12527308}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:12527308};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12527308,
CC ECO:0000269|PubMed:15299664};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:12527308,
CC ECO:0000269|PubMed:15299664};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- CAUTION: Three distinct genes (AMY1A, AMY1B and AMY1C), located in a
CC gene cluster on 1p21, encode proteins sharing the same peptidic
CC sequence. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Amylase entry;
CC URL="https://en.wikipedia.org/wiki/Amylase";
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DR EMBL; AL513482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30784.1; -.
DR RefSeq; NP_001008219.1; NM_001008218.1.
DR RefSeq; NP_001008220.1; NM_001008219.2.
DR RefSeq; NP_001008222.1; NM_001008221.1.
DR RefSeq; NP_001333709.1; NM_001346780.1.
DR RefSeq; NP_004029.2; NM_004038.3.
DR RefSeq; XP_011539564.1; XM_011541262.1.
DR RefSeq; XP_016856547.1; XM_017001058.1.
DR AlphaFoldDB; P0DTE8; -.
DR SMR; P0DTE8; -.
DR BindingDB; P0DTE8; -.
DR GlyConnect; 28; 4 N-Linked glycans.
DR GlyGen; P0DTE8; 2 sites.
DR MassIVE; P0DTE8; -.
DR DNASU; 276; -.
DR Ensembl; ENST00000370079.3; ENSP00000359096.3; ENSG00000187733.7.
DR Ensembl; ENST00000622339.5; ENSP00000481450.2; ENSG00000187733.7.
DR Ensembl; ENST00000684141.1; ENSP00000507077.1; ENSG00000187733.7.
DR GeneID; 276; -.
DR GeneID; 277; -.
DR GeneID; 278; -.
DR KEGG; hsa:276; -.
DR KEGG; hsa:277; -.
DR KEGG; hsa:278; -.
DR MANE-Select; ENST00000330330.10; ENSP00000330484.5; NM_001008218.2; NP_001008219.1.
DR MANE-Select; ENST00000370083.9; ENSP00000359100.4; NM_004038.4; NP_004029.2.
DR MANE-Select; ENST00000622339.5; ENSP00000481450.2; NM_001008219.3; NP_001008220.1.
DR CTD; 276; -.
DR CTD; 277; -.
DR CTD; 278; -.
DR GeneCards; AMY1C; -.
DR HGNC; HGNC:476; AMY1C.
DR MIM; 104702; gene.
DR neXtProt; NX_P0DTE8; -.
DR OpenTargets; ENSG00000187733; -.
DR OMA; CYTGSEN; -.
DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
DR SignaLink; P0DTE8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000187733; Expressed in right uterine tube and 43 other tissues.
DR ExpressionAtlas; P0DTE8; baseline.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; IDA:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..511
FT /note="Alpha-amylase 1C"
FT /id="PRO_0000450821"
FT ACT_SITE 212
FT /note="Nucleophile"
FT ACT_SITE 248
FT /note="Proton donor"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT BINDING 210
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT BINDING 313
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT BINDING 352
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT SITE 315
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 16
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P00687"
FT MOD_RES 365
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:1710976"
FT MOD_RES 427
FT /note="Deamidated asparagine; partial; alternate"
FT /evidence="ECO:0000269|PubMed:1710976"
FT MOD_RES 474
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:1710976"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:1710976"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..101
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT DISULFID 85..130
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT DISULFID 156..175
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
FT DISULFID 393..399
FT DISULFID 465..477
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664"
SQ SEQUENCE 511 AA; 57768 MW; 7710BCAC83EBE8B2 CRC64;
MKLFWLLFTI GFCWAQYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP
NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMCGN
AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLSGL
LDLALGKDYV RSKIAEYMNH LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG
SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP
RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE HRWRQIRNMV NFRNVVDGQP
FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT FSLTLQTGLP AGTYCDVISG DKINGNCTGI
KIYVSDDGKA HFSISNSAED PFIAIHAESK L
