ID Q6NSB3_HUMAN Unreviewed; 495 AA.
AC Q6NSB3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 127.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE Flags: Fragment;
GN Name=AMY1A {ECO:0000313|EMBL:AAH70302.1};
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 {ECO:0000313|EMBL:AAH70302.1};
RN [1] {ECO:0000313|EMBL:AAH70302.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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).
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:0000256|ARBA:ARBA00000548,
CC ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; BC070302; AAH70302.1; -; mRNA.
DR RefSeq; NP_001008222.1; NM_001008221.1.
DR RefSeq; NP_004029.2; NM_004038.3.
DR AlphaFoldDB; Q6NSB3; -.
DR SMR; Q6NSB3; -.
DR PeptideAtlas; Q6NSB3; -.
DR DNASU; 276; -.
DR GeneID; 276; -.
DR KEGG; hsa:276; -.
DR CTD; 276; -.
DR PharmGKB; PA24781; -.
DR OrthoDB; 3249969at2759; -.
DR BioGRID-ORCS; 276; 17 hits in 619 CRISPR screens.
DR GenomeRNAi; 276; -.
DR Genevisible; Q6NSB3; HS.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF50; ALPHA-AMYLASE 1A-RELATED; 1.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..495
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013198096"
FT DOMAIN 26..413
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 422..492
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT NON_TER 495
FT /evidence="ECO:0000313|EMBL:AAH70302.1"
SQ SEQUENCE 495 AA; 56210 MW; 7BC87EAD21F1FFFB 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
KIYVSAKKKK KKKKK
//
