ID Q6DHR7_DANRE Unreviewed; 512 AA.
AC Q6DHR7;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 131.
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};
GN Name=amy2al2 {ECO:0000313|ZFIN:ZDB-GENE-040801-179};
GN ORFNames=zgc:92137 {ECO:0000313|EMBL:AAH75900.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH75900.1};
RN [1] {ECO:0000313|EMBL:AAH75900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole {ECO:0000313|EMBL:AAH75900.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_001003729.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19200601;
RA Jima D.D., Shah R.N., Orcutt T.M., Joshi D., Law J.M., Litman G.W.,
RA Trede N.S., Yoder J.A.;
RT "Enhanced transcription of complement and coagulation genes in the absence
RT of adaptive immunity.";
RL Mol. Immunol. 46:1505-1516(2009).
RN [3] {ECO:0000313|RefSeq:NP_001003729.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22297719;
RA Mohseny A.B., Xiao W., Carvalho R., Spaink H.P., Hogendoorn P.C.,
RA Cleton-Jansen A.M.;
RT "An osteosarcoma zebrafish model implicates Mmp-19 and Ets-1 as well as
RT reduced host immune response in angiogenesis and migration.";
RL J. Pathol. 227:245-253(2012).
RN [4] {ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5] {ECO:0000313|RefSeq:NP_001003729.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [6] {ECO:0000313|RefSeq:NP_001003729.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28888969;
RA Scheldeman C., Mills J.D., Siekierska A., Serra I., Copmans D., Iyer A.M.,
RA Whalley B.J., Maes J., Jansen A.C., Lagae L., Aronica E., de Witte P.A.M.;
RT "mTOR-related neuropathology in mutant tsc2 zebrafish: Phenotypic,
RT transcriptomic and pharmacological analysis.";
RL Neurobiol. Dis. 108:225-237(2017).
RN [7] {ECO:0000313|RefSeq:NP_001003729.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; BC075900; AAH75900.1; -; mRNA.
DR RefSeq; NP_001003729.1; NM_001003729.1.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 445049; -.
DR KEGG; dre:445049; -.
DR AGR; ZFIN:ZDB-GENE-040801-179; -.
DR CTD; 445049; -.
DR ZFIN; ZDB-GENE-040801-179; amy2al2.
DR OrthoDB; 3249969at2759; -.
DR PhylomeDB; Q6DHR7; -.
DR Proteomes; UP000000437; Chromosome 17.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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:SF49; ALPHA-AMYLASE; 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 1: Evidence at protein 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 Proteomics identification {ECO:0007829|PeptideAtlas:Q6DHR7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001003729.1}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..512
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001003729.1"
FT /id="PRO_5035034055"
FT DOMAIN 26..414
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 423..511
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 512 AA; 57519 MW; 4BADDC012DE08185 CRC64;
MMLLVLVAIF GLGFAQHNPN TKNGRTSIVH LFEWRWADIA EECERYLAPN GYGGVQISPP
SEHVKLTNPW HPWWQRYQPI SYNLCSRSGT EAELKDMITR CNNVGVNIYA DVVINHMCKS
IHGAGTPSSC GSHFDANKED FPTVPYSYLD FNDGKCKSAS GQIESYNDIY QVRDCRLEDL
LDLALEKDYV RGKVAEYLNK LIELGVAGFR VDACKHMWPG DLSNVYSRLK TLNTKWFPSG
TKPFIYQEVI DLGGEPIKAS EYYGLARVTE FKHSAKIGTA VRKWDGEKLS YLKNWGEGWG
FMPSDKALVF VDNHDNQRGH GAGGASVLTF WDSRLYKMAA GFMLAHPYGV TRVMSSYQWD
RKIVNGKDEN DWMGPPSFSD GSTKPVPINP DSTCGDGWVC EHRWRQIRNM VIFRNVVNGQ
PLFNWWDNGN SQIAFSRGSK GFIVINNDNW ELNATLNTGL QSGTYCDIIS GEKSGNSCTG
KQVSVDSDGK ATFSISHTEE DPFMAIHADS KL
//
