AMY2B_HUMAN
ID AMY2B_HUMAN Reviewed; 511 AA.
AC P19961; B3KTI1; B3KXB7; D3DT76; Q9UBH3;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Alpha-amylase 2B;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase 2B;
DE AltName: Full=Carcinoid alpha-amylase;
DE Flags: Precursor;
GN Name=AMY2B;
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] (ISOFORM 1).
RX PubMed=2701942; DOI=10.1016/0378-1119(89)90003-6;
RA Tomita N., Horii A., Doi S., Yokouchi H., Shiosaki K., Higashiyama M.,
RA Matsuura N., Ogawa M., Mori T., Matsubara K.;
RT "A novel type of human alpha-amylase produced in lung carcinoid tumor.";
RL Gene 76:11-18(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2401405; DOI=10.1016/0378-1119(90)90191-s;
RA Yokouchi H., Horii A., Emi M., Tomita N., Doi S., Ogawa M., Mori T.,
RA Matsubara K.;
RT "Cloning and characterization of a third type of human alpha-amylase gene,
RT AMY2B.";
RL Gene 90:281-286(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Kidney;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=2452973; DOI=10.1128/mcb.8.3.1197-1205.1988;
RA Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C., Meisler M.H.;
RT "Concerted evolution of human amylase genes.";
RL Mol. Cell. Biol. 8:1197-1205(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RC TISSUE=Pancreas;
RX PubMed=3260028; DOI=10.1093/nar/16.10.4724;
RA Groot P.C., Bleeker M.J., Pronk J.C., Arwert F., Mager W.H., Planta R.J.,
RA Eriksson A.W., Frants R.R.;
RT "Human pancreatic amylase is encoded by two different genes.";
RL Nucleic Acids Res. 16:4724-4724(1988).
RN [9]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Urine;
RX PubMed=8268204; DOI=10.1016/0167-4838(93)90087-8;
RA Omichi K., Hase S.;
RT "Identification of the characteristic amino-acid sequence for human alpha-
RT amylase encoded by the AMY2B gene.";
RL Biochim. Biophys. Acta 1203:224-229(1993).
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:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P04746};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P04746};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P19961-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P19961-2; Sequence=VSP_056932, VSP_056933;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M24895; AAA35525.1; -; mRNA.
DR EMBL; D90097; BAA14130.1; -; Genomic_DNA.
DR EMBL; AK095605; BAG53093.1; -; mRNA.
DR EMBL; AK127047; BAG54429.1; -; mRNA.
DR EMBL; AC105272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72902.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72903.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72904.1; -; Genomic_DNA.
DR EMBL; BC011179; AAH11179.1; -; mRNA.
DR EMBL; BC020861; AAH20861.1; -; mRNA.
DR EMBL; X07057; CAA30100.1; -; Genomic_DNA.
DR EMBL; M18670; AAA51725.1; -; Genomic_DNA.
DR CCDS; CCDS782.1; -. [P19961-1]
DR PIR; JS0165; ALHU2B.
DR RefSeq; NP_066188.1; NM_020978.4. [P19961-1]
DR AlphaFoldDB; P19961; -.
DR SMR; P19961; -.
DR BioGRID; 106777; 7.
DR IntAct; P19961; 5.
DR STRING; 9606.ENSP00000354610; -.
DR DrugBank; DB01870; 1,4-dithio-alpha-D-glucopyranose.
DR DrugBank; DB02730; 4-Methylthio-Alpha-D-Mannose.
DR DrugBank; DB03092; 5-Hydroxymethyl-Chonduritol.
DR DrugBank; DB03277; alpha-maltotriose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03323; Maltose.
DR DrugBank; DB02218; N-[4-hydroxymethyl-cyclohexan-6-yl-1,2,3-triol]-4,6-dideoxy-4-aminoglucopyranoside.
DR DrugBank; DB04417; P-Nitrophenol.
DR DrugBank; DB03088; Pidolic acid.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR iPTMnet; P19961; -.
DR PhosphoSitePlus; P19961; -.
DR BioMuta; AMY2B; -.
DR DMDM; 113789; -.
DR jPOST; P19961; -.
DR MassIVE; P19961; -.
DR MaxQB; P19961; -.
DR PaxDb; P19961; -.
DR PeptideAtlas; P19961; -.
DR PRIDE; P19961; -.
DR ProteomicsDB; 3680; -.
DR ProteomicsDB; 53704; -. [P19961-1]
DR TopDownProteomics; P19961-1; -. [P19961-1]
DR Antibodypedia; 34942; 233 antibodies from 28 providers.
DR DNASU; 280; -.
DR Ensembl; ENST00000361355.8; ENSP00000354610.4; ENSG00000240038.7. [P19961-1]
DR Ensembl; ENST00000477657.5; ENSP00000433347.1; ENSG00000240038.7. [P19961-2]
DR Ensembl; ENST00000610648.1; ENSP00000481588.1; ENSG00000240038.7. [P19961-1]
DR Ensembl; ENST00000684275.1; ENSP00000507176.1; ENSG00000240038.7. [P19961-1]
DR GeneID; 280; -.
DR KEGG; hsa:280; -.
DR MANE-Select; ENST00000684275.1; ENSP00000507176.1; NM_001387437.1; NP_001374366.1.
DR UCSC; uc001duq.5; human. [P19961-1]
DR CTD; 280; -.
DR DisGeNET; 280; -.
DR GeneCards; AMY2B; -.
DR HGNC; HGNC:478; AMY2B.
DR HPA; ENSG00000240038; Tissue enriched (pancreas).
DR MIM; 104660; gene.
DR neXtProt; NX_P19961; -.
DR OpenTargets; ENSG00000240038; -.
DR PharmGKB; PA24785; -.
DR VEuPathDB; HostDB:ENSG00000240038; -.
DR eggNOG; KOG2212; Eukaryota.
DR GeneTree; ENSGT00940000154802; -.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; P19961; -.
DR OMA; FRYAYDL; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; P19961; -.
DR TreeFam; TF312850; -.
DR PathwayCommons; P19961; -.
DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
DR SignaLink; P19961; -.
DR BioGRID-ORCS; 280; 12 hits in 984 CRISPR screens.
DR ChiTaRS; AMY2B; human.
DR GeneWiki; AMY2B; -.
DR GenomeRNAi; 280; -.
DR Pharos; P19961; Tbio.
DR PRO; PR:P19961; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P19961; protein.
DR Bgee; ENSG00000240038; Expressed in body of pancreas and 96 other tissues.
DR ExpressionAtlas; P19961; baseline and differential.
DR Genevisible; P19961; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 Alternative splicing; Calcium; Carbohydrate metabolism; Chloride;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Metal-binding; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..15
FT CHAIN 16..511
FT /note="Alpha-amylase 2B"
FT /id="PRO_0000001402"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 210
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 313
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 352
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
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:P04746"
FT DISULFID 43..101
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 85..130
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 156..175
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 393..399
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 465..477
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT VAR_SEQ 368..370
FT /note="DVN -> EHG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056932"
FT VAR_SEQ 371..511
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056933"
SQ SEQUENCE 511 AA; 57710 MW; 05FC3B1EC1143857 CRC64;
MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP
NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMSGN
AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLVGL
LDLALEKDYV RSKIAEYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG
SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP
RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE HRWRQIRNMV NFRNVVDGQP
FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT FSLTLQTGLP AGTYCDVISG DKINGNCTGI
KIYVSDDGKA HFSISNSAED PFIAIHAESK L
