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 11-NOV-2015, entry version 161. DE RecName: Full=Alpha-amylase 2B; DE EC=3.2.1.1; 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT 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 RT gene, 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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; RA Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C., RA 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., RA Planta R.J., 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 RT alpha-amylase encoded by the AMY2B gene."; RL Biochim. Biophys. Acta 1203:224-229(1993). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic CC linkages in polysaccharides containing three or more (1->4)-alpha- CC linked D-glucose units. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250}; CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250}; 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 Note=No experimental confirmation available.; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.484588; -. DR ProteinModelPortal; P19961; -. DR SMR; P19961; 17-511. DR BioGrid; 106777; 1. DR IntAct; P19961; 2. DR STRING; 9606.ENSP00000354610; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PhosphoSite; P19961; -. DR DMDM; 113789; -. DR MaxQB; P19961; -. DR PaxDb; P19961; -. DR PRIDE; P19961; -. DR Ensembl; ENST00000361355; ENSP00000354610; ENSG00000240038. [P19961-1] DR Ensembl; ENST00000477657; ENSP00000433347; ENSG00000240038. [P19961-2] DR Ensembl; ENST00000610648; ENSP00000481588; ENSG00000240038. [P19961-1] DR GeneID; 280; -. DR KEGG; hsa:280; -. DR UCSC; uc001duq.3; human. [P19961-1] DR CTD; 280; -. DR GeneCards; AMY2B; -. DR HGNC; HGNC:478; AMY2B. DR HPA; HPA045394; -. DR HPA; HPA045399; -. DR HPA; HPA046980; -. DR MIM; 104660; gene. DR neXtProt; NX_P19961; -. DR PharmGKB; PA24785; -. DR eggNOG; KOG2212; Eukaryota. DR eggNOG; COG0366; LUCA. DR GeneTree; ENSGT00390000002882; -. DR HOGENOM; HOG000253313; -. DR HOVERGEN; HBG000061; -. DR InParanoid; P19961; -. DR KO; K01176; -. DR OMA; RNGMVHL; -. DR OrthoDB; EOG7RJPR2; -. DR PhylomeDB; P19961; -. DR TreeFam; TF312850; -. DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate. DR ChiTaRS; AMY2B; human. DR GeneWiki; AMY2B; -. DR GenomeRNAi; 280; -. DR NextBio; 1133; -. DR PRO; PR:P19961; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P19961; -. DR CleanEx; HS_AMY2B; -. DR ExpressionAtlas; P19961; baseline and differential. DR Genevisible; P19961; HS. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0004556; F:alpha-amylase activity; TAS:ProtInc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc. DR GO; GO:0007586; P:digestion; TAS:ProtInc. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR031319; A-amylase_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR006589; Glyco_hydro_13_sub_cat_dom. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357; PTHR10357; 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; SSF51445; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Carbohydrate metabolism; Chloride; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycosidase; Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 15 FT CHAIN 16 511 Alpha-amylase 2B. FT /FTId=PRO_0000001402. FT ACT_SITE 212 212 Nucleophile. {ECO:0000250}. FT ACT_SITE 248 248 Proton donor. {ECO:0000250}. FT METAL 115 115 Calcium. {ECO:0000250}. FT METAL 173 173 Calcium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 182 182 Calcium. {ECO:0000250}. FT METAL 216 216 Calcium; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 210 210 Chloride. {ECO:0000250}. FT BINDING 313 313 Chloride. {ECO:0000250}. FT BINDING 352 352 Chloride. {ECO:0000250}. FT SITE 315 315 Transition state stabilizer. FT {ECO:0000250}. FT MOD_RES 16 16 Pyrrolidone carboxylic acid. FT {ECO:0000250|UniProtKB:P04746}. FT DISULFID 43 101 {ECO:0000250}. FT DISULFID 85 130 {ECO:0000250}. FT DISULFID 156 175 {ECO:0000250}. FT DISULFID 393 399 {ECO:0000250}. FT DISULFID 465 477 {ECO:0000250}. FT VAR_SEQ 368 370 DVN -> EHG (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_056932. FT VAR_SEQ 371 511 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=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 //