ID AMYC_HUMAN Reviewed; 511 AA. AC P19961; Q9UBH3; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 31-OCT-2006, entry version 74. DE Alpha-amylase 2B precursor (EC 3.2.1.1) (1,4-alpha-D-glucan DE glucanohydrolase) (Alpha-amylase carcinoid). 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]. RX MEDLINE=89306646; 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 MEDLINE=90382677; 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]. 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RX MEDLINE=88216594; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RC TISSUE=Pancreas; RX MEDLINE=88247775; PubMed=3260028; 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 [6] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Urine; RX MEDLINE=94092712; 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 oligosaccharides and polysaccharides. CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity). CC -!- COFACTOR: Binds 1 chloride ion per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (By similarity). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. 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; 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 PIR; JS0165; ALHU2B. DR UniGene; Hs.484588; -. DR HSSP; P04746; 1HNY. DR SMR; P19961; 16-511. DR Ensembl; ENSG00000197839; Homo sapiens. DR KEGG; hsa:280; -. DR H-InvDB; HIX0021182; -. DR HGNC; HGNC:478; AMY2B. DR MIM; 104660; gene. DR ArrayExpress; P19961; -. DR RZPD-ProtExp; C0614; -. DR RZPD-ProtExp; IOH10274; -. DR RZPD-ProtExp; IOH40716; -. DR RZPD-ProtExp; IOH7158; -. DR RZPD-ProtExp; RZPDo839E0770; -. DR RZPD-ProtExp; RZPDo839E0780; -. DR GO; GO:0004556; F:alpha-amylase activity; TAS:ProtInc. DR GO; GO:0005975; P:carbohydrate metabolism; NAS:ProtInc. DR GO; GO:0007586; P:digestion; TAS:ProtInc. DR InterPro; IPR013772; A-amylase. DR InterPro; IPR006048; A-amylase_b_C. DR InterPro; IPR013773; A-amylase_short. DR InterPro; IPR006046; Glyco_hydro_13. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat. DR InterPro; IPR006589; Glyco_hydro_13_sub_cat. DR InterPro; IPR013781; Glyco_hydro_cat. 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. KW Calcium; Carbohydrate metabolism; Chloride; Direct protein sequencing; KW Glycosidase; Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; KW Signal. FT SIGNAL 1 15 FT CHAIN 16 511 Alpha-amylase 2B. FT /FTId=PRO_0000001402. FT ACT_SITE 212 212 Nucleophile (By similarity). FT ACT_SITE 248 248 Proton donor (By similarity). FT ACT_SITE 315 315 By similarity. FT METAL 115 115 Calcium (By similarity). FT METAL 173 173 Calcium (via carbonyl oxygen) (By FT similarity). FT METAL 182 182 Calcium (By similarity). FT METAL 216 216 Calcium (via carbonyl oxygen) (By FT similarity). FT BINDING 210 210 Chloride (By similarity). FT BINDING 313 313 Chloride (By similarity). FT BINDING 352 352 Chloride (By similarity). FT MOD_RES 16 16 Pyrrolidone carboxylic acid (By FT similarity). FT DISULFID 43 101 By similarity. FT DISULFID 85 130 By similarity. FT DISULFID 156 175 By similarity. FT DISULFID 393 399 By similarity. FT DISULFID 465 477 By similarity. 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 //