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Database: UniProt
Entry: P01023
LinkDB: P01023
Original site: P01023 
ID   A2MG_HUMAN              Reviewed;        1474 AA.
AC   P01023; Q13677; Q59F47; Q5QTS0; Q68DN2; Q6PIY3; Q6PN97;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   02-JUN-2021, entry version 230.
DE   RecName: Full=Alpha-2-macroglobulin;
DE            Short=Alpha-2-M;
DE   AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5;
DE   Flags: Precursor;
GN   Name=A2M; Synonyms=CPAMD5; ORFNames=FWP007;
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], AND VARIANTS ASP-639 AND VAL-1000.
RX   PubMed=2581245; DOI=10.1073/pnas.82.8.2282;
RA   Kan C.-C., Solomon E., Belt K.T., Chain A.C., Hiorns L.R., Fey G.H.;
RT   "Nucleotide sequence of cDNA encoding human alpha 2-macroglobulin and
RT   assignment of the chromosomal locus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:2282-2286(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASP-639 AND VAL-1000.
RC   TISSUE=Prostate;
RX   PubMed=15611997; DOI=10.1002/pros.20183;
RA   Lin V.K., Wang S.-Y., Boetticher N.C., Vazquez D.V., Saboorian H.,
RA   McConnell J.D., Roehrborn C.G.;
RT   "Alpha(2) macroglobulin, a PSA-binding protein, is expressed in human
RT   prostate stroma.";
RL   Prostate 63:299-308(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-639.
RC   TISSUE=Spleen;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-639 AND VAL-1000.
RC   TISSUE=Liver;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-639 AND VAL-1000.
RC   TISSUE=Skin;
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 1-29.
RC   TISSUE=Placenta;
RX   PubMed=1374237; DOI=10.1016/0006-291x(92)90631-t;
RA   Matthijs G., Devriendt K., Cassiman J.-J., van den Berghe H., Marynen P.;
RT   "Structure of the human alpha-2 macroglobulin gene and its promotor.";
RL   Biochem. Biophys. Res. Commun. 184:596-603(1992).
RN   [8]
RP   PROTEIN SEQUENCE OF 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISULFIDE BONDS.
RX   PubMed=6203908;
RA   Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M.,
RA   Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.;
RT   "Primary structure of human alpha 2-macroglobulin. V. The complete
RT   structure.";
RL   J. Biol. Chem. 259:8318-8327(1984).
RN   [9]
RP   ERRATUM OF PUBMED:6203908.
RA   Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M.,
RA   Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.;
RL   J. Biol. Chem. 260:6500-6500(1985).
RN   [10]
RP   PROTEIN SEQUENCE OF 273-286 AND 426-436, AND DISULFIDE BONDS.
RX   PubMed=2430963;
RA   Jensen P.E.H., Sottrup-Jensen L.;
RT   "Primary structure of human alpha 2-macroglobulin. Complete disulfide
RT   bridge assignment and localization of two interchain bridges in the dimeric
RT   proteinase binding unit.";
RL   J. Biol. Chem. 261:15863-15869(1986).
RN   [11]
RP   PROTEIN SEQUENCE OF 672-747.
RX   PubMed=1692292; DOI=10.1016/0014-5793(90)80226-9;
RA   Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J.;
RT   "A genetic polymorphism in a functional domain of human pregnancy zone
RT   protein: the bait region. Genomic structure of the bait domains of human
RT   pregnancy zone protein and alpha 2 macroglobulin.";
RL   FEBS Lett. 262:349-352(1990).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 672-746, AND VARIANT TYR-972.
RX   PubMed=1370808; DOI=10.1007/bf00197266;
RA   Poller W., Faber J.-P., Klobeck G., Olek K.;
RT   "Cloning of the human alpha 2-macroglobulin gene and detection of mutations
RT   in two functional domains: the bait region and the thiolester site.";
RL   Hum. Genet. 88:313-319(1992).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 832-1474.
RC   TISSUE=Liver;
RX   PubMed=2408344; DOI=10.1007/bf01534685;
RA   Bell G.I., Rall L.B., Sanchez-Pescador R., Merryweather J.P., Scott J.,
RA   Eddy R.L., Shows T.B.;
RT   "Human alpha 2-macroglobulin gene is located on chromosome 12.";
RL   Somat. Cell Mol. Genet. 11:285-289(1985).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1208-1474.
RC   TISSUE=Aorta;
RA   Liu B., Zhao B., Wang X.Y., Xu Y.Y., Liu Y.Q., Song L., Ye J., Sheng H.,
RA   Gao Y., Zhang C.L., Wei Y.J., Zhang J., Song L., Jiang Y.X., Zhao Z.W.,
RA   Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA   Zhao M.S., Hui R.T.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   INHIBITORY SITE.
RX   PubMed=6167263; DOI=10.1016/s0006-291x(81)80055-1;
RA   Hall P.K., Nelles L.P., Travis J., Roberts R.C.;
RT   "Proteolytic cleavage sites on alpha 2-macroglobulin resulting in
RT   proteinase binding are different for trypsin and Staphylococcus aureus V-8
RT   proteinase.";
RL   Biochem. Biophys. Res. Commun. 100:8-16(1981).
RN   [16]
RP   INHIBITORY SITE.
RX   PubMed=6165619; DOI=10.1016/0014-5793(81)80197-4;
RA   Sottrup-Jensen L., Loenblad P.B., Stepanik T.M., Petersen T.E.,
RA   Magnusson S., Joernvall H.;
RT   "Primary structure of the 'bait' region for proteinases in alpha 2-
RT   macroglobulin. Nature of the complex.";
RL   FEBS Lett. 127:167-173(1981).
RN   [17]
RP   INHIBITORY SITE.
RX   PubMed=6172288; DOI=10.1016/0014-5793(81)80804-6;
RA   Mortensen S.B., Sottrup-Jensen L., Hansen H.F., Petersen T.E.,
RA   Magnusson S.;
RT   "Primary and secondary cleavage sites in the bait region of alpha 2-
RT   macroglobulin.";
RL   FEBS Lett. 135:295-300(1981).
RN   [18]
RP   INHIBITORY SITE.
RX   PubMed=6195065; DOI=10.1515/bchm2.1983.364.2.1297;
RA   Virca G.D., Salvesen G.S., Travis J.;
RT   "Human neutrophil elastase and cathepsin G cleavage sites in the bait
RT   region of alpha 2-macroglobulin. Proposed structural limits of the bait
RT   region.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 364:1297-1302(1983).
RN   [19]
RP   GLYCOSYLATION AT ASN-991.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [20]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-869 AND ASN-1424.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [21]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-247; ASN-396; ASN-410;
RP   ASN-869; ASN-991 AND ASN-1424.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [22]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-396; ASN-991 AND ASN-1424.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [23]
RP   GLYCOSYLATION AT ASN-55 AND ASN-1424.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [26]
RP   STRUCTURE BY NMR OF 1337-1474.
RX   PubMed=9865955; DOI=10.1002/pro.5560071214;
RA   Huang W., Dolmer K., Liao X., Gettins P.G.W.;
RT   "Localization of basic residues required for receptor binding to the single
RT   alpha-helix of the receptor binding domain of human alpha2-macroglobulin.";
RL   Protein Sci. 7:2602-2612(1998).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 126-227, AND DOMAIN STRUCTURE.
RX   PubMed=17608619; DOI=10.1042/bj20070764;
RA   Doan N., Gettins P.G.W.;
RT   "Human alpha2-macroglobulin is composed of multiple domains, as predicted
RT   by homology with complement component C3.";
RL   Biochem. J. 407:23-30(2007).
RN   [28]
RP   VARIANT VAL-1000.
RX   PubMed=1707161; DOI=10.1093/nar/19.1.198-a;
RA   Poller W., Faber J.-P., Olek K.;
RT   "Sequence polymorphism in the human alpha2-macroglobulin (A2M) gene.";
RL   Nucleic Acids Res. 19:198-198(1991).
CC   -!- FUNCTION: Is able to inhibit all four classes of proteinases by a
CC       unique 'trapping' mechanism. This protein has a peptide stretch, called
CC       the 'bait region' which contains specific cleavage sites for different
CC       proteinases. When a proteinase cleaves the bait region, a
CC       conformational change is induced in the protein which traps the
CC       proteinase. The entrapped enzyme remains active against low molecular
CC       weight substrates (activity against high molecular weight substrates is
CC       greatly reduced). Following cleavage in the bait region, a thioester
CC       bond is hydrolyzed and mediates the covalent binding of the protein to
CC       the proteinase.
CC   -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000269|PubMed:2430963,
CC       ECO:0000269|PubMed:6203908}.
CC   -!- INTERACTION:
CC       P01023; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-640741, EBI-22011868;
CC       P01023; P63010-2: AP2B1; NbExp=3; IntAct=EBI-640741, EBI-11529439;
CC       P01023; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-640741, EBI-718459;
CC       P01023; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-640741, EBI-2837444;
CC       P01023; Q92478: CLEC2B; NbExp=3; IntAct=EBI-640741, EBI-13350535;
CC       P01023; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-640741, EBI-350590;
CC       P01023; P04141: CSF2; NbExp=3; IntAct=EBI-640741, EBI-1809826;
CC       P01023; P35222: CTNNB1; NbExp=3; IntAct=EBI-640741, EBI-491549;
CC       P01023; Q7L576: CYFIP1; NbExp=3; IntAct=EBI-640741, EBI-1048143;
CC       P01023; Q9NR90-2: DAZ3; NbExp=3; IntAct=EBI-640741, EBI-25830216;
CC       P01023; Q9UHI6: DDX20; NbExp=3; IntAct=EBI-640741, EBI-347658;
CC       P01023; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-640741, EBI-2795449;
CC       P01023; O75616: ERAL1; NbExp=3; IntAct=EBI-640741, EBI-6393536;
CC       P01023; Q9Y261-2: FOXA2; NbExp=3; IntAct=EBI-640741, EBI-25830360;
CC       P01023; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-640741, EBI-10253815;
CC       P01023; Q9ULV1: FZD4; NbExp=3; IntAct=EBI-640741, EBI-2466380;
CC       P01023; P0C0S5: H2AZ1; NbExp=3; IntAct=EBI-640741, EBI-1199859;
CC       P01023; P68431: H3C12; NbExp=3; IntAct=EBI-640741, EBI-79722;
CC       P01023; P09017: HOXC4; NbExp=3; IntAct=EBI-640741, EBI-3923226;
CC       P01023; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-640741, EBI-21911304;
CC       P01023; Q92993: KAT5; NbExp=3; IntAct=EBI-640741, EBI-399080;
CC       P01023; Q92993-2: KAT5; NbExp=3; IntAct=EBI-640741, EBI-20795332;
CC       P01023; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-640741, EBI-10172290;
CC       P01023; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-640741, EBI-10261141;
CC       P01023; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-640741, EBI-10258746;
CC       P01023; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-640741, EBI-739832;
CC       P01023; P07948: LYN; NbExp=3; IntAct=EBI-640741, EBI-79452;
CC       P01023; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-640741, EBI-4397720;
CC       P01023; A4FUJ8: MKL1; NbExp=3; IntAct=EBI-640741, EBI-21250407;
CC       P01023; P41218: MNDA; NbExp=3; IntAct=EBI-640741, EBI-2829677;
CC       P01023; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-640741, EBI-995714;
CC       P01023; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-640741, EBI-1058491;
CC       P01023; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-640741, EBI-25830200;
CC       P01023; Q99497: PARK7; NbExp=3; IntAct=EBI-640741, EBI-1164361;
CC       P01023; O75925: PIAS1; NbExp=3; IntAct=EBI-640741, EBI-629434;
CC       P01023; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-640741, EBI-9090282;
CC       P01023; O75626-3: PRDM1; NbExp=3; IntAct=EBI-640741, EBI-25829882;
CC       P01023; P57729: RAB38; NbExp=3; IntAct=EBI-640741, EBI-6552718;
CC       P01023; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-640741, EBI-25829984;
CC       P01023; Q96D59: RNF183; NbExp=3; IntAct=EBI-640741, EBI-743938;
CC       P01023; P04271: S100B; NbExp=3; IntAct=EBI-640741, EBI-458391;
CC       P01023; Q16637-3: SMN2; NbExp=3; IntAct=EBI-640741, EBI-395447;
CC       P01023; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-640741, EBI-10696971;
CC       P01023; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-640741, EBI-357085;
CC       P01023; O75558: STX11; NbExp=3; IntAct=EBI-640741, EBI-714135;
CC       P01023; Q8N4C7: STX19; NbExp=3; IntAct=EBI-640741, EBI-8484990;
CC       P01023; P43405-2: SYK; NbExp=3; IntAct=EBI-640741, EBI-25892332;
CC       P01023; P28347-2: TEAD1; NbExp=3; IntAct=EBI-640741, EBI-12151837;
CC       P01023; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-640741, EBI-11525489;
CC       P01023; Q8WVJ9: TWIST2; NbExp=3; IntAct=EBI-640741, EBI-1797313;
CC       P01023; P10599: TXN; NbExp=3; IntAct=EBI-640741, EBI-594644;
CC       P01023; Q9BVJ6: UTP14A; NbExp=3; IntAct=EBI-640741, EBI-473284;
CC       P01023; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-640741, EBI-11141397;
CC       P01023; Q96AX1: VPS33A; NbExp=3; IntAct=EBI-640741, EBI-2527283;
CC       P01023; Q8N895: ZNF366; NbExp=3; IntAct=EBI-640741, EBI-2813661;
CC       P01023; Q99KR7: Ppif; Xeno; NbExp=3; IntAct=EBI-640741, EBI-6455001;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6203908}.
CC   -!- TISSUE SPECIFICITY: Secreted in plasma. {ECO:0000269|PubMed:6203908}.
CC   -!- DEVELOPMENTAL STAGE: Unlike the rat protein, which is an acute phase
CC       protein, this protein is always in circulation at high levels.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT02228.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD92851.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-2 macroglobulin entry;
CC       URL="https://en.wikipedia.org/wiki/Alpha_2-macroglobulin";
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DR   EMBL; M11313; AAA51551.1; -; mRNA.
DR   EMBL; AY591530; AAT02228.1; ALT_INIT; mRNA.
DR   EMBL; AB209614; BAD92851.1; ALT_INIT; mRNA.
DR   EMBL; CR749334; CAH18188.1; -; mRNA.
DR   EMBL; AC007436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026246; AAH26246.1; -; mRNA.
DR   EMBL; BC040071; AAH40071.1; -; mRNA.
DR   EMBL; Z11711; CAA77774.1; -; Genomic_DNA.
DR   EMBL; X68728; CAA48670.1; -; Genomic_DNA.
DR   EMBL; X68729; CAA48670.1; JOINED; Genomic_DNA.
DR   EMBL; M36501; AAA51552.1; -; mRNA.
DR   EMBL; AF109189; AAQ13498.1; -; mRNA.
DR   CCDS; CCDS44827.1; -.
DR   PIR; A94033; MAHU.
DR   RefSeq; NP_000005.2; NM_000014.5.
DR   RefSeq; NP_001334352.1; NM_001347423.1.
DR   RefSeq; NP_001334353.1; NM_001347424.1.
DR   RefSeq; NP_001334354.1; NM_001347425.1.
DR   PDB; 1BV8; NMR; -; A=1337-1474.
DR   PDB; 2P9R; X-ray; 2.30 A; A/B=126-227.
DR   PDB; 4ACQ; X-ray; 4.30 A; A/B/C/D=24-1474.
DR   PDBsum; 1BV8; -.
DR   PDBsum; 2P9R; -.
DR   PDBsum; 4ACQ; -.
DR   BMRB; P01023; -.
DR   PCDDB; P01023; -.
DR   SMR; P01023; -.
DR   BioGRID; 106524; 124.
DR   CORUM; P01023; -.
DR   DIP; DIP-1118N; -.
DR   IntAct; P01023; 181.
DR   MINT; P01023; -.
DR   STRING; 9606.ENSP00000323929; -.
DR   BindingDB; P01023; -.
DR   ChEMBL; CHEMBL4295690; -.
DR   DrugBank; DB00626; Bacitracin.
DR   DrugBank; DB00102; Becaplermin.
DR   DrugBank; DB00515; Cisplatin.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB06796; Mangafodipir.
DR   DrugBank; DB08888; Ocriplasmin.
DR   DrugBank; DB12965; Silver.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   MEROPS; I39.001; -.
DR   MoonDB; P01023; Predicted.
DR   CarbonylDB; P01023; -.
DR   GlyConnect; 730; 47 N-Linked glycans (7 sites).
DR   GlyGen; P01023; 14 sites, 24 N-linked glycans (6 sites), 2 O-linked glycans (6 sites).
DR   iPTMnet; P01023; -.
DR   PhosphoSitePlus; P01023; -.
DR   SwissPalm; P01023; -.
DR   BioMuta; A2M; -.
DR   DMDM; 308153640; -.
DR   DOSAC-COBS-2DPAGE; P01023; -.
DR   SWISS-2DPAGE; P01023; -.
DR   CPTAC; non-CPTAC-1068; -.
DR   EPD; P01023; -.
DR   jPOST; P01023; -.
DR   MassIVE; P01023; -.
DR   MaxQB; P01023; -.
DR   PaxDb; P01023; -.
DR   PeptideAtlas; P01023; -.
DR   PRIDE; P01023; -.
DR   ProteomicsDB; 51307; -.
DR   Antibodypedia; 859; 915 antibodies.
DR   DNASU; 2; -.
DR   Ensembl; ENST00000318602; ENSP00000323929; ENSG00000175899.
DR   GeneID; 2; -.
DR   KEGG; hsa:2; -.
DR   UCSC; uc001qvk.2; human.
DR   CTD; 2; -.
DR   DisGeNET; 2; -.
DR   GeneCards; A2M; -.
DR   HGNC; HGNC:7; A2M.
DR   HPA; ENSG00000175899; Tissue enhanced (liver, lung).
DR   MalaCards; A2M; -.
DR   MIM; 103950; gene.
DR   neXtProt; NX_P01023; -.
DR   OpenTargets; ENSG00000175899; -.
DR   PharmGKB; PA24357; -.
DR   VEuPathDB; HostDB:ENSG00000175899.14; -.
DR   eggNOG; KOG1366; Eukaryota.
DR   GeneTree; ENSGT00940000154904; -.
DR   HOGENOM; CLU_001634_0_1_1; -.
DR   InParanoid; P01023; -.
DR   OMA; CFGEESQ; -.
DR   OrthoDB; 354230at2759; -.
DR   PhylomeDB; P01023; -.
DR   TreeFam; TF313285; -.
DR   PathwayCommons; P01023; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-194840; Rho GTPase cycle.
DR   Reactome; R-HSA-8963896; HDL assembly.
DR   SIGNOR; P01023; -.
DR   BioGRID-ORCS; 2; 2 hits in 987 CRISPR screens.
DR   ChiTaRS; A2M; human.
DR   EvolutionaryTrace; P01023; -.
DR   GenomeRNAi; 2; -.
DR   Pharos; P01023; Tbio.
DR   PRO; PR:P01023; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P01023; protein.
DR   Bgee; ENSG00000175899; Expressed in lung and 243 other tissues.
DR   ExpressionAtlas; P01023; baseline and differential.
DR   Genevisible; P01023; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0019838; F:growth factor binding; IDA:UniProtKB.
DR   GO; GO:0019966; F:interleukin-1 binding; IDA:UniProtKB.
DR   GO; GO:0019959; F:interleukin-8 binding; IPI:UniProtKB.
DR   GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IMP:AgBase.
DR   GO; GO:0043120; F:tumor necrosis factor binding; IDA:UniProtKB.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:2000267; P:negative regulation of blood coagulation, intrinsic pathway; TAS:Reactome.
DR   GO; GO:0001869; P:negative regulation of complement activation, lectin pathway; IDA:UniProtKB.
DR   GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR   CDD; cd02897; A2M_2; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.60.40.690; -; 1.
DR   InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR   InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR041813; A2M_TED.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR019742; MacrogloblnA2_CS.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR041555; MG3.
DR   InterPro; IPR040839; MG4.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   InterPro; IPR010916; TonB_box_CS.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF07677; A2M_recep; 1.
DR   Pfam; PF01835; MG2; 1.
DR   Pfam; PF17791; MG3; 1.
DR   Pfam; PF17789; MG4; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SMART; SM01361; A2M_recep; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF49410; SSF49410; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bait region; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Isopeptide bond; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal; Thioester bond.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   CHAIN           24..1474
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT                   /id="PRO_0000000055"
FT   REGION          690..728
FT                   /note="Bait region"
FT   REGION          704..709
FT                   /note="Inhibitory"
FT   REGION          719..723
FT                   /note="Inhibitory"
FT   REGION          730..735
FT                   /note="Inhibitory"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19139490"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:6203908"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6203908"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:6203908"
FT   CARBOHYD        869
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952"
FT   CARBOHYD        991
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:6203908"
FT   CARBOHYD        1424
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT                   ECO:0000269|PubMed:19159218"
FT   DISULFID        48..86
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        251..299
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        269..287
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        278
FT                   /note="Interchain (with C-431)"
FT                   /evidence="ECO:0000269|PubMed:2430963"
FT   DISULFID        431
FT                   /note="Interchain (with C-278)"
FT                   /evidence="ECO:0000269|PubMed:2430963"
FT   DISULFID        470..563
FT                   /evidence="ECO:0000269|PubMed:2430963"
FT   DISULFID        595..771
FT                   /evidence="ECO:0000269|PubMed:2430963,
FT                   ECO:0000269|PubMed:6203908"
FT   DISULFID        642..689
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        821..849
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        847..883
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        921..1321
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        1079..1127
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   DISULFID        1352..1467
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   CROSSLNK        693
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-? in other proteins)"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        694
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-? in other proteins)"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        972..975
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT                   /evidence="ECO:0000269|PubMed:6203908"
FT   VARIANT         639
FT                   /note="N -> D (in dbSNP:rs226405)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:15611997, ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|PubMed:2581245, ECO:0000269|Ref.3"
FT                   /id="VAR_026820"
FT   VARIANT         704
FT                   /note="R -> H (in dbSNP:rs1800434)"
FT                   /id="VAR_000012"
FT   VARIANT         815
FT                   /note="L -> Q (in dbSNP:rs3180392)"
FT                   /id="VAR_026821"
FT   VARIANT         972
FT                   /note="C -> Y (probably interferes with the activity;
FT                   dbSNP:rs1800433)"
FT                   /evidence="ECO:0000269|PubMed:1370808"
FT                   /id="VAR_000013"
FT   VARIANT         1000
FT                   /note="I -> V (in dbSNP:rs669)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:15611997, ECO:0000269|PubMed:1707161,
FT                   ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:2581245"
FT                   /id="VAR_000014"
FT   CONFLICT        63
FT                   /note="Missing (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="D -> V (in Ref. 3; AAT02228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350..353
FT                   /note="LSFV -> ACCS (in Ref. 6; AAH26246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        563
FT                   /note="C -> E (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        844
FT                   /note="A -> V (in Ref. 4; BAD92851)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        872
FT                   /note="V -> M (in Ref. 5; CAH18188)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1148
FT                   /note="A -> D (in Ref. 13; AAA51552)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1195
FT                   /note="H -> D (in Ref. 13; AAA51552)"
FT                   /evidence="ECO:0000305"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          143..151
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          174..182
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          187..193
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          201..208
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          214..221
FT                   /evidence="ECO:0007829|PDB:2P9R"
FT   STRAND          1341..1347
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   HELIX           1355..1359
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1360..1369
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1379..1384
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1389..1391
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   HELIX           1393..1400
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   TURN            1401..1403
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1407..1410
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1412..1419
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1427..1434
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1445..1450
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1454..1456
FT                   /evidence="ECO:0007829|PDB:1BV8"
FT   STRAND          1459..1463
FT                   /evidence="ECO:0007829|PDB:1BV8"
SQ   SEQUENCE   1474 AA;  163291 MW;  0A46DF09EFD3CF40 CRC64;
     MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TETTEKGCVL LSYLNETVTV
     SASLESVRGN RSLFTDLEAE NDVLHCVAFA VPKSSSNEEV MFLTVQVKGP TQEFKKRTTV
     MVKNEDSLVF VQTDKSIYKP GQTVKFRVVS MDENFHPLNE LIPLVYIQDP KGNRIAQWQS
     FQLEGGLKQF SFPLSSEPFQ GSYKVVVQKK SGGRTEHPFT VEEFVLPKFE VQVTVPKIIT
     ILEEEMNVSV CGLYTYGKPV PGHVTVSICR KYSDASDCHG EDSQAFCEKF SGQLNSHGCF
     YQQVKTKVFQ LKRKEYEMKL HTEAQIQEEG TVVELTGRQS SEITRTITKL SFVKVDSHFR
     QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD EHGLVQFSIN TTNVMGTSLT
     VRVNYKDRSP CYGYQWVSEE HEEAHHTAYL VFSPSKSFVH LEPMSHELPC GHTQTVQAHY
     ILNGGTLLGL KKLSFYYLIM AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL
     LIYAVLPTGD VIGDSAKYDV ENCLANKVDL SFSPSQSLPA SHAHLRVTAA PQSVCALRAV
     DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQDNE DCINRHNVYI NGITYTPVSS
     TNEKDMYSFL EDMGLKAFTN SKIRKPKMCP QLQQYEMHGP EGLRVGFYES DVMGRGHARL
     VHVEEPHTET VRKYFPETWI WDLVVVNSAG VAEVGVTVPD TITEWKAGAF CLSEDAGLGI
     SSTASLRAFQ PFFVELTMPY SVIRGEAFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE
     KEQAPHCICA NGRQTVSWAV TPKSLGNVNF TVSAEALESQ ELCGTEVPSV PEHGRKDTVI
     KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV LGDILGSAMQ
     NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEI KSKAIGYLNT GYQRQLNYKH
     YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA QARAYIFIDE AHITQALIWL SQRQKDNGCF
     RSSGSLLNNA IKGGVEDEVT LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH
     GSHVYTKALL AYAFALAGNQ DKRKEVLKSL NEEAVKKDNS VHWERPQKPK APVGHFYEPQ
     APSAEVEMTS YVLLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS TQDTVVALHA
     LSKYGAATFT RTGKAAQVTI QSSGTFSSKF QVDNNNRLLL QQVSLPELPG EYSMKVTGEG
     CVYLQTSLKY NILPEKEEFP FALGVQTLPQ TCDEPKAHTS FQISLSVSYT GSRSASNMAI
     VDVKMVSGFI PLKPTVKMLE RSNHVSRTEV SSNHVLIYLD KVSNQTLSLF FTVLQDVPVR
     DLKPAIVKVY DYYETDEFAI AEYNAPCSKD LGNA
//
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