CBPA2_HUMAN
ID CBPA2_HUMAN Reviewed; 419 AA.
AC P48052; A4D1M4; C9JIK1; Q53XS1; Q96A12; Q96QN3; Q9UCF1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Carboxypeptidase A2;
DE EC=3.4.17.15;
DE Flags: Precursor;
GN Name=CPA2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-82.
RC TISSUE=Brain, and Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-419, AND 3D-STRUCTURE MODELING.
RC TISSUE=Pancreas;
RX PubMed=7896805; DOI=10.1074/jbc.270.12.6651;
RA Catasus L., Vendrell J., Aviles F.X., Carreira S., Puigserver A.,
RA Billeter M.;
RT "The sequence and conformation of human pancreatic procarboxypeptidase A2.
RT cDNA cloning, sequence analysis, and three-dimensional model.";
RL J. Biol. Chem. 270:6651-6657(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-419, AND CHARACTERIZATION.
RX PubMed=8806703; DOI=10.1006/abbi.1996.0310;
RA Laethem R.M., Blumenkopf T.A., Cory M., Elwell L., Moxham C.P., Ray P.H.,
RA Walton L.M., Smith G.K.;
RT "Expression and characterization of human pancreatic preprocarboxypeptidase
RT A1 and preprocarboxypeptidase A2.";
RL Arch. Biochem. Biophys. 332:8-18(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-419, AND VARIANT GLY-82.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 19-45, AND CHARACTERIZATION.
RX PubMed=2920728; DOI=10.1111/j.1432-1033.1989.tb14590.x;
RA Pascual R., Burgos F.J., Salva M., Soriano F., Mendez E., Aviles F.X.;
RT "Purification and properties of five different forms of human
RT procarboxypeptidases.";
RL Eur. J. Biochem. 179:609-616(1989).
RN [8]
RP PROTEIN SEQUENCE OF 115-144.
RC TISSUE=Pancreas;
RX PubMed=8318831; DOI=10.1002/bmc.1130070308;
RA Linder D., Linder M., Schade H., Sziegoleit A.;
RT "Separation of human pancreatic carboxypeptidase A isoenzymes by high
RT performance liquid chromatography.";
RL Biomed. Chromatogr. 7:143-145(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 19-419 IN COMPLEX WITH ZINC,
RP DISULFIDE BONDS, AND COFACTOR.
RX PubMed=9384570; DOI=10.1093/emboj/16.23.6906;
RA Garcia-Saez I., Reverter D., Vendrell J., Aviles F.X., Coll M.;
RT "The three-dimensional structure of human procarboxypeptidase A2.
RT Deciphering the basis of the inhibition, activation and intrinsic activity
RT of the zymogen.";
RL EMBO J. 16:6906-6913(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-419.
RX PubMed=9450539; DOI=10.1016/s0014-5793(97)01476-2;
RA Reverter D., Garcia-Saez I., Catasus L., Vendrell J., Coll M., Aviles F.X.;
RT "Characterisation and preliminary X-ray diffraction analysis of human
RT pancreatic procarboxypeptidase A2.";
RL FEBS Lett. 420:7-10(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 118-419 IN COMPLEX WITH ZINC,
RP DISULFIDE BONDS, AND COFACTOR.
RX PubMed=10742178; DOI=10.1038/74092;
RA Reverter D., Fernandez-Catalan C., Baumgartner R., Pfander R., Huber R.,
RA Bode W., Vendrell J., Holak T.A., Aviles F.X.;
RT "Structure of a novel leech carboxypeptidase inhibitor determined free in
RT solution and in complex with human carboxypeptidase A2.";
RL Nat. Struct. Biol. 7:322-328(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=12948494; DOI=10.1016/s0022-2836(03)00888-x;
RA Dantas G., Kuhlman B., Callender D., Wong M., Baker D.;
RT "A large scale test of computational protein design: folding and stability
RT of nine completely redesigned globular proteins.";
RL J. Mol. Biol. 332:449-460(2003).
RN [13]
RP STRUCTURE BY NMR OF 19-96.
RX PubMed=12538893; DOI=10.1110/ps.0227303;
RA Jimenez M.A., Villegas V., Santoro J., Serrano L., Vendrell J.,
RA Aviles F.X., Rico M.;
RT "NMR solution structure of the activation domain of human
RT procarboxypeptidase A2.";
RL Protein Sci. 12:296-305(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to that of carboxypeptidase A (EC 3.4.17.1), but with
CC a preference for bulkier C-terminal residues.; EC=3.4.17.15;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10742178,
CC ECO:0000269|PubMed:9384570};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74425.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH07009.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH14571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH15140.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAL24092.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC024085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24092.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC007009; AAH07009.1; ALT_INIT; mRNA.
DR EMBL; BC014571; AAH14571.1; ALT_INIT; mRNA.
DR EMBL; BC015140; AAH15140.1; ALT_INIT; mRNA.
DR EMBL; U19977; AAA74425.1; ALT_INIT; mRNA.
DR EMBL; BT007403; AAP36067.1; -; mRNA.
DR CCDS; CCDS5817.2; -.
DR PIR; A56171; A56171.
DR RefSeq; NP_001860.2; NM_001869.2.
DR PDB; 1AYE; X-ray; 1.80 A; A=19-419.
DR PDB; 1DTD; X-ray; 1.65 A; A=118-419.
DR PDB; 1O6X; NMR; -; A=19-96.
DR PDBsum; 1AYE; -.
DR PDBsum; 1DTD; -.
DR PDBsum; 1O6X; -.
DR AlphaFoldDB; P48052; -.
DR BMRB; P48052; -.
DR SMR; P48052; -.
DR BioGRID; 107750; 8.
DR IntAct; P48052; 8.
DR MINT; P48052; -.
DR STRING; 9606.ENSP00000222481; -.
DR BindingDB; P48052; -.
DR ChEMBL; CHEMBL4939; -.
DR MEROPS; M14.002; -.
DR iPTMnet; P48052; -.
DR PhosphoSitePlus; P48052; -.
DR BioMuta; CPA2; -.
DR DMDM; 294862522; -.
DR MassIVE; P48052; -.
DR PaxDb; P48052; -.
DR PeptideAtlas; P48052; -.
DR PRIDE; P48052; -.
DR ProteomicsDB; 55843; -.
DR Antibodypedia; 17945; 540 antibodies from 32 providers.
DR DNASU; 1358; -.
DR Ensembl; ENST00000222481.9; ENSP00000222481.4; ENSG00000158516.12.
DR GeneID; 1358; -.
DR KEGG; hsa:1358; -.
DR MANE-Select; ENST00000222481.9; ENSP00000222481.4; NM_001869.3; NP_001860.2.
DR UCSC; uc003vpq.4; human.
DR CTD; 1358; -.
DR DisGeNET; 1358; -.
DR GeneCards; CPA2; -.
DR HGNC; HGNC:2297; CPA2.
DR HPA; ENSG00000158516; Tissue enriched (pancreas).
DR MIM; 600688; gene.
DR neXtProt; NX_P48052; -.
DR OpenTargets; ENSG00000158516; -.
DR PharmGKB; PA26817; -.
DR VEuPathDB; HostDB:ENSG00000158516; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000160121; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; P48052; -.
DR OMA; DTIYSWM; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; P48052; -.
DR TreeFam; TF317197; -.
DR BRENDA; 3.4.17.15; 2681.
DR PathwayCommons; P48052; -.
DR SABIO-RK; P48052; -.
DR SignaLink; P48052; -.
DR BioGRID-ORCS; 1358; 8 hits in 1063 CRISPR screens.
DR ChiTaRS; CPA2; human.
DR EvolutionaryTrace; P48052; -.
DR GeneWiki; Carboxypeptidase_A2; -.
DR GenomeRNAi; 1358; -.
DR Pharos; P48052; Tchem.
DR PRO; PR:P48052; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P48052; protein.
DR Bgee; ENSG00000158516; Expressed in body of pancreas and 100 other tissues.
DR ExpressionAtlas; P48052; baseline and differential.
DR Genevisible; P48052; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd03870; M14_CPA; 1.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR034248; CPA_M14_CPD.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..114
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8318831"
FT /id="PRO_0000004353"
FT CHAIN 115..419
FT /note="Carboxypeptidase A2"
FT /id="PRO_0000004354"
FT ACT_SITE 380
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 179..182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10742178,
FT ECO:0000269|PubMed:9384570"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10742178,
FT ECO:0000269|PubMed:9384570"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10742178,
FT ECO:0000269|PubMed:9384570"
FT BINDING 307..308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 248..271
FT /evidence="ECO:0000269|PubMed:10742178,
FT ECO:0000269|PubMed:9384570"
FT DISULFID 320..354
FT /evidence="ECO:0000269|PubMed:10742178,
FT ECO:0000269|PubMed:9384570"
FT VARIANT 82
FT /note="E -> G (in dbSNP:rs17850135)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT /id="VAR_031204"
FT CONFLICT 19
FT /note="L -> S (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="K -> N (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="T -> I (in Ref. 4; AAA74425)"
FT /evidence="ECO:0000305"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1AYE"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1AYE"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1AYE"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:1AYE"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1AYE"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:1DTD"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:1DTD"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1AYE"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:1DTD"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:1DTD"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1DTD"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:1DTD"
SQ SEQUENCE 419 AA; 47030 MW; 00269F2AE50CA38D CRC64;
MAMRLILFFG ALFGHIYCLE TFVGDQVLEI VPSNEEQIKN LLQLEAQEHL QLDFWKSPTT
PGETAHVRVP FVNVQAVKVF LESQGIAYSI MIEDVQVLLD KENEEMLFNR RRERSGNFNF
GAYHTLEEIS QEMDNLVAEH PGLVSKVNIG SSFENRPMNV LKFSTGGDKP AIWLDAGIHA
REWVTQATAL WTANKIVSDY GKDPSITSIL DALDIFLLPV TNPDGYVFSQ TKNRMWRKTR
SKVSGSLCVG VDPNRNWDAG FGGPGASSNP CSDSYHGPSA NSEVEVKSIV DFIKSHGKVK
AFITLHSYSQ LLMFPYGYKC TKLDDFDELS EVAQKAAQSL RSLHGTKYKV GPICSVIYQA
SGGSIDWSYD YGIKYSFAFE LRDTGRYGFL LPARQILPTA EETWLGLKAI MEHVRDHPY
