CBPA1_HUMAN
ID CBPA1_HUMAN Reviewed; 419 AA.
AC P15085; A4D1M1; Q53XU0; Q9BS67; Q9UCF2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Carboxypeptidase A1 {ECO:0000305};
DE EC=3.4.17.1 {ECO:0000269|PubMed:8806703};
DE Flags: Precursor;
GN Name=CPA1 {ECO:0000312|HGNC:HGNC:2296}; Synonyms=CPA;
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].
RC TISSUE=Pancreas;
RX PubMed=1417781; DOI=10.1042/bj2870299;
RA Catasus L., Villegas V., Pascual R., Aviles F.X., Wicker-Planquart C.,
RA Puigserver A.;
RT "cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase
RT A1.";
RL Biochem. J. 287:299-303(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 MRNA], AND VARIANT ARG-276.
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 [5]
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 [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-276.
RC TISSUE=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 [8]
RP PROTEIN SEQUENCE OF 17-43 AND 114-135, AND INTERACTION WITH PROELASTASE 2.
RX PubMed=2307232; DOI=10.1016/0014-5793(90)80665-6;
RA Moulard M., Michon T., Kerfelec B., Chapus C.;
RT "Further studies on the human pancreatic binary complexes involving
RT procarboxypeptidase A.";
RL FEBS Lett. 261:179-183(1990).
RN [9]
RP PROTEIN SEQUENCE OF 17-42.
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 [10]
RP PROTEIN SEQUENCE OF 113-143.
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 330-396.
RX PubMed=1969228;
RA Stewart E.A., Craik C.S., Hake L., Bowcock A.M.;
RT "Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter.";
RL Am. J. Hum. Genet. 46:795-800(1990).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 111-419 IN COMPLEX WITH
RP POLYACRYLIC ACID AND ZINC IONS, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=18566513; DOI=10.1107/s0907444908013474;
RA Pallares I., Fernandez D., Comellas-Bigler M., Fernandez-Recio J.,
RA Ventura S., Aviles F.X., Bode W., Vendrell J.;
RT "Direct interaction between a human digestive protease and the mucoadhesive
RT poly(acrylic acid).";
RL Acta Crystallogr. D 64:784-791(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 112-418 IN COMPLEX WITH ASCARIS
RP CARBOXYPEPTIDASE INHIBITOR AND ZINC IONS, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=19179285; DOI=10.1073/pnas.0812623106;
RA Sanglas L., Aviles F.X., Huber R., Gomis-Rueth F.X., Arolas J.L.;
RT "Mammalian metallopeptidase inhibition at the defense barrier of Ascaris
RT parasite.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1743-1747(2009).
CC -!- FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal
CC amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or
CC -Pro (PubMed:8806703). Catalyzes the conversion of leukotriene C4 to
CC leukotriene F4 via the hydrolysis of an amide bond (By similarity).
CC {ECO:0000250|UniProtKB:P00730, ECO:0000269|PubMed:8806703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid, but little or no action
CC with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1;
CC Evidence={ECO:0000269|PubMed:8806703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene C4 = glycine + leukotriene F4;
CC Xref=Rhea:RHEA:50740, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:133618;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50741;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18566513};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18566513};
CC -!- SUBUNIT: Monomer. May form a complex with proelastase 2.
CC {ECO:0000269|PubMed:18566513, ECO:0000269|PubMed:19179285}.
CC -!- INTERACTION:
CC P15085; P19399; Xeno; NbExp=2; IntAct=EBI-1642148, EBI-15754788;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; X67318; CAA47732.1; -; mRNA.
DR EMBL; AK291493; BAF84182.1; -; mRNA.
DR EMBL; BT007313; AAP35977.1; -; mRNA.
DR EMBL; CH236950; EAL24089.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83763.1; -; Genomic_DNA.
DR EMBL; BC005279; AAH05279.1; -; mRNA.
DR CCDS; CCDS5820.1; -.
DR PIR; S29127; S29127.
DR RefSeq; NP_001859.1; NM_001868.3.
DR PDB; 2V77; X-ray; 1.60 A; A/B=111-419.
DR PDB; 3FJU; X-ray; 1.60 A; A=112-418.
DR PDB; 4UEE; X-ray; 2.27 A; A/B=111-419.
DR PDB; 4UEF; X-ray; 1.69 A; A/B=111-419.
DR PDB; 4UEZ; X-ray; 2.29 A; A/B=111-419.
DR PDB; 4UF4; X-ray; 1.77 A; A/B=1-419.
DR PDB; 5OM9; X-ray; 1.80 A; A/B=1-419.
DR PDB; 6I6Z; X-ray; 1.72 A; A/B=111-418.
DR PDBsum; 2V77; -.
DR PDBsum; 3FJU; -.
DR PDBsum; 4UEE; -.
DR PDBsum; 4UEF; -.
DR PDBsum; 4UEZ; -.
DR PDBsum; 4UF4; -.
DR PDBsum; 5OM9; -.
DR PDBsum; 6I6Z; -.
DR AlphaFoldDB; P15085; -.
DR SMR; P15085; -.
DR BioGRID; 107749; 1.
DR DIP; DIP-48699N; -.
DR IntAct; P15085; 3.
DR STRING; 9606.ENSP00000011292; -.
DR BindingDB; P15085; -.
DR ChEMBL; CHEMBL2088; -.
DR DrugBank; DB06924; (2R)-2-benzyl-3-nitropropanoic acid.
DR DrugBank; DB07484; (2R)-4,4-dihydroxy-5-nitro-2-(phenylmethyl)pentanoic acid.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB03441; 2-Benzyl-3-Iodopropanoic Acid.
DR DrugBank; DB04316; D-[(N-Hydroxyamino)Carbonyl]Phenylalanine.
DR DrugBank; DB03201; D-Cysteine.
DR DrugBank; DB11095; Desirudin.
DR DrugBank; DB02652; L-[(N-Hydroxyamino)Carbonyl]Phenylalanine.
DR DrugBank; DB07506; L-BENZYLSUCCINIC ACID.
DR DrugBank; DB04058; N-Carbamoylphenylalanine.
DR DrugBank; DB07351; O-(((1R)-((N-(PHENYL-METHOXY-CARBONYL)-ALANYL)-AMINO)METHYL)HYDROXYPHOSPHINYL)3-L-PHENYLLACTATE.
DR DrugBank; DB08762; O-(((1R)-((N-PHENYLMETHOXYCARBONYL-L-ALANYL)AMINO)ETHYL)HYDROXYPHOSPHONO)-L-BENZYLACETIC ACID.
DR DrugBank; DB08368; OCTANE-1,3,5,7-TETRACARBOXYLIC ACID.
DR DrugBank; DB03012; Phenylalanine-N-Sulfonamide.
DR GuidetoPHARMACOLOGY; 1587; -.
DR MEROPS; M14.001; -.
DR iPTMnet; P15085; -.
DR PhosphoSitePlus; P15085; -.
DR BioMuta; CPA1; -.
DR DMDM; 399196; -.
DR jPOST; P15085; -.
DR MassIVE; P15085; -.
DR MaxQB; P15085; -.
DR PaxDb; P15085; -.
DR PeptideAtlas; P15085; -.
DR PRIDE; P15085; -.
DR ProteomicsDB; 53103; -.
DR Antibodypedia; 17964; 540 antibodies from 39 providers.
DR DNASU; 1357; -.
DR Ensembl; ENST00000011292.8; ENSP00000011292.3; ENSG00000091704.10.
DR GeneID; 1357; -.
DR KEGG; hsa:1357; -.
DR MANE-Select; ENST00000011292.8; ENSP00000011292.3; NM_001868.4; NP_001859.1.
DR UCSC; uc003vpx.4; human.
DR CTD; 1357; -.
DR DisGeNET; 1357; -.
DR GeneCards; CPA1; -.
DR GeneReviews; CPA1; -.
DR HGNC; HGNC:2296; CPA1.
DR HPA; ENSG00000091704; Tissue enriched (pancreas).
DR MalaCards; CPA1; -.
DR MIM; 114850; gene.
DR neXtProt; NX_P15085; -.
DR OpenTargets; ENSG00000091704; -.
DR Orphanet; 676; Hereditary chronic pancreatitis.
DR PharmGKB; PA26816; -.
DR VEuPathDB; HostDB:ENSG00000091704; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000158082; -.
DR InParanoid; P15085; -.
DR OMA; SHGISYE; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; P15085; -.
DR TreeFam; TF317197; -.
DR BRENDA; 3.4.17.1; 2681.
DR PathwayCommons; P15085; -.
DR SignaLink; P15085; -.
DR BioGRID-ORCS; 1357; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; CPA1; human.
DR EvolutionaryTrace; P15085; -.
DR GeneWiki; Carboxypeptidase_A1; -.
DR GenomeRNAi; 1357; -.
DR Pharos; P15085; Tchem.
DR PRO; PR:P15085; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P15085; protein.
DR Bgee; ENSG00000091704; Expressed in body of pancreas and 93 other tissues.
DR ExpressionAtlas; P15085; baseline and differential.
DR Genevisible; P15085; HS.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006691; P:leukotriene metabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
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..16
FT /evidence="ECO:0000269|PubMed:2307232,
FT ECO:0000269|PubMed:2920728"
FT PROPEP 17..110
FT /note="Activation peptide"
FT /id="PRO_0000004345"
FT CHAIN 111..419
FT /note="Carboxypeptidase A1"
FT /id="PRO_0000004346"
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:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT BINDING 307..308
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0007744|PDB:2V77"
FT DISULFID 248..271
FT /evidence="ECO:0000269|PubMed:18566513,
FT ECO:0000269|PubMed:19179285"
FT VARIANT 208
FT /note="A -> T (in dbSNP:rs34474469)"
FT /id="VAR_048593"
FT VARIANT 276
FT /note="H -> R (in dbSNP:rs17849959)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_054311"
FT CONFLICT 139..141
FT /note="NPH -> HPG (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:4UF4"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:4UF4"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4UF4"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4UF4"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:4UF4"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4UF4"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:4UF4"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4UF4"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:4UF4"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:3FJU"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4UEE"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:3FJU"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:3FJU"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:3FJU"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:3FJU"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:3FJU"
SQ SEQUENCE 419 AA; 47140 MW; 439FAFFFAEE958B1 CRC64;
MRGLLVLSVL LGAVFGKEDF VGHQVLRISV ADEAQVQKVK ELEDLEHLQL DFWRGPAHPG
SPIDVRVPFP SIQAVKIFLE SHGISYETMI EDVQSLLDEE QEQMFAFRSR ARSTDTFNYA
TYHTLEEIYD FLDLLVAENP HLVSKIQIGN TYEGRPIYVL KFSTGGSKRP AIWIDTGIHS
REWVTQASGV WFAKKITQDY GQDAAFTAIL DTLDIFLEIV TNPDGFAFTH STNRMWRKTR
SHTAGSLCIG VDPNRNWDAG FGLSGASSNP CSETYHGKFA NSEVEVKSIV DFVKDHGNIK
AFISIHSYSQ LLMYPYGYKT EPVPDQDELD QLSKAAVTAL ASLYGTKFNY GSIIKAIYQA
SGSTIDWTYS QGIKYSFTFE LRDTGRYGFL LPASQIIPTA KETWLALLTI MEHTLNHPY
