CBPA4_HUMAN
ID CBPA4_HUMAN Reviewed; 421 AA.
AC Q9UI42; B7Z576; Q86UY9;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Carboxypeptidase A4;
DE EC=3.4.17.-;
DE AltName: Full=Carboxypeptidase A3;
DE Flags: Precursor;
GN Name=CPA4; Synonyms=CPA3; ORFNames=UNQ694/PRO1339;
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] (ISOFORM 1), FUNCTION, AND INDUCTION.
RX PubMed=10383164;
RA Huang H., Reed C.P., Zhang J.S., Shridhar V., Wang L., Smith D.I.;
RT "Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone
RT deacetylase inhibitors during differentiation of prostate epithelial cancer
RT cells.";
RL Cancer Res. 59:2981-2988(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP IMPRINTING.
RX PubMed=12552318; DOI=10.1007/s00439-002-0891-3;
RA Kayashima T., Yamasaki K., Yamada T., Sakai H., Miwa N., Ohta T.,
RA Yoshiura K., Matsumoto N., Nakane Y., Kanetake H., Ishino F., Niikawa N.,
RA Kishino T.;
RT "The novel imprinted carboxypeptidase A4 gene (CPA4) in the 7q32 imprinting
RT domain.";
RL Hum. Genet. 112:220-226(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=20385563; DOI=10.1074/jbc.m109.060350;
RA Tanco S., Zhang X., Morano C., Aviles F.X., Lorenzo J., Fricker L.D.;
RT "Characterization of the substrate specificity of human carboxypeptidase A4
RT and implications for a role in extracellular peptide processing.";
RL J. Biol. Chem. 285:18385-18396(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-421 IN COMPLEX WITH LXN AND
RP ZINC IONS, GLYCOSYLATION AT ASN-260, AND DISULFIDE BOND.
RX PubMed=16091843; DOI=10.1007/s00018-005-5174-4;
RA Garcia-Castellanos R., Bonet-Figueredo R., Pallares I., Ventura S.,
RA Aviles F.X., Vendrell J., Gomis-Rueth F.-X.;
RT "Detailed molecular comparison between the inhibition mode of A/B-type
RT carboxypeptidases in the zymogen state and by the endogenous inhibitor
RT latexin.";
RL Cell. Mol. Life Sci. 62:1996-2014(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 114-421 IN COMPLEX WITH LXN,
RP GLYCOSYLATION AT ASN-260, AND DISULFIDE BOND.
RX PubMed=15738388; DOI=10.1073/pnas.0500678102;
RA Pallares I., Bonet R., Garcia-Castellanos R., Ventura S., Aviles F.X.,
RA Vendrell J., Gomis-Rueth F.-X.;
RT "Structure of human carboxypeptidase A4 with its endogenous protein
RT inhibitor, latexin.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3978-3983(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 112-421 IN COMPLEX WITH
RP N.VERSICOLOR MCPI AND ZINC, COFACTOR, SUBUNIT, ACTIVITY REGULATION, AND
RP DISULFIDE BOND.
RX PubMed=22294694; DOI=10.1074/jbc.m111.330100;
RA Covaleda G., del Rivero M.A., Chavez M.A., Aviles F.X., Reverter D.;
RT "Crystal structure of novel metallocarboxypeptidase inhibitor from marine
RT mollusk Nerita versicolor in complex with human carboxypeptidase A4.";
RL J. Biol. Chem. 287:9250-9258(2012).
CC -!- FUNCTION: Metalloprotease that could be involved in the histone
CC hyperacetylation pathway (PubMed:10383164). Releases a C-terminal amino
CC acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val
CC (PubMed:20385563). {ECO:0000269|PubMed:10383164,
CC ECO:0000269|PubMed:20385563}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22294694};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22294694};
CC -!- ACTIVITY REGULATION: Inhibited by interaction with the
CC metallocarboxypeptidase inhibitor (MCPI) from N.versicolor that binds
CC to the catalytic zinc ion. {ECO:0000269|PubMed:22294694}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55.6 uM for 3-(2-furyl)acryloyl-Phe-Phe
CC {ECO:0000269|PubMed:20385563};
CC KM=19.4 uM for 3-(2-furyl)acryloyl-Phe-Leu
CC {ECO:0000269|PubMed:20385563};
CC KM=23.3 uM for 3-(2-furyl)acryloyl-Phe-Ile
CC {ECO:0000269|PubMed:20385563};
CC KM=40.4 uM for 3-(2-furyl)acryloyl-Phe-Met
CC {ECO:0000269|PubMed:20385563};
CC KM=57.3 uM for 3-(2-furyl)acryloyl-Phe-Val
CC {ECO:0000269|PubMed:20385563};
CC KM=0.329 uM for neurotensin {ECO:0000269|PubMed:20385563};
CC KM=9.23 uM for Met-enkephalin-Arg-Phe {ECO:0000269|PubMed:20385563};
CC pH dependence:
CC Optimum pH is 8.5-9. {ECO:0000269|PubMed:20385563};
CC -!- SUBUNIT: Monomer. Interacts with LXN. {ECO:0000269|PubMed:15738388,
CC ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:22294694}.
CC -!- INTERACTION:
CC Q9UI42-1; P84875; Xeno; NbExp=3; IntAct=EBI-16060275, EBI-16060264;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UI42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UI42-2; Sequence=VSP_042894;
CC -!- TISSUE SPECIFICITY: Fetal expression in the adrenal gland, brain,
CC heart, intestine, kidney, liver and lung. Except for fetal brain that
CC shows no imprinting, expression was found preferentially from the
CC maternal allele.
CC -!- INDUCTION: Up-regulated by inhibitors of histone dacetylation.
CC {ECO:0000269|PubMed:10383164}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {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; AF095719; AAF23230.1; -; mRNA.
DR EMBL; AY358699; AAQ89062.1; -; mRNA.
DR EMBL; AK298550; BAH12812.1; -; mRNA.
DR EMBL; AC024085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052289; AAH52289.1; -; mRNA.
DR CCDS; CCDS55163.1; -. [Q9UI42-2]
DR CCDS; CCDS5818.1; -. [Q9UI42-1]
DR RefSeq; NP_001156918.1; NM_001163446.1. [Q9UI42-2]
DR RefSeq; NP_057436.2; NM_016352.3. [Q9UI42-1]
DR PDB; 2BO9; X-ray; 1.60 A; A/C=114-421.
DR PDB; 2BOA; X-ray; 2.20 A; A/B=19-421.
DR PDB; 2PCU; X-ray; 1.60 A; A=116-420.
DR PDB; 4A94; X-ray; 1.70 A; A/B=112-421.
DR PDB; 4BD9; X-ray; 2.20 A; A=112-421.
DR PDBsum; 2BO9; -.
DR PDBsum; 2BOA; -.
DR PDBsum; 2PCU; -.
DR PDBsum; 4A94; -.
DR PDBsum; 4BD9; -.
DR AlphaFoldDB; Q9UI42; -.
DR SMR; Q9UI42; -.
DR BioGRID; 119373; 130.
DR DIP; DIP-60558N; -.
DR IntAct; Q9UI42; 21.
DR STRING; 9606.ENSP00000222482; -.
DR BindingDB; Q9UI42; -.
DR ChEMBL; CHEMBL2644; -.
DR MEROPS; M14.017; -.
DR GlyConnect; 1065; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UI42; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9UI42; -.
DR PhosphoSitePlus; Q9UI42; -.
DR SwissPalm; Q9UI42; -.
DR BioMuta; CPA4; -.
DR DMDM; 61252703; -.
DR EPD; Q9UI42; -.
DR jPOST; Q9UI42; -.
DR MassIVE; Q9UI42; -.
DR MaxQB; Q9UI42; -.
DR PaxDb; Q9UI42; -.
DR PeptideAtlas; Q9UI42; -.
DR PRIDE; Q9UI42; -.
DR ProteomicsDB; 84471; -. [Q9UI42-1]
DR ProteomicsDB; 84472; -. [Q9UI42-2]
DR Antibodypedia; 17950; 90 antibodies from 26 providers.
DR DNASU; 51200; -.
DR Ensembl; ENST00000222482.10; ENSP00000222482.4; ENSG00000128510.12. [Q9UI42-1]
DR Ensembl; ENST00000445470.6; ENSP00000412947.2; ENSG00000128510.12. [Q9UI42-2]
DR GeneID; 51200; -.
DR KEGG; hsa:51200; -.
DR MANE-Select; ENST00000222482.10; ENSP00000222482.4; NM_016352.4; NP_057436.2.
DR UCSC; uc003vpr.4; human. [Q9UI42-1]
DR CTD; 51200; -.
DR DisGeNET; 51200; -.
DR GeneCards; CPA4; -.
DR HGNC; HGNC:15740; CPA4.
DR HPA; ENSG00000128510; Tissue enhanced (esophagus, skin).
DR MIM; 607635; gene.
DR neXtProt; NX_Q9UI42; -.
DR OpenTargets; ENSG00000128510; -.
DR PharmGKB; PA26819; -.
DR VEuPathDB; HostDB:ENSG00000128510; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161774; -.
DR InParanoid; Q9UI42; -.
DR OMA; QQNEGQE; -.
DR PhylomeDB; Q9UI42; -.
DR TreeFam; TF317197; -.
DR BRENDA; 3.4.17.1; 2681.
DR PathwayCommons; Q9UI42; -.
DR SignaLink; Q9UI42; -.
DR BioGRID-ORCS; 51200; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; CPA4; human.
DR EvolutionaryTrace; Q9UI42; -.
DR GeneWiki; CPA4_(gene); -.
DR GenomeRNAi; 51200; -.
DR Pharos; Q9UI42; Tchem.
DR PRO; PR:Q9UI42; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UI42; protein.
DR Bgee; ENSG00000128510; Expressed in skin of abdomen and 87 other tissues.
DR ExpressionAtlas; Q9UI42; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016573; P:histone acetylation; NAS:UniProtKB.
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; Alternative splicing; Carboxypeptidase; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..113
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000004357"
FT CHAIN 114..421
FT /note="Carboxypeptidase A4"
FT /id="PRO_0000004358"
FT ACT_SITE 382
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 181..184
FT /ligand="substrate"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22294694"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22294694"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 275..276
FT /ligand="substrate"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22294694"
FT BINDING 309..310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15738388,
FT ECO:0000269|PubMed:16091843"
FT DISULFID 250..273
FT /evidence="ECO:0000269|PubMed:15738388,
FT ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:22294694"
FT VAR_SEQ 96..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042894"
FT VARIANT 27
FT /note="L -> F (in dbSNP:rs34587586)"
FT /id="VAR_048594"
FT VARIANT 157
FT /note="P -> T (in dbSNP:rs3735051)"
FT /id="VAR_020393"
FT VARIANT 183
FT /note="R -> L (in dbSNP:rs3735053)"
FT /id="VAR_048595"
FT VARIANT 303
FT /note="G -> C (in dbSNP:rs2171492)"
FT /id="VAR_020394"
FT CONFLICT 18
FT /note="Q -> R (in Ref. 1; AAF23230)"
FT /evidence="ECO:0000305"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2BOA"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:2BOA"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:2BOA"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2BOA"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2BOA"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2BOA"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2BOA"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2BOA"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:2BOA"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2BOA"
FT HELIX 94..115
FT /evidence="ECO:0007829|PDB:2BOA"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2BOA"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:2BO9"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:2BO9"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:2BO9"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:2BO9"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:4BD9"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:2BO9"
FT HELIX 398..417
FT /evidence="ECO:0007829|PDB:2BO9"
SQ SEQUENCE 421 AA; 47351 MW; 52750CC50B470EC9 CRC64;
MRWILFIGAL IGSSICGQEK FFGDQVLRIN VRNGDEISKL SQLVNSNNLK LNFWKSPSSF
NRPVDVLVPS VSLQAFKSFL RSQGLEYAVT IEDLQALLDN EDDEMQHNEG QERSSNNFNY
GAYHSLEAIY HEMDNIAADF PDLARRVKIG HSFENRPMYV LKFSTGKGVR RPAVWLNAGI
HSREWISQAT AIWTARKIVS DYQRDPAITS ILEKMDIFLL PVANPDGYVY TQTQNRLWRK
TRSRNPGSSC IGADPNRNWN ASFAGKGASD NPCSEVYHGP HANSEVEVKS VVDFIQKHGN
FKGFIDLHSY SQLLMYPYGY SVKKAPDAEE LDKVARLAAK ALASVSGTEY QVGPTCTTVY
PASGSSIDWA YDNGIKFAFT FELRDTGTYG FLLPANQIIP TAEETWLGLK TIMEHVRDNL
Y
