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Serpin B3 (Protein T4-A) (Squamous cell carcinoma antigen 1) (SCCA-1)

 SPB3_HUMAN              Reviewed;         390 AA.
P29508; A6NDM2; B2RBT5; B3W5Y6; Q53H28; Q53YB5; Q86VF3; Q86W04;
Q8IWL4; Q8IXI3; Q96J21; Q9BYF8;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
25-OCT-2017, entry version 176.
RecName: Full=Serpin B3;
AltName: Full=Protein T4-A;
AltName: Full=Squamous cell carcinoma antigen 1;
Short=SCCA-1;
Name=SERPINB3; Synonyms=SCCA, SCCA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
VARIANT ALA-357.
PubMed=1958219; DOI=10.1016/S0006-291X(05)81380-4;
Suminami Y., Kishi F., Sekiguchi K., Kato H.;
"Squamous cell carcinoma antigen is a new member of the serine
protease inhibitors.";
Biochem. Biophys. Res. Commun. 181:51-58(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=7724531; DOI=10.1073/pnas.92.8.3147;
Schneider S.S., Schick C., Fish K.E., Miller E., Pena J.C.,
Treter S.D., Hui S.M., Silverman G.A.;
"A serine proteinase inhibitor locus at 18q21.3 contains a tandem
duplication of the human squamous cell carcinoma antigen gene.";
Proc. Natl. Acad. Sci. U.S.A. 92:3147-3151(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ALA-357.
Suminami Y., Kishi F., Murakami A., Sakaguchi Y., Kato H.;
"Novel forms of SCC antigen transcripts produced by alternative
splicing.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-351, AND
MUTAGENESIS OF ALA-341; PHE-352 AND 354-SER-SER-355.
TISSUE=Hepatoma;
PubMed=12975381; DOI=10.1074/jbc.M302842200;
Moore P.L., Ong S., Harrison T.J.;
"Squamous cell carcinoma antigen 1-mediated binding of hepatitis B
virus to hepatocytes does not involve the hepatic serpin clearance
system.";
J. Biol. Chem. 278:46709-46717(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hepatoma;
Tong C., Chenyu X., Jun Z., Ningshao X.;
"SCCA1 mRNA sequence from human hepatocellular carcinoma cell line
HepG2, complete cds.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-351.
TISSUE=Liver;
Turato C., Biasiolo A., Quarta S., Beneduce L., Zuin J., Fassina G.,
Gatta A., Pontisso P.;
"Characterization of the new isoform of squamous cell carcinoma
antigen-1 (SCCA-PD) detected in hepatocellular carcinoma.";
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-357.
TISSUE=Dermoid cancer;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 1-21; 88-94; 112-125; 147-160; 215-260; 266-300;
322-331 AND 378-386, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Bensaad K., Vousden K.H.;
Submitted (FEB-2008) to UniProtKB.
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 109-390 (ISOFORM 1), VARIANT ALA-351,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Liver cancer;
PubMed=14970861; DOI=10.1038/sj.bjc.6601543;
Pontisso P., Calabrese F., Benvegnu L., Lise M., Belluco C.,
Ruvoletto M.G., De Falco S., Marino M., Valente M., Nitti D.,
Gatta A., Fassina G.;
"Overexpression of squamous cell carcinoma antigen variants in
hepatocellular carcinoma.";
Br. J. Cancer 90:833-837(2004).
[15]
SUBCELLULAR LOCATION.
PubMed=10956412;
DOI=10.1002/1097-0215(20000720)89:4<368::AID-IJC9>3.0.CO;2-6;
Uemura Y., Pak S.C., Luke C., Cataltepe S., Tsu C., Schick C.,
Kamachi Y., Pomeroy S.L., Perlmutter D.H., Silverman G.A.;
"Circulating serpin tumor markers SCCA1 and SCCA2 are not actively
secreted but reside in the cytosol of squamous carcinoma cells.";
Int. J. Cancer 89:368-377(2000).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-390, FUNCTION, INDUCTION,
MUTAGENESIS OF PHE-352, AND INTERACTION WITH MAPK8.
PubMed=19166818; DOI=10.1016/j.bbrc.2009.01.057;
Zheng B., Matoba Y., Kumagai T., Katagiri C., Hibino T., Sugiyama M.;
"Crystal structure of SCCA1 and insight about the interaction with
JNK1.";
Biochem. Biophys. Res. Commun. 380:143-147(2009).
[18]
VARIANT ALA-351.
PubMed=21383048; DOI=10.1258/ebm.2011.010229;
Turato C., Biasiolo A., Pengo P., Frecer V., Quarta S., Fasolato S.,
Ruvoletto M., Beneduce L., Zuin J., Fassina G., Gatta A., Pontisso P.;
"Increased antiprotease activity of the SERPINB3 polymorphic variant
SCCA-PD.";
Exp. Biol. Med. 236:281-290(2011).
-!- FUNCTION: May act as a papain-like cysteine protease inhibitor to
modulate the host immune response against tumor cells. Also
functions as an inhibitor of UV-induced apoptosis via suppression
of the activity of c-Jun NH(2)-terminal kinase (JNK1).
{ECO:0000269|PubMed:19166818}.
-!- SUBUNIT: Interacts with MAPK8/JNK1. {ECO:0000269|PubMed:19166818}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10956412,
ECO:0000269|PubMed:14970861}. Note=Seems to also be secreted in
plasma by cancerous cells but at a low level.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P29508-1; Sequence=Displayed;
Name=2; Synonyms=SCCA1b;
IsoId=P29508-2; Sequence=VSP_032657;
-!- TISSUE SPECIFICITY: Squamous cells. Expressed in some
hepatocellular carcinoma (at protein level).
{ECO:0000269|PubMed:14970861}.
-!- DEVELOPMENTAL STAGE: Its expression is closely related to cellular
differentiation in both normal and malignant squamous cells.
-!- INDUCTION: Strongly up-regulated in the upper epidermis of sun-
exposed skin. {ECO:0000269|PubMed:19166818}.
-!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAO11731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; S66896; AAB20405.1; -; mRNA.
EMBL; U19556; AAA97552.1; -; mRNA.
EMBL; U19568; AAA86317.1; -; Genomic_DNA.
EMBL; U19559; AAA86317.1; JOINED; Genomic_DNA.
EMBL; U19560; AAA86317.1; JOINED; Genomic_DNA.
EMBL; U19562; AAA86317.1; JOINED; Genomic_DNA.
EMBL; U19565; AAA86317.1; JOINED; Genomic_DNA.
EMBL; U19567; AAA86317.1; JOINED; Genomic_DNA.
EMBL; U19562; AAA86316.1; -; Genomic_DNA.
EMBL; U19559; AAA86316.1; JOINED; Genomic_DNA.
EMBL; U19560; AAA86316.1; JOINED; Genomic_DNA.
EMBL; AB046399; BAB40772.1; -; mRNA.
EMBL; AJ515706; CAD56658.1; -; mRNA.
EMBL; AY245778; AAO92269.1; -; mRNA.
EMBL; AY245781; AAO92272.1; -; mRNA.
EMBL; EU852041; ACF21012.1; -; mRNA.
EMBL; BT006748; AAP35394.1; -; mRNA.
EMBL; AK222746; BAD96466.1; -; mRNA.
EMBL; AK222753; BAD96473.1; -; mRNA.
EMBL; AK314805; BAG37332.1; -; mRNA.
EMBL; AC069356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471096; EAW63156.1; -; Genomic_DNA.
EMBL; CH471096; EAW63157.1; -; Genomic_DNA.
EMBL; BC005224; AAH05224.1; -; mRNA.
EMBL; AY190327; AAO11731.1; ALT_INIT; mRNA.
CCDS; CCDS11987.1; -. [P29508-1]
PIR; I38201; I38201.
RefSeq; NP_008850.1; NM_006919.2. [P29508-1]
UniGene; Hs.227948; -.
PDB; 2ZV6; X-ray; 2.70 A; A/B/C=2-390.
PDB; 4ZK0; X-ray; 2.15 A; A=1-390.
PDB; 4ZK3; X-ray; 2.00 A; A=1-390.
PDBsum; 2ZV6; -.
PDBsum; 4ZK0; -.
PDBsum; 4ZK3; -.
ProteinModelPortal; P29508; -.
SMR; P29508; -.
BioGrid; 112223; 52.
IntAct; P29508; 7.
MINT; MINT-1139917; -.
STRING; 9606.ENSP00000283752; -.
DrugBank; DB03929; D-Serine.
DrugBank; DB04522; Phosphonoserine.
MEROPS; I04.008; -.
iPTMnet; P29508; -.
PhosphoSitePlus; P29508; -.
BioMuta; SERPINB3; -.
DMDM; 20141712; -.
SWISS-2DPAGE; P29508; -.
UCD-2DPAGE; P29508; -.
EPD; P29508; -.
MaxQB; P29508; -.
PaxDb; P29508; -.
PeptideAtlas; P29508; -.
PRIDE; P29508; -.
TopDownProteomics; P29508-1; -. [P29508-1]
TopDownProteomics; P29508-2; -. [P29508-2]
DNASU; 6317; -.
Ensembl; ENST00000283752; ENSP00000283752; ENSG00000057149. [P29508-1]
Ensembl; ENST00000332821; ENSP00000329498; ENSG00000057149. [P29508-2]
GeneID; 6317; -.
KEGG; hsa:6317; -.
UCSC; uc002lji.3; human. [P29508-1]
CTD; 6317; -.
DisGeNET; 6317; -.
EuPathDB; HostDB:ENSG00000057149.14; -.
GeneCards; SERPINB3; -.
HGNC; HGNC:10569; SERPINB3.
HPA; CAB018772; -.
HPA; CAB036006; -.
HPA; CAB036007; -.
HPA; HPA048341; -.
HPA; HPA049988; -.
HPA; HPA055992; -.
MIM; 600517; gene.
neXtProt; NX_P29508; -.
OpenTargets; ENSG00000057149; -.
PharmGKB; PA35538; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118789; -.
HOVERGEN; HBG005957; -.
InParanoid; P29508; -.
KO; K13963; -.
OMA; TNAYELK; -.
PhylomeDB; P29508; -.
TreeFam; TF352619; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P29508; -.
GeneWiki; SERPINB3; -.
GenomeRNAi; 6317; -.
PRO; PR:P29508; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000057149; -.
Genevisible; P29508; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IMP:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0001618; F:virus receptor activity; IDA:UniProtKB.
GO; GO:0035425; P:autocrine signaling; IMP:UniProtKB.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IMP:UniProtKB.
GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB.
GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
GO; GO:0045861; P:negative regulation of proteolysis; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0038001; P:paracrine signaling; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0010950; P:positive regulation of endopeptidase activity; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Polymorphism;
Protease inhibitor; Reference proteome; Serine protease inhibitor.
CHAIN 1 390 Serpin B3.
/FTId=PRO_0000094103.
SITE 354 355 Reactive bond.
MOD_RES 1 1 N-acetylmethionine. {ECO:0000269|Ref.13}.
VAR_SEQ 205 256 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_032657.
VARIANT 351 351 G -> A (increased antiprotease activity
and increased MAPK8 inhibition activity;
dbSNP:rs3180227).
{ECO:0000269|PubMed:12975381,
ECO:0000269|PubMed:14970861,
ECO:0000269|PubMed:21383048,
ECO:0000269|Ref.6}.
/FTId=VAR_024351.
VARIANT 357 357 T -> A (in dbSNP:rs1065205).
{ECO:0000269|PubMed:1958219,
ECO:0000269|Ref.3, ECO:0000269|Ref.9}.
/FTId=VAR_024352.
MUTAGEN 341 341 A->R: Loss of inhibitory activity.
{ECO:0000269|PubMed:12975381}.
MUTAGEN 352 352 F->A: Loss of inhibitory activity.
{ECO:0000269|PubMed:12975381,
ECO:0000269|PubMed:19166818}.
MUTAGEN 352 352 F->G: Loss of inhibitory activity to
papain but does not decrease the
suppression activity to MAPK8.
{ECO:0000269|PubMed:12975381,
ECO:0000269|PubMed:19166818}.
MUTAGEN 354 355 SS->PP: Loss of inhibitory activity.
{ECO:0000269|PubMed:12975381}.
CONFLICT 16 16 F -> S (in Ref. 4; CAD56658).
{ECO:0000305}.
CONFLICT 47 47 D -> N (in Ref. 4; CAD56658).
{ECO:0000305}.
CONFLICT 105 105 N -> T (in Ref. 4; CAD56658).
{ECO:0000305}.
CONFLICT 185 185 Q -> R (in Ref. 5; AAO92272).
{ECO:0000305}.
CONFLICT 202 202 P -> S (in Ref. 5; AAO92272).
{ECO:0000305}.
CONFLICT 278 278 T -> A (in Ref. 5; AAO92269).
{ECO:0000305}.
CONFLICT 349 349 V -> E (in Ref. 5; AAO92272).
{ECO:0000305}.
HELIX 4 19 {ECO:0000244|PDB:4ZK3}.
STRAND 27 29 {ECO:0000244|PDB:4ZK3}.
HELIX 31 42 {ECO:0000244|PDB:4ZK3}.
HELIX 47 56 {ECO:0000244|PDB:4ZK3}.
HELIX 59 61 {ECO:0000244|PDB:4ZK3}.
HELIX 81 91 {ECO:0000244|PDB:4ZK3}.
STRAND 97 110 {ECO:0000244|PDB:4ZK3}.
HELIX 117 127 {ECO:0000244|PDB:4ZK3}.
STRAND 130 134 {ECO:0000244|PDB:4ZK3}.
TURN 136 138 {ECO:0000244|PDB:4ZK3}.
HELIX 140 153 {ECO:0000244|PDB:4ZK3}.
TURN 154 157 {ECO:0000244|PDB:4ZK3}.
TURN 165 167 {ECO:0000244|PDB:2ZV6}.
STRAND 174 188 {ECO:0000244|PDB:4ZK3}.
HELIX 192 194 {ECO:0000244|PDB:4ZK3}.
STRAND 196 203 {ECO:0000244|PDB:4ZK3}.
STRAND 206 224 {ECO:0000244|PDB:4ZK3}.
TURN 225 228 {ECO:0000244|PDB:4ZK3}.
STRAND 229 236 {ECO:0000244|PDB:4ZK3}.
STRAND 239 250 {ECO:0000244|PDB:4ZK3}.
TURN 251 253 {ECO:0000244|PDB:4ZK3}.
HELIX 254 260 {ECO:0000244|PDB:4ZK3}.
HELIX 263 269 {ECO:0000244|PDB:4ZK3}.
HELIX 272 274 {ECO:0000244|PDB:4ZK3}.
STRAND 276 285 {ECO:0000244|PDB:4ZK3}.
STRAND 287 294 {ECO:0000244|PDB:4ZK3}.
HELIX 296 302 {ECO:0000244|PDB:4ZK3}.
HELIX 306 308 {ECO:0000244|PDB:4ZK3}.
HELIX 315 318 {ECO:0000244|PDB:4ZK3}.
STRAND 319 321 {ECO:0000244|PDB:4ZK3}.
STRAND 324 336 {ECO:0000244|PDB:4ZK3}.
STRAND 338 352 {ECO:0000244|PDB:4ZK3}.
STRAND 361 364 {ECO:0000244|PDB:4ZK3}.
STRAND 369 375 {ECO:0000244|PDB:4ZK3}.
TURN 376 379 {ECO:0000244|PDB:4ZK3}.
STRAND 380 387 {ECO:0000244|PDB:4ZK3}.
SEQUENCE 390 AA; 44565 MW; E5F27F986C752CFA CRC64;
MNSLSEANTK FMFDLFQQFR KSKENNIFYS PISITSALGM VLLGAKDNTA QQIKKVLHFD
QVTENTTGKA ATYHVDRSGN VHHQFQKLLT EFNKSTDAYE LKIANKLFGE KTYLFLQEYL
DAIKKFYQTS VESVDFANAP EESRKKINSW VESQTNEKIK NLIPEGNIGS NTTLVLVNAI
YFKGQWEKKF NKEDTKEEKF WPNKNTYKSI QMMRQYTSFH FASLEDVQAK VLEIPYKGKD
LSMIVLLPNE IDGLQKLEEK LTAEKLMEWT SLQNMRETRV DLHLPRFKVE ESYDLKDTLR
TMGMVDIFNG DADLSGMTGS RGLVLSGVLH KAFVEVTEEG AEAAAATAVV GFGSSPTSTN
EEFHCNHPFL FFIRQNKTNS ILFYGRFSSP


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