ID   SPB5_HUMAN              Reviewed;         375 AA.
AC   P36952; B2R6Y4; Q6N0B4; Q8WW89;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   28-JUN-2023, entry version 197.
DE   RecName: Full=Serpin B5;
DE   AltName: Full=Maspin;
DE   AltName: Full=Peptidase inhibitor 5;
DE            Short=PI-5;
GN   Name=SERPINB5; Synonyms=PI5;
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), AND VARIANTS PRO-176 AND LEU-187.
RC   TISSUE=Mammary gland;
RX   PubMed=8290962; DOI=10.1126/science.8290962;
RA   Zou Z., Anisowicz A., Hendrix M.J.C., Thor A., Neveu M., Sheng S.,
RA   Rafidi K., Seftor E., Sager R.;
RT   "Maspin, a serpin with tumor-suppressing activity in human mammary
RT   epithelial cells.";
RL   Science 263:526-529(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-176.
RC   TISSUE=Esophagus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-176.
RC   TISSUE=Prostate;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-375 (ISOFORM 1), AND VARIANT
RP   VAL-319.
RC   TISSUE=Small intestine;
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   [6]
RP   PROTEIN SEQUENCE OF 341-360, AND CHARACTERIZATION.
RX   PubMed=7797587; DOI=10.1074/jbc.270.26.15832;
RA   Pemberton P.A., Wong D.T., Gibson H.L., Kiefer M.C., Fitzpatrick P.A.,
RA   Sager R., Barr P.J.;
RT   "The tumor suppressor maspin does not undergo the stressed to relaxed
RT   transition or inhibit trypsin-like serine proteases. Evidence that maspin
RT   is not a protease inhibitory serpin.";
RL   J. Biol. Chem. 270:15832-15837(1995).
RN   [7]
RP   INTERACTION WITH IRF6.
RX   PubMed=16049006; DOI=10.1074/jbc.m503523200;
RA   Bailey C.M., Khalkhali-Ellis Z., Kondo S., Margaryan N.V., Seftor R.E.B.,
RA   Wheaton W.W., Amir S., Pins M.R., Schutte B.C., Hendrix M.J.C.;
RT   "Mammary serine protease inhibitor (Maspin) binds directly to interferon
RT   regulatory factor 6: identification of a novel serpin partnership.";
RL   J. Biol. Chem. 280:34210-34217(2005).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=15760906; DOI=10.1074/jbc.m412043200;
RA   Law R.H., Irving J.A., Buckle A.M., Ruzyla K., Buzza M.,
RA   Bashtannyk-Puhalovich T.A., Beddoe T.C., Nguyen K., Worrall D.M.,
RA   Bottomley S.P., Bird P.I., Rossjohn J., Whisstock J.C.;
RT   "The high resolution crystal structure of the human tumor suppressor maspin
RT   reveals a novel conformational switch in the G-helix.";
RL   J. Biol. Chem. 280:22356-22364(2005).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] PRO-176, AND IDENTIFICATION BY MASS
RP   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).
CC   -!- FUNCTION: Tumor suppressor. It blocks the growth, invasion, and
CC       metastatic properties of mammary tumors. As it does not undergo the S
CC       (stressed) to R (relaxed) conformational transition characteristic of
CC       active serpins, it exhibits no serine protease inhibitory activity.
CC   -!- SUBUNIT: Interacts with IRF6. {ECO:0000269|PubMed:16049006}.
CC   -!- INTERACTION:
CC       P36952; Q9Y6M0: PRSS21; NbExp=7; IntAct=EBI-2371394, EBI-7054564;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P36952-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P36952-2; Sequence=VSP_037145, VSP_037146;
CC   -!- TISSUE SPECIFICITY: Normal mammary epithelial cells.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42267/SerpinB5";
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DR   EMBL; U04313; AAA18957.1; -; mRNA.
DR   EMBL; AK312765; BAG35631.1; -; mRNA.
DR   EMBL; AC036176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020713; AAH20713.1; -; mRNA.
DR   EMBL; BX640597; CAE45703.1; -; mRNA.
DR   CCDS; CCDS32839.1; -. [P36952-1]
DR   PIR; A36898; A36898.
DR   RefSeq; NP_002630.2; NM_002639.4. [P36952-1]
DR   PDB; 1WZ9; X-ray; 2.10 A; A/B=1-375.
DR   PDB; 1XQG; X-ray; 3.10 A; A/B=1-375.
DR   PDB; 1XQJ; X-ray; 3.10 A; A=1-375.
DR   PDB; 1XU8; X-ray; 2.80 A; A/B=1-375.
DR   PDBsum; 1WZ9; -.
DR   PDBsum; 1XQG; -.
DR   PDBsum; 1XQJ; -.
DR   PDBsum; 1XU8; -.
DR   AlphaFoldDB; P36952; -.
DR   SMR; P36952; -.
DR   BioGRID; 111286; 164.
DR   IntAct; P36952; 54.
DR   MINT; P36952; -.
DR   STRING; 9606.ENSP00000372221; -.
DR   DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine.
DR   MEROPS; I04.980; -.
DR   GlyCosmos; P36952; 4 sites, No reported glycans.
DR   GlyGen; P36952; 5 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P36952; -.
DR   MetOSite; P36952; -.
DR   PhosphoSitePlus; P36952; -.
DR   SwissPalm; P36952; -.
DR   BioMuta; SERPINB5; -.
DR   DMDM; 229462757; -.
DR   CPTAC; CPTAC-582; -.
DR   CPTAC; CPTAC-583; -.
DR   EPD; P36952; -.
DR   jPOST; P36952; -.
DR   MassIVE; P36952; -.
DR   MaxQB; P36952; -.
DR   PaxDb; P36952; -.
DR   PeptideAtlas; P36952; -.
DR   PRIDE; P36952; -.
DR   ProteomicsDB; 55240; -. [P36952-1]
DR   ProteomicsDB; 55241; -. [P36952-2]
DR   TopDownProteomics; P36952-1; -. [P36952-1]
DR   Antibodypedia; 4036; 620 antibodies from 43 providers.
DR   DNASU; 5268; -.
DR   Ensembl; ENST00000382771.9; ENSP00000372221.4; ENSG00000206075.14. [P36952-1]
DR   Ensembl; ENST00000489441.5; ENSP00000467158.1; ENSG00000206075.14. [P36952-2]
DR   GeneID; 5268; -.
DR   KEGG; hsa:5268; -.
DR   MANE-Select; ENST00000382771.9; ENSP00000372221.4; NM_002639.5; NP_002630.2.
DR   UCSC; uc002liy.3; human. [P36952-1]
DR   AGR; HGNC:8949; -.
DR   CTD; 5268; -.
DR   DisGeNET; 5268; -.
DR   GeneCards; SERPINB5; -.
DR   HGNC; HGNC:8949; SERPINB5.
DR   HPA; ENSG00000206075; Tissue enhanced (esophagus, skin).
DR   MIM; 154790; gene.
DR   neXtProt; NX_P36952; -.
DR   OpenTargets; ENSG00000206075; -.
DR   PharmGKB; PA35515; -.
DR   VEuPathDB; HostDB:ENSG00000206075; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000160674; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; P36952; -.
DR   OMA; IFAPLCT; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; P36952; -.
DR   TreeFam; TF352619; -.
DR   PathwayCommons; P36952; -.
DR   SignaLink; P36952; -.
DR   SIGNOR; P36952; -.
DR   BioGRID-ORCS; 5268; 8 hits in 1153 CRISPR screens.
DR   ChiTaRS; SERPINB5; human.
DR   EvolutionaryTrace; P36952; -.
DR   GeneWiki; Maspin; -.
DR   GenomeRNAi; 5268; -.
DR   Pharos; P36952; Tbio.
DR   PRO; PR:P36952; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P36952; protein.
DR   Bgee; ENSG00000206075; Expressed in skin of abdomen and 95 other tissues.
DR   ExpressionAtlas; P36952; baseline and differential.
DR   Genevisible; P36952; HS.
DR   GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0060512; P:prostate gland morphogenesis; IEA:Ensembl.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR   CDD; cd02057; serpinB5_maspin; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR   InterPro; IPR000240; Serpin_B9/Maspin.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   InterPro; IPR033836; SERPINB5_serpin_dom.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF55; SERPIN B5; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00676; MASPIN.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Glycoprotein; Reference proteome; Secreted.
FT   CHAIN           1..375
FT                   /note="Serpin B5"
FT                   /id="PRO_0000032486"
FT   SITE            340..341
FT                   /note="Reactive bond homolog"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         190..231
FT                   /note="TDTKPVQMMNMEATFCMGNIDSINCKIIELPFQNKHLSMFIL -> VCGAAC
FT                   SSKRSPIIDVKNDRDRVGHKSIPMRNLRARPAKCLS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037145"
FT   VAR_SEQ         232..375
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037146"
FT   VARIANT         176
FT                   /note="S -> P (in dbSNP:rs2289519)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8290962,
FT                   ECO:0007744|PubMed:21269460"
FT                   /id="VAR_055223"
FT   VARIANT         187
FT                   /note="V -> L (in dbSNP:rs2289520)"
FT                   /evidence="ECO:0000269|PubMed:8290962"
FT                   /id="VAR_055224"
FT   VARIANT         319
FT                   /note="I -> V (in dbSNP:rs1455555)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_022115"
FT   CONFLICT        66
FT                   /note="V -> I (in Ref. 1; AAA18957)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="K -> Q (in Ref. 5; CAE45703)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2..22
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1XQG"
FT   HELIX           32..45
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           48..57
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:1XQG"
FT   HELIX           66..80
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          84..95
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           102..108
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            109..115
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           125..139
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            147..150
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          159..168
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          181..190
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          192..209
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            210..213
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          214..221
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           222..224
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          225..235
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           239..249
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           252..258
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          265..274
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          276..282
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            295..297
FT                   /evidence="ECO:0007829|PDB:1XU8"
FT   TURN            299..301
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            305..307
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          315..326
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            337..341
FT                   /evidence="ECO:0007829|PDB:1XQG"
FT   STRAND          344..349
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          354..360
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   TURN            361..364
FT                   /evidence="ECO:0007829|PDB:1WZ9"
FT   STRAND          365..372
FT                   /evidence="ECO:0007829|PDB:1WZ9"
SQ   SEQUENCE   375 AA;  42100 MW;  9F24E18505912804 CRC64;
     MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF
     ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD
     FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKIL VVNAAYFVGK WMKKFSESET
     KECPFRVNKT DTKPVQMMNM EATFCMGNID SINCKIIELP FQNKHLSMFI LLPKDVEDES
     TGLEKIEKQL NSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED
     TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFIYIIRH
     NKTRNIIFFG KFCSP
//
