LANC2_HUMAN
ID LANC2_HUMAN Reviewed; 450 AA.
AC Q9NS86; B2R8D4; Q6NSL4; Q8TCQ3; Q9BSR1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=LanC-like protein 2;
DE AltName: Full=Testis-specific adriamycin sensitivity protein;
GN Name=LANCL2; Synonyms=GPR69B, TASP;
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], AND TISSUE SPECIFICITY.
RX PubMed=11762191; DOI=10.3109/10425170109080770;
RA Mayer H., Pongratz M., Prohaska R.;
RT "Molecular cloning, characterization, and tissue-specific expression of
RT human LANCL2, a novel member of the LanC-like protein family.";
RL DNA Seq. 12:161-166(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sugimoto Y., Tsukahara S., Ishikawa E., Tsuruo T.;
RT "Isolation and identification of genes whose downregulation result in
RT anticancer drug resistance.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Eley G.D., Wang X.-Y., Frederick L., Hebrink D., Nash C., James C.D.;
RT "2 MB physical and transcript map of the 7p11.2 locus surrounding EGFR
RT frequently amplified in glioblastoma multiforme.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-56.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-56.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-56.
RC TISSUE=Ovary;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-450.
RC TISSUE=Testis;
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 [10]
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, AND
RP INTERACTION WITH INOSITOL PHOSPHOLIPIDS.
RX PubMed=16979580; DOI=10.1016/j.bbamem.2006.07.018;
RA Landlinger C., Salzer U., Prohaska R.;
RT "Myristoylation of human LanC-like protein 2 (LANCL2) is essential for the
RT interaction with the plasma membrane and the increase in cellular
RT sensitivity to adriamycin.";
RL Biochim. Biophys. Acta 1758:1759-1767(2006).
RN [11]
RP SUBCELLULAR LOCATION, AND POSSIBLE FUNCTION IN CELLULAR SENSITIVITY TO
RP ADRIAMYCIN.
RX PubMed=12566319;
RA Park S., James C.D.;
RT "Lanthionine synthetase components C-like 2 increases cellular sensitivity
RT to adriamycin by decreasing the expression of P-glycoprotein through a
RT transcription-mediated mechanism.";
RL Cancer Res. 63:723-727(2003).
RN [12]
RP FUNCTION.
RX PubMed=19667068; DOI=10.1074/jbc.m109.035329;
RA Sturla L., Fresia C., Guida L., Bruzzone S., Scarfi' S., Usai C.,
RA Fruscione F., Magnone M., Millo E., Basile G., Grozio A., Jacchetti E.,
RA Allegretti M., De Flora A., Zocchi E.;
RT "LANCL2 is necessary for abscisic acid binding and signaling in human
RT granulocytes and in rat insulinoma cells.";
RL J. Biol. Chem. 284:28045-28057(2009).
RN [13]
RP IDENTIFICATION BY MASS 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).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Necessary for abscisic acid (ABA) binding on the cell
CC membrane and activation of the ABA signaling pathway in granulocytes.
CC {ECO:0000269|PubMed:19667068}.
CC -!- SUBUNIT: Interacts with an array of inositol phospholipids such as
CC phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-
CC phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P). PIP-
CC binding enhances membrane association. {ECO:0000269|PubMed:16979580}.
CC -!- INTERACTION:
CC Q9NS86; Q92624: APPBP2; NbExp=6; IntAct=EBI-2510837, EBI-743771;
CC Q9NS86; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-2510837, EBI-11522811;
CC Q9NS86; Q9Y2W6: TDRKH; NbExp=3; IntAct=EBI-2510837, EBI-12842466;
CC Q9NS86; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2510837, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12566319}. Cytoplasm
CC {ECO:0000269|PubMed:12566319}. Cell membrane
CC {ECO:0000269|PubMed:12566319, ECO:0000269|PubMed:16979580}.
CC Note=Localizes to the juxta-nuclear vesicles (PubMed:16979580).
CC Associates with the cortical actin cytoskeleton (PubMed:16979580).
CC Cholesterol depletion by methyl-beta-cyclodextrin causes partial
CC dissociation from the cell membrane in vitro and an enhanced cell
CC detachment from the matrix in vivo (PubMed:16979580). Membrane-
CC association is important for the increased cellular sensitivity to an
CC anticancer drug (adriamycin) (PubMed:16979580).
CC {ECO:0000269|PubMed:16979580}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC {ECO:0000269|PubMed:11762191}.
CC -!- PTM: Myristoylated. Essential for membrane association.
CC {ECO:0000269|PubMed:16979580}.
CC -!- MISCELLANEOUS: Its exogenous expression in a sarcoma cell line
CC decreases the expression of ABCB1 (P-glycoprotein 1) and increases
CC cellular sensitivity to an anticancer drug (adriamycin).
CC -!- SIMILARITY: Belongs to the LanC-like protein family. {ECO:0000305}.
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DR EMBL; AJ278245; CAC21715.1; -; mRNA.
DR EMBL; AB035966; BAA96800.1; -; mRNA.
DR EMBL; AF353942; AAK83286.1; -; mRNA.
DR EMBL; AK313326; BAG36131.1; -; mRNA.
DR EMBL; AC073347; AAQ93360.1; -; Genomic_DNA.
DR EMBL; CH236957; EAL23810.1; -; Genomic_DNA.
DR EMBL; CH471201; EAW50968.1; -; Genomic_DNA.
DR EMBL; BC004887; AAH04887.2; -; mRNA.
DR EMBL; BC070049; AAH70049.1; -; mRNA.
DR EMBL; AL713665; CAD28471.1; -; mRNA.
DR CCDS; CCDS5517.1; -.
DR RefSeq; NP_061167.1; NM_018697.3.
DR PDB; 6WQ1; X-ray; 2.29 A; A/B/C/D=1-450.
DR PDBsum; 6WQ1; -.
DR AlphaFoldDB; Q9NS86; -.
DR SMR; Q9NS86; -.
DR BioGRID; 120998; 67.
DR IntAct; Q9NS86; 18.
DR MINT; Q9NS86; -.
DR STRING; 9606.ENSP00000254770; -.
DR BindingDB; Q9NS86; -.
DR ChEMBL; CHEMBL3351212; -.
DR GuidetoPHARMACOLOGY; 3082; -.
DR GlyGen; Q9NS86; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NS86; -.
DR MetOSite; Q9NS86; -.
DR PhosphoSitePlus; Q9NS86; -.
DR BioMuta; LANCL2; -.
DR DMDM; 47116933; -.
DR CPTAC; CPTAC-532; -.
DR CPTAC; CPTAC-533; -.
DR EPD; Q9NS86; -.
DR jPOST; Q9NS86; -.
DR MassIVE; Q9NS86; -.
DR MaxQB; Q9NS86; -.
DR PaxDb; Q9NS86; -.
DR PeptideAtlas; Q9NS86; -.
DR PRIDE; Q9NS86; -.
DR ProteomicsDB; 82510; -.
DR Antibodypedia; 13819; 224 antibodies from 21 providers.
DR DNASU; 55915; -.
DR Ensembl; ENST00000254770.3; ENSP00000254770.2; ENSG00000132434.10.
DR GeneID; 55915; -.
DR KEGG; hsa:55915; -.
DR MANE-Select; ENST00000254770.3; ENSP00000254770.2; NM_018697.4; NP_061167.1.
DR UCSC; uc003tqp.3; human.
DR CTD; 55915; -.
DR DisGeNET; 55915; -.
DR GeneCards; LANCL2; -.
DR HGNC; HGNC:6509; LANCL2.
DR HPA; ENSG00000132434; Low tissue specificity.
DR MIM; 612919; gene.
DR neXtProt; NX_Q9NS86; -.
DR OpenTargets; ENSG00000132434; -.
DR PharmGKB; PA30294; -.
DR VEuPathDB; HostDB:ENSG00000132434; -.
DR eggNOG; KOG2787; Eukaryota.
DR GeneTree; ENSGT00530000063186; -.
DR HOGENOM; CLU_036244_0_0_1; -.
DR InParanoid; Q9NS86; -.
DR OMA; MAGTIHF; -.
DR OrthoDB; 681208at2759; -.
DR PhylomeDB; Q9NS86; -.
DR TreeFam; TF300068; -.
DR PathwayCommons; Q9NS86; -.
DR SignaLink; Q9NS86; -.
DR BioGRID-ORCS; 55915; 10 hits in 1083 CRISPR screens.
DR ChiTaRS; LANCL2; human.
DR GeneWiki; LANCL2; -.
DR GenomeRNAi; 55915; -.
DR Pharos; Q9NS86; Tchem.
DR PRO; PR:Q9NS86; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NS86; protein.
DR Bgee; ENSG00000132434; Expressed in middle temporal gyrus and 175 other tissues.
DR ExpressionAtlas; Q9NS86; baseline and differential.
DR Genevisible; Q9NS86; HS.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR020464; LanC-like_prot_euk.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01951; LANCEUKARYTE.
DR PRINTS; PR01950; LANCSUPER.
DR SMART; SM01260; LANC_like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Lipoprotein; Membrane; Myristate;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..450
FT /note="LanC-like protein 2"
FT /id="PRO_0000191272"
FT REGION 2..15
FT /note="Interaction with inositol phospholipids"
FT MOD_RES 198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJK2"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:16979580"
FT VARIANT 56
FT /note="T -> P (in dbSNP:rs2272263)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.7"
FT /id="VAR_060064"
FT VARIANT 74
FT /note="I -> V (in dbSNP:rs6961412)"
FT /id="VAR_053480"
FT MUTAGEN 2
FT /note="G->A: Loss of membrane localization and results in
FT localization to the nucleus, particularly to the nucleoli."
FT /evidence="ECO:0000269|PubMed:16979580"
FT HELIX 71..92
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:6WQ1"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 221..241
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:6WQ1"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:6WQ1"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:6WQ1"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 370..384
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 387..401
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:6WQ1"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:6WQ1"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:6WQ1"
SQ SEQUENCE 450 AA; 50854 MW; 8FD27E11BB91C05D CRC64;
MGETMSKRLK LHLGGEAEME ERAFVNPFPD YEAAAGALLA SGAAEETGCV RPPATTDEPG
LPFHQDGKII HNFIRRIQTK IKDLLQQMEE GLKTADPHDC SAYTGWTGIA LLYLQLYRVT
CDQTYLLRSL DYVKRTLRNL NGRRVTFLCG DAGPLAVGAV IYHKLRSDCE SQECVTKLLQ
LQRSVVCQES DLPDELLYGR AGYLYALLYL NTEIGPGTVC ESAIKEVVNA IIESGKTLSR
EERKTERCPL LYQWHRKQYV GAAHGMAGIY YMLMQPAAKV DQETLTEMVK PSIDYVRHKK
FRSGNYPSSL SNETDRLVHW CHGAPGVIHM LMQAYKVFKE EKYLKEAMEC SDVIWQRGLL
RKGYGICHGT AGNGYSFLSL YRLTQDKKYL YRACKFAEWC LDYGAHGCRI PDRPYSLFEG
MAGAIHFLSD VLGPETSRFP AFELDSSKRD
