CSN6_HUMAN
ID CSN6_HUMAN Reviewed; 327 AA.
AC Q7L5N1; A4D2A3; O15387;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=COP9 signalosome complex subunit 6;
DE Short=SGN6;
DE Short=Signalosome subunit 6;
DE AltName: Full=JAB1-containing signalosome subunit 6;
DE AltName: Full=MOV34 homolog;
DE AltName: Full=Vpr-interacting protein;
DE Short=hVIP;
GN Name=COPS6; Synonyms=CSN6, HVIP;
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 [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 [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-327.
RX PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
RA Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
RA Hinnebusch A.G., Hershey J.W.B.;
RT "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits.
RT Possible roles in RNA binding and macromolecular assembly.";
RL J. Biol. Chem. 272:27042-27052(1997).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9535219; DOI=10.1096/fasebj.12.6.469;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R.,
RA Gordon C., Naumann M., Dubiel W.;
RT "A novel protein complex involved in signal transduction possessing
RT similarities to 26S proteasome subunits.";
RL FASEB J. 12:469-478(1998).
RN [6]
RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION).
RX PubMed=8195203; DOI=10.1016/s0021-9258(17)40719-8;
RA Zhao L.-J., Mukherjee S., Narayan O.;
RT "Biochemical mechanism of HIV-I Vpr function. Specific interaction with a
RT cellular protein.";
RL J. Biol. Chem. 269:15577-15582(1994).
RN [7]
RP SUBCELLULAR LOCATION (MICROBIAL INFECTION), TISSUE SPECIFICITY, AND
RP INTERACTION WITH HUMAN VPR (MICROBIAL INFECTION).
RX PubMed=9520381; DOI=10.1073/pnas.95.7.3419;
RA Mahalingam S., Ayyavoo V., Patel M., Kieber-Emmons T., Kao G.D.,
RA Muschel R.J., Weiner D.B.;
RT "HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor
RT linked to the G2/M phase transition of the mammalian cell cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3419-3424(1998).
RN [8]
RP FUNCTION.
RX PubMed=11285227; DOI=10.1093/emboj/20.7.1630;
RA Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C.,
RA Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation by
RT the ubiquitin system.";
RL EMBO J. 20:1630-1639(2001).
RN [9]
RP FUNCTION, COMPOSITION OF THE CSN COMPLEX, AND INTERACTION WITH RBX1.
RX PubMed=11337588; DOI=10.1126/science.1059780;
RA Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
RA Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
RT "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
RL Science 292:1382-1385(2001).
RN [10]
RP INTERACTION WITH EIF3S6.
RX PubMed=12220626; DOI=10.1016/s0014-5793(02)03147-2;
RA Hoareau Alves K., Bochard V., Rety S., Jalinot P.;
RT "Association of the mammalian proto-oncoprotein Int-6 with the three
RT protein complexes eIF3, COP9 signalosome and 26S proteasome.";
RL FEBS Lett. 527:15-21(2002).
RN [11]
RP INTERACTION WITH VPR (MICROBIAL INFECTION).
RX PubMed=12237292; DOI=10.1074/jbc.m203905200;
RA Ramanathan M.P., Curley E. III, Su M., Chambers J.A., Weiner D.B.;
RT "Carboxyl terminus of hVIP/mov34 is critical for HIV-1-Vpr interaction and
RT glucocorticoid-mediated signaling.";
RL J. Biol. Chem. 277:47854-47860(2002).
RN [12]
RP FUNCTION.
RX PubMed=12732143; DOI=10.1016/s0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R.,
RA Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [13]
RP FUNCTION.
RX PubMed=12628923; DOI=10.1093/emboj/cdg127;
RA Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D.,
RA Huang X., Berse M., Sperling J., Schade R., Dubiel W.;
RT "Protein kinase CK2 and protein kinase D are associated with the COP9
RT signalosome.";
RL EMBO J. 22:1302-1312(2003).
RN [14]
RP IDENTIFICATION IN THE CSN COMPLEX.
RX PubMed=18850735; DOI=10.1021/pr800574c;
RA Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
RT "Characterization of the human COP9 signalosome complex using affinity
RT purification and mass spectrometry.";
RL J. Proteome Res. 7:4914-4925(2008).
RN [15]
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 [16]
RP FUNCTION, AND INTERACTION WITH COP1 AND SFN.
RX PubMed=21625211; DOI=10.1038/onc.2011.192;
RA Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C., Tseng C.,
RA Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.;
RT "COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3
RT ubiquitin ligase for 14-3-3sigma.";
RL Oncogene 30:4791-4801(2011).
RN [17]
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).
RN [18]
RP COMPOSITION OF THE CSN COMPLEX, AND INTERACTION WITH COPS9.
RX PubMed=26456823; DOI=10.1016/j.celrep.2015.09.021;
RA Rozen S., Fuezesi-Levi M.G., Ben-Nissan G., Mizrachi L., Gabashvili A.,
RA Levin Y., Ben-Dor S., Eisenstein M., Sharon M.;
RT "CSNAP is a stoichiometric subunit of the COP9 signalosome.";
RL Cell Rep. 13:585-598(2015).
RN [19]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes. The CSN
CC complex is an essential regulator of the ubiquitin (Ubl) conjugation
CC pathway by mediating the deneddylation of the cullin subunits of SCF-
CC type E3 ligase complexes, leading to decrease the Ubl ligase activity
CC of SCF-type complexes such as SCF, CSA or DDB2. The complex is also
CC involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with
CC CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively. Has
CC some glucocorticoid receptor-responsive activity. Stabilizes COP1
CC through reducing COP1 auto-ubiquitination and decelerating COP1
CC turnover rate, hence regulates the ubiquitination of COP1 targets.
CC {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143,
CC ECO:0000269|PubMed:21625211, ECO:0000269|PubMed:9535219}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9
CC isoform 1 (PubMed:18850735, PubMed:26456823). In the complex, it
CC probably interacts directly with COPS2, COPS4, COPS5, COPS7 (COPS7A or
CC COPS7B) and COPS9 isoform 1 (PubMed:11337588, PubMed:26456823).
CC Interacts with the translation initiation factor EIF3S6
CC (PubMed:12220626). Interacts weakly with RBX1 (PubMed:11337588).
CC Directly interacts with COP1 and 14-3-3 protein sigma/SFN
CC (PubMed:21625211). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12220626,
CC ECO:0000269|PubMed:18850735, ECO:0000269|PubMed:21625211,
CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:26456823}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the HIV-1 protein Vpr.
CC {ECO:0000269|PubMed:12237292, ECO:0000269|PubMed:8195203,
CC ECO:0000269|PubMed:9520381}.
CC -!- INTERACTION:
CC Q7L5N1; Q13515: BFSP2; NbExp=3; IntAct=EBI-486838, EBI-10229433;
CC Q7L5N1; Q9BX70: BTBD2; NbExp=7; IntAct=EBI-486838, EBI-710091;
CC Q7L5N1; Q9Y297: BTRC; NbExp=2; IntAct=EBI-486838, EBI-307461;
CC Q7L5N1; Q6UXH8-3: CCBE1; NbExp=3; IntAct=EBI-486838, EBI-12013534;
CC Q7L5N1; Q8NHY2: COP1; NbExp=3; IntAct=EBI-486838, EBI-1176214;
CC Q7L5N1; Q9UNS2: COPS3; NbExp=23; IntAct=EBI-486838, EBI-350590;
CC Q7L5N1; Q9BT78: COPS4; NbExp=18; IntAct=EBI-486838, EBI-742413;
CC Q7L5N1; Q92905: COPS5; NbExp=24; IntAct=EBI-486838, EBI-594661;
CC Q7L5N1; P28482: MAPK1; NbExp=2; IntAct=EBI-486838, EBI-959949;
CC Q7L5N1; P31947: SFN; NbExp=7; IntAct=EBI-486838, EBI-476295;
CC Q7L5N1; Q92529: SHC3; NbExp=3; IntAct=EBI-486838, EBI-79084;
CC Q7L5N1; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-486838, EBI-739895;
CC Q7L5N1; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-486838, EBI-10237226;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9535219}. Cytoplasm
CC {ECO:0000269|PubMed:9535219}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:9520381}. Note=(Microbial infection) The
CC interaction with HIV-1 Vpr protein possibly leads its translocation to
CC a perinuclear region. {ECO:0000269|PubMed:9520381}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9520381}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN6 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M67A family, it lacks the
CC JAMM motif that probably constitutes the catalytic center and therefore
CC it probably does not have a protease activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; CH236956; EAL23857.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76601.1; -; Genomic_DNA.
DR EMBL; BC002520; AAH02520.2; -; mRNA.
DR EMBL; U70735; AAD03469.1; ALT_INIT; mRNA.
DR CCDS; CCDS5682.1; -.
DR RefSeq; NP_006824.2; NM_006833.4.
DR PDB; 4D10; X-ray; 3.80 A; F/N=1-327.
DR PDB; 4D18; X-ray; 4.08 A; F/N=1-327.
DR PDB; 4QFT; X-ray; 1.76 A; A=31-211.
DR PDB; 4R14; X-ray; 2.60 A; A/B=38-210.
DR PDB; 4WSN; X-ray; 5.50 A; F/N/V/d/l/t=1-327.
DR PDB; 6R6H; EM; 8.40 A; F=20-327.
DR PDB; 6R7F; EM; 8.20 A; F=29-316.
DR PDB; 6R7H; EM; 8.80 A; F=29-316.
DR PDB; 6R7I; EM; 5.90 A; F=1-327.
DR PDBsum; 4D10; -.
DR PDBsum; 4D18; -.
DR PDBsum; 4QFT; -.
DR PDBsum; 4R14; -.
DR PDBsum; 4WSN; -.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
DR PDBsum; 6R7I; -.
DR AlphaFoldDB; Q7L5N1; -.
DR SMR; Q7L5N1; -.
DR BioGRID; 116176; 369.
DR ComplexPortal; CPX-1870; COP9 signalosome variant 1.
DR ComplexPortal; CPX-1871; COP9 signalosome variant 2.
DR CORUM; Q7L5N1; -.
DR DIP; DIP-32655N; -.
DR IntAct; Q7L5N1; 305.
DR MINT; Q7L5N1; -.
DR STRING; 9606.ENSP00000304102; -.
DR MEROPS; M67.972; -.
DR GlyGen; Q7L5N1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L5N1; -.
DR PhosphoSitePlus; Q7L5N1; -.
DR BioMuta; COPS6; -.
DR DMDM; 55976470; -.
DR EPD; Q7L5N1; -.
DR jPOST; Q7L5N1; -.
DR MassIVE; Q7L5N1; -.
DR MaxQB; Q7L5N1; -.
DR PaxDb; Q7L5N1; -.
DR PeptideAtlas; Q7L5N1; -.
DR PRIDE; Q7L5N1; -.
DR ProteomicsDB; 68811; -.
DR Antibodypedia; 30510; 218 antibodies from 25 providers.
DR DNASU; 10980; -.
DR Ensembl; ENST00000303904.8; ENSP00000304102.3; ENSG00000168090.10.
DR GeneID; 10980; -.
DR KEGG; hsa:10980; -.
DR MANE-Select; ENST00000303904.8; ENSP00000304102.3; NM_006833.5; NP_006824.2.
DR UCSC; uc003usu.4; human.
DR CTD; 10980; -.
DR DisGeNET; 10980; -.
DR GeneCards; COPS6; -.
DR HGNC; HGNC:21749; COPS6.
DR HPA; ENSG00000168090; Low tissue specificity.
DR MIM; 614729; gene.
DR neXtProt; NX_Q7L5N1; -.
DR OpenTargets; ENSG00000168090; -.
DR PharmGKB; PA134919933; -.
DR VEuPathDB; HostDB:ENSG00000168090; -.
DR eggNOG; KOG3050; Eukaryota.
DR GeneTree; ENSGT00950000183073; -.
DR HOGENOM; CLU_027018_1_2_1; -.
DR InParanoid; Q7L5N1; -.
DR OMA; DLVGWYT; -.
DR OrthoDB; 1455324at2759; -.
DR PhylomeDB; Q7L5N1; -.
DR TreeFam; TF101148; -.
DR PathwayCommons; Q7L5N1; -.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q7L5N1; -.
DR SIGNOR; Q7L5N1; -.
DR BioGRID-ORCS; 10980; 740 hits in 1097 CRISPR screens.
DR ChiTaRS; COPS6; human.
DR GeneWiki; COPS6; -.
DR GenomeRNAi; 10980; -.
DR Pharos; Q7L5N1; Tbio.
DR PRO; PR:Q7L5N1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7L5N1; protein.
DR Bgee; ENSG00000168090; Expressed in stromal cell of endometrium and 207 other tissues.
DR ExpressionAtlas; Q7L5N1; baseline and differential.
DR Genevisible; Q7L5N1; HS.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR CDD; cd08063; MPN_CSN6; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033859; MPN_CSN6.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Host-virus interaction;
KW Nucleus; Reference proteome; Signalosome.
FT CHAIN 1..327
FT /note="COP9 signalosome complex subunit 6"
FT /id="PRO_0000194860"
FT DOMAIN 41..174
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 211..327
FT /note="Interaction with Vpr"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4QFT"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:4QFT"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:4QFT"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4QFT"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4QFT"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4QFT"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:4QFT"
FT STRAND 120..130
FT /evidence="ECO:0007829|PDB:4QFT"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:4QFT"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4QFT"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4QFT"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:4QFT"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4R14"
FT STRAND 165..186
FT /evidence="ECO:0007829|PDB:4QFT"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:4QFT"
SQ SEQUENCE 327 AA; 36163 MW; E33CAC6ADF799A8D CRC64;
MAAAAAAAAA TNGTGGSSGM EVDAAVVPSV MACGVTGSVS VALHPLVILN ISDHWIRMRS
QEGRPVQVIG ALIGKQEGRN IEVMNSFELL SHTVEEKIII DKEYYYTKEE QFKQVFKELE
FLGWYTTGGP PDPSDIHVHK QVCEIIESPL FLKLNPMTKH TDLPVSVFES VIDIINGEAT
MLFAELTYTL ATEEAERIGV DHVARMTATG SGENSTVAEH LIAQHSAIKM LHSRVKLILE
YVKASEAGEV PFNHEILREA YALCHCLPVL STDKFKTDFY DQCNDVGLMA YLGTITKTCN
TMNQFVNKFN VLYDRQGIGR RMRGLFF
