AT7L3_HUMAN
ID AT7L3_HUMAN Reviewed; 347 AA.
AC Q14CW9; Q8IY68; Q96N40; Q9NPU5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ataxin-7-like protein 3 {ECO:0000255|HAMAP-Rule:MF_03047};
DE AltName: Full=SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047};
GN Name=ATXN7L3 {ECO:0000255|HAMAP-Rule:MF_03047};
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 MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 5-347 (ISOFORM 2).
RC TISSUE=Lymph;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-347 (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 MRNA] OF 161-347.
RC TISSUE=Amygdala;
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 [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SAGA
RP COMPLEX, INTERACTION WITH ENY2 AND USP22, AND DOMAIN.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=21746879; DOI=10.1128/mcb.05231-11;
RA Lang G., Bonnet J., Umlauf D., Karmodiya K., Koffler J., Stierle M.,
RA Devys D., Tora L.;
RT "The tightly controlled deubiquitination activity of the human SAGA complex
RT differentially modifies distinct gene regulatory elements.";
RL Mol. Cell. Biol. 31:3734-3744(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-131 AND SER-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-281 AND SER-326, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, INTERACTION WITH ENY2 AND
RP USP22, AND SUBCELLULAR LOCATION.
RX PubMed=27601583; DOI=10.1128/mcb.00193-16;
RA Li W., Atanassov B.S., Lan X., Mohan R.D., Swanson S.K., Farria A.T.,
RA Florens L., Washburn M.P., Workman J.L., Dent S.Y.;
RT "Cytoplasmic ATXN7L3B interferes with nuclear functions of the SAGA
RT deubiquitinase module.";
RL Mol. Cell. Biol. 36:2855-2866(2016).
RN [14]
RP STRUCTURE BY NMR OF 197-276 IN COMPLEX WITH ZINC.
RX PubMed=20634802; DOI=10.1038/embor.2010.98;
RA Bonnet J., Wang Y.H., Spedale G., Atkinson R.A., Romier C., Hamiche A.,
RA Pijnappel W.W., Timmers H.T., Tora L., Devys D., Kieffer B.;
RT "The structural plasticity of SCA7 domains defines their differential
RT nucleosome-binding properties.";
RL EMBO Rep. 11:612-618(2010).
CC -!- FUNCTION: Component of the transcription regulatory histone acetylation
CC (HAT) complex SAGA, a multiprotein complex that activates transcription
CC by remodeling chromatin and mediating histone acetylation and
CC deubiquitination. Within the SAGA complex, participates in a subcomplex
CC that specifically deubiquitinates both histones H2A and H2B
CC (PubMed:18206972, PubMed:21746879). The SAGA complex is recruited to
CC specific gene promoters by activators such as MYC, where it is required
CC for transcription. Required for nuclear receptor-mediated
CC transactivation. Within the complex, it is required to recruit USP22
CC and ENY2 into the SAGA complex (PubMed:18206972). Regulates H2B
CC monoubiquitination (H2Bub1) levels. Affects subcellular distribution of
CC ENY2, USP22 and ATXN7L3B (PubMed:27601583). {ECO:0000255|HAMAP-
CC Rule:MF_03047, ECO:0000269|PubMed:18206972,
CC ECO:0000269|PubMed:21746879, ECO:0000269|PubMed:27601583}.
CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H,
CC TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3,
CC and USP22 form an additional subcomplex of SAGA called the DUB module
CC (deubiquitination module) (PubMed:18206972, PubMed:21746879,
CC PubMed:27601583). Interacts directly with ENY2 and USP22
CC (PubMed:18206972). {ECO:0000255|HAMAP-Rule:MF_03047,
CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:21746879,
CC ECO:0000269|PubMed:27601583}.
CC -!- INTERACTION:
CC Q14CW9; Q9NPA8: ENY2; NbExp=6; IntAct=EBI-949215, EBI-719226;
CC Q14CW9; Q9UPT9-2: USP22; NbExp=3; IntAct=EBI-949215, EBI-12074414;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047,
CC ECO:0000269|PubMed:27601583}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14CW9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14CW9-2; Sequence=VSP_036721;
CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of
CC the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047,
CC ECO:0000269|PubMed:18206972}.
CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain together with the
CC C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the
CC SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000255|HAMAP-
CC Rule:MF_03047}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37418.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB71070.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC037418; AAH37418.1; ALT_INIT; mRNA.
DR EMBL; BC113595; AAI13596.1; -; mRNA.
DR EMBL; BC126113; AAI26114.1; -; mRNA.
DR EMBL; AK056002; BAB71070.1; ALT_INIT; mRNA.
DR EMBL; AL390158; CAB99093.1; -; mRNA.
DR CCDS; CCDS42345.1; -. [Q14CW9-1]
DR CCDS; CCDS45697.1; -. [Q14CW9-2]
DR RefSeq; NP_001092303.1; NM_001098833.1.
DR RefSeq; NP_064603.1; NM_020218.1.
DR RefSeq; XP_016880374.1; XM_017024885.1.
DR RefSeq; XP_016880375.1; XM_017024886.1.
DR PDB; 2KKT; NMR; -; A=197-276.
DR PDBsum; 2KKT; -.
DR AlphaFoldDB; Q14CW9; -.
DR BMRB; Q14CW9; -.
DR SMR; Q14CW9; -.
DR BioGRID; 121289; 49.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR CORUM; Q14CW9; -.
DR IntAct; Q14CW9; 37.
DR MINT; Q14CW9; -.
DR STRING; 9606.ENSP00000397259; -.
DR iPTMnet; Q14CW9; -.
DR PhosphoSitePlus; Q14CW9; -.
DR BioMuta; ATXN7L3; -.
DR DMDM; 121948758; -.
DR EPD; Q14CW9; -.
DR jPOST; Q14CW9; -.
DR MassIVE; Q14CW9; -.
DR MaxQB; Q14CW9; -.
DR PaxDb; Q14CW9; -.
DR PeptideAtlas; Q14CW9; -.
DR PRIDE; Q14CW9; -.
DR ProteomicsDB; 60332; -. [Q14CW9-1]
DR ProteomicsDB; 60333; -. [Q14CW9-2]
DR Antibodypedia; 54391; 87 antibodies from 24 providers.
DR DNASU; 56970; -.
DR Ensembl; ENST00000389384.8; ENSP00000374035.3; ENSG00000087152.16. [Q14CW9-1]
DR Ensembl; ENST00000454077.6; ENSP00000397259.1; ENSG00000087152.16. [Q14CW9-2]
DR Ensembl; ENST00000587097.6; ENSP00000465614.2; ENSG00000087152.16. [Q14CW9-1]
DR GeneID; 56970; -.
DR MANE-Select; ENST00000587097.6; ENSP00000465614.2; NM_001382309.1; NP_001369238.1.
DR UCSC; uc002ifz.4; human. [Q14CW9-1]
DR CTD; 56970; -.
DR DisGeNET; 56970; -.
DR GeneCards; ATXN7L3; -.
DR HGNC; HGNC:25416; ATXN7L3.
DR HPA; ENSG00000087152; Low tissue specificity.
DR MIM; 619010; gene.
DR neXtProt; NX_Q14CW9; -.
DR OpenTargets; ENSG00000087152; -.
DR PharmGKB; PA134991793; -.
DR VEuPathDB; HostDB:ENSG00000087152; -.
DR eggNOG; KOG2612; Eukaryota.
DR GeneTree; ENSGT00940000158253; -.
DR InParanoid; Q14CW9; -.
DR OMA; PSNYENM; -.
DR OrthoDB; 1244885at2759; -.
DR PhylomeDB; Q14CW9; -.
DR TreeFam; TF324580; -.
DR PathwayCommons; Q14CW9; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q14CW9; -.
DR BioGRID-ORCS; 56970; 211 hits in 1084 CRISPR screens.
DR ChiTaRS; ATXN7L3; human.
DR EvolutionaryTrace; Q14CW9; -.
DR GenomeRNAi; 56970; -.
DR Pharos; Q14CW9; Tbio.
DR PRO; PR:Q14CW9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14CW9; protein.
DR Bgee; ENSG00000087152; Expressed in prefrontal cortex and 176 other tissues.
DR ExpressionAtlas; Q14CW9; baseline and differential.
DR Genevisible; Q14CW9; HS.
DR GO; GO:0071819; C:DUBm complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IC:ComplexPortal.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR InterPro; IPR013243; SCA7_dom.
DR Pfam; PF08313; SCA7; 1.
DR Pfam; PF08209; Sgf11; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromatin regulator;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..347
FT /note="Ataxin-7-like protein 3"
FT /id="PRO_0000278301"
FT DOMAIN 196..263
FT /note="SCA7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT ZN_FING 84..105
FT /note="SGF11-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT REGION 116..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 159
FT /note="K -> KLWYLPFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036721"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:2KKT"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2KKT"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:2KKT"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2KKT"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:2KKT"
SQ SEQUENCE 347 AA; 38651 MW; 742D85BFF4ADD0C0 CRC64;
MKMEEMSLSG LDNSKLEAIA QEIYADLVED SCLGFCFEVH RAVKCGYFFL DDTDPDSMKD
FEIVDQPGLD IFGQVFNQWK SKECVCPNCS RSIAASRFAP HLEKCLGMGR NSSRIANRRI
ANSNNMNKSE SDQEDNDDIN DNDWSYGSEK KAKKRKSDKN PNSPRRSKSL KHKNGELSNS
DPFKYNNSTG ISYETLGPEE LRSLLTTQCG VISEHTKKMC TRSLRCPQHT DEQRRTVRIY
FLGPSAVLPE VESSLDNDSF DMTDSQALIS RLQWDGSSDL SPSDSGSSKT SENQGWGLGT
NSSESRKTKK KKSHLSLVGT ASGLGSNKKK KPKPPAPPTP SIYDDIN
