SENP7_HUMAN
ID SENP7_HUMAN Reviewed; 1050 AA.
AC Q9BQF6; A1L3A5; A8MW39; B7WNW8; Q7Z3F4; Q96PS5; Q9C0F6; Q9HBT5;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Sentrin-specific protease 7 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000269|PubMed:18799455};
DE AltName: Full=SUMO-1-specific protease 2;
DE AltName: Full=Sentrin/SUMO-specific protease SENP7;
GN Name=SENP7 {ECO:0000303|Ref.2, ECO:0000312|HGNC:HGNC:30402};
GN Synonyms=KIAA1707 {ECO:0000303|PubMed:11214970}, SSP2, SUSP2;
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 2).
RA Choi S.J., Jeon Y.-J., Kim K.I., Nishimori S., Suzuki T., Uchida S.,
RA Shimbara N., Tanaka K., Chung C.H.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RA Gong L., Yeh E.T.H.;
RT "SENP7, a novel human sentrin-specific protease.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Fetal kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1050, AND VARIANT HIS-612.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-443 AND SER-444, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-373; SER-443 AND
RP SER-444, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 728-1050, FUNCTION, AND
RP MUTAGENESIS OF PHE-775 AND VAL-779.
RX PubMed=18799455; DOI=10.1074/jbc.m805655200;
RA Lima C.D., Reverter D.;
RT "Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation
RT activities for SENP6 and SENP7.";
RL J. Biol. Chem. 283:32045-32055(2008).
CC -!- FUNCTION: Protease that acts as a positive regulator of the cGAS-STING
CC pathway by catalyzing desumoylation of CGAS. Desumoylation of CGAS
CC promotes DNA-binding activity of CGAS, subsequent oligomerization and
CC activation (By similarity). Deconjugates SUMO2 and SUMO3 from targeted
CC proteins, but not SUMO1 (PubMed:18799455). Catalyzes the deconjugation
CC of poly-SUMO2 and poly-SUMO3 chains (PubMed:18799455). Has very low
CC efficiency in processing full-length SUMO proteins to their mature
CC forms (PubMed:18799455). {ECO:0000250|UniProtKB:Q8BUH8,
CC ECO:0000269|PubMed:18799455}.
CC -!- INTERACTION:
CC Q9BQF6; P45973: CBX5; NbExp=4; IntAct=EBI-766251, EBI-78219;
CC Q9BQF6; Q13263: TRIM28; NbExp=3; IntAct=EBI-766251, EBI-78139;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BUH8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9BQF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQF6-2; Sequence=VSP_039499;
CC Name=3;
CC IsoId=Q9BQF6-3; Sequence=VSP_039498, VSP_039502;
CC Name=4;
CC IsoId=Q9BQF6-4; Sequence=VSP_039499, VSP_039501;
CC Name=5;
CC IsoId=Q9BQF6-5; Sequence=VSP_039500;
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AF199458; AAL25651.1; -; mRNA.
DR EMBL; AF217504; AAG09703.1; -; mRNA.
DR EMBL; AL136599; CAB66534.1; -; mRNA.
DR EMBL; BX537943; CAD97911.1; -; mRNA.
DR EMBL; AC068764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129988; AAI29989.1; -; mRNA.
DR EMBL; AB051494; BAB21798.1; -; mRNA.
DR CCDS; CCDS2941.2; -. [Q9BQF6-1]
DR CCDS; CCDS63704.1; -. [Q9BQF6-4]
DR CCDS; CCDS63705.1; -. [Q9BQF6-2]
DR CCDS; CCDS63706.1; -. [Q9BQF6-5]
DR RefSeq; NP_001070671.1; NM_001077203.2.
DR RefSeq; NP_001269730.1; NM_001282801.1. [Q9BQF6-5]
DR RefSeq; NP_001269731.1; NM_001282802.1. [Q9BQF6-2]
DR RefSeq; NP_001269732.1; NM_001282803.1. [Q9BQF6-4]
DR RefSeq; NP_001269733.1; NM_001282804.1.
DR RefSeq; NP_065705.3; NM_020654.4. [Q9BQF6-1]
DR RefSeq; XP_016862414.1; XM_017006925.1. [Q9BQF6-2]
DR PDB; 3EAY; X-ray; 2.40 A; A=728-1050.
DR PDBsum; 3EAY; -.
DR AlphaFoldDB; Q9BQF6; -.
DR SMR; Q9BQF6; -.
DR BioGRID; 121491; 23.
DR IntAct; Q9BQF6; 12.
DR MINT; Q9BQF6; -.
DR STRING; 9606.ENSP00000377655; -.
DR BindingDB; Q9BQF6; -.
DR ChEMBL; CHEMBL1741213; -.
DR MEROPS; C48.009; -.
DR iPTMnet; Q9BQF6; -.
DR PhosphoSitePlus; Q9BQF6; -.
DR BioMuta; SENP7; -.
DR DMDM; 300669717; -.
DR EPD; Q9BQF6; -.
DR jPOST; Q9BQF6; -.
DR MassIVE; Q9BQF6; -.
DR MaxQB; Q9BQF6; -.
DR PaxDb; Q9BQF6; -.
DR PeptideAtlas; Q9BQF6; -.
DR PRIDE; Q9BQF6; -.
DR ProteomicsDB; 78669; -. [Q9BQF6-1]
DR ProteomicsDB; 78670; -. [Q9BQF6-2]
DR ProteomicsDB; 78671; -. [Q9BQF6-3]
DR ProteomicsDB; 78672; -. [Q9BQF6-4]
DR ProteomicsDB; 78673; -. [Q9BQF6-5]
DR Antibodypedia; 15887; 247 antibodies from 29 providers.
DR DNASU; 57337; -.
DR Ensembl; ENST00000314261.11; ENSP00000313624.7; ENSG00000138468.16. [Q9BQF6-5]
DR Ensembl; ENST00000348610.3; ENSP00000342159.3; ENSG00000138468.16. [Q9BQF6-2]
DR Ensembl; ENST00000394085.7; ENSP00000377647.3; ENSG00000138468.16. [Q9BQF6-3]
DR Ensembl; ENST00000394091.5; ENSP00000377651.1; ENSG00000138468.16. [Q9BQF6-4]
DR Ensembl; ENST00000394095.7; ENSP00000377655.2; ENSG00000138468.16. [Q9BQF6-1]
DR GeneID; 57337; -.
DR KEGG; hsa:57337; -.
DR MANE-Select; ENST00000394095.7; ENSP00000377655.2; NM_020654.5; NP_065705.3.
DR UCSC; uc003dus.5; human. [Q9BQF6-1]
DR CTD; 57337; -.
DR DisGeNET; 57337; -.
DR GeneCards; SENP7; -.
DR HGNC; HGNC:30402; SENP7.
DR HPA; ENSG00000138468; Low tissue specificity.
DR MIM; 612846; gene.
DR neXtProt; NX_Q9BQF6; -.
DR OpenTargets; ENSG00000138468; -.
DR PharmGKB; PA134925171; -.
DR VEuPathDB; HostDB:ENSG00000138468; -.
DR eggNOG; KOG0779; Eukaryota.
DR GeneTree; ENSGT00940000157308; -.
DR HOGENOM; CLU_024324_1_1_1; -.
DR InParanoid; Q9BQF6; -.
DR OMA; PLQWKRS; -.
DR OrthoDB; 1241636at2759; -.
DR PhylomeDB; Q9BQF6; -.
DR TreeFam; TF350136; -.
DR BRENDA; 3.4.22.B75; 2681.
DR PathwayCommons; Q9BQF6; -.
DR SignaLink; Q9BQF6; -.
DR BioGRID-ORCS; 57337; 12 hits in 1086 CRISPR screens.
DR ChiTaRS; SENP7; human.
DR EvolutionaryTrace; Q9BQF6; -.
DR GeneWiki; SENP7; -.
DR GenomeRNAi; 57337; -.
DR Pharos; Q9BQF6; Tchem.
DR PRO; PR:Q9BQF6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BQF6; protein.
DR Bgee; ENSG00000138468; Expressed in calcaneal tendon and 172 other tissues.
DR ExpressionAtlas; Q9BQF6; baseline and differential.
DR Genevisible; Q9BQF6; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Immunity;
KW Innate immunity; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1050
FT /note="Sentrin-specific protease 7"
FT /id="PRO_0000101726"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..1050
FT /note="Protease"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT COMPBIAS 186..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 860
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 939
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 992
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUH8"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZF42"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..812
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_039498"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_039499"
FT VAR_SEQ 95..225
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039501"
FT VAR_SEQ 95..160
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_039500"
FT VAR_SEQ 813..827
FT /note="TRKENNLTEDNPNLS -> MKKFLYIKSVFHTLR (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_039502"
FT VARIANT 79
FT /note="K -> Q (in dbSNP:rs6809436)"
FT /id="VAR_029651"
FT VARIANT 612
FT /note="Q -> H (in dbSNP:rs2433031)"
FT /evidence="ECO:0000269|PubMed:11214970"
FT /id="VAR_029652"
FT MUTAGEN 775
FT /note="F->W: Slightly increased deconjugation activity."
FT /evidence="ECO:0000269|PubMed:18799455"
FT MUTAGEN 779
FT /note="V->E: Reduces deconjugation activity."
FT /evidence="ECO:0000269|PubMed:18799455"
FT CONFLICT 90
FT /note="K -> R (in Ref. 3; CAB66534)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="K -> R (in Ref. 3; CAB66534)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="N -> Y (in Ref. 3; CAB66534)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="L -> H (in Ref. 1; AAL25651)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="N -> S (in Ref. 3; CAB66534)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="Q -> R (in Ref. 3; CAB66534)"
FT /evidence="ECO:0000305"
FT CONFLICT 1006
FT /note="D -> N (in Ref. 1; AAL25651)"
FT /evidence="ECO:0000305"
FT STRAND 747..752
FT /evidence="ECO:0007829|PDB:3EAY"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:3EAY"
FT STRAND 760..763
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 764..768
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 778..791
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 795..799
FT /evidence="ECO:0007829|PDB:3EAY"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 807..812
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 828..833
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 837..840
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 845..847
FT /evidence="ECO:0007829|PDB:3EAY"
FT STRAND 849..857
FT /evidence="ECO:0007829|PDB:3EAY"
FT STRAND 860..867
FT /evidence="ECO:0007829|PDB:3EAY"
FT STRAND 933..938
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 946..965
FT /evidence="ECO:0007829|PDB:3EAY"
FT TURN 973..975
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 992..1005
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 1023..1027
FT /evidence="ECO:0007829|PDB:3EAY"
FT HELIX 1029..1046
FT /evidence="ECO:0007829|PDB:3EAY"
SQ SEQUENCE 1050 AA; 119658 MW; CB455A0B22709052 CRC64;
MDKRKLGRRP SSSEIITEGK RKKSSSDLSE IRKMLNAKPE DVHVQSPLSK FRSSERWTLP
LQWERSLRNK VISLDHKNKK HIRGCPVTSK SSPERQLKVM LTNVLWTDLG RKFRKTLPRN
DANLCDANKV QSDSLPSTSV DSLETCQKLE PLRQSLNLSE RIPRVILTNV LGTELGRKYI
RTPPVTEGSL SDTDNLQSEQ LSSSSDGSLE SYQNLNPHKS CYLSERGSQR SKTVDDNSAK
QTAHNKEKRR KDDGISLLIS DTQPEDLNSG SRGCDHLEQE SRNKDVKYSD SKVELTLISR
KTKRRLRNNL PDSQYCTSLD KSTEQTKKQE DDSTISTEFE KPSENYHQDP KLPEEITTKP
TKSDFTKLSS LNSQELTLSN ATKSASAGST TETVENSNSI DIVGISSLVE KDENELNTIE
KPILRGHNEG NQSLISAEPI VVSSDEEGPV EHKSSEILKL QSKQDRETTN ENESTSESAL
LELPLITCES VQMSSELCPY NPVMENISSI MPSNEMDLQL DFIFTSVYIG KIKGASKGCV
TITKKYIKIP FQVSLNEISL LVDTTHLKRF GLWKSKDDNH SKRSHAILFF WVSSDYLQEI
QTQLEHSVLS QQSKSSEFIF LELHNPVSQR EELKLKDIMT EISIISGELE LSYPLSWVQA
FPLFQNLSSK ESSFIHYYCV STCSFPAGVA VAEEMKLKSV SQPSNTDAAK PTYTFLQKQS
SGCYSLSITS NPDEEWREVR HTGLVQKLIV YPPPPTKGGL GVTNEDLECL EEGEFLNDVI
IDFYLKYLIL EKASDELVER SHIFSSFFYK CLTRKENNLT EDNPNLSMAQ RRHKRVRTWT
RHINIFNKDY IFVPVNESSH WYLAVICFPW LEEAVYEDFP QTVSQQSQAQ QSQNDNKTID
NDLRTTSTLS LSAEDSQSTE SNMSVPKKMC KRPCILILDS LKAASVQNTV QNLREYLEVE
WEVKLKTHRQ FSKTNMVDLC PKVPKQDNSS DCGVYLLQYV ESFFKDPIVN FELPIHLEKW
FPRHVIKTKR EDIRELILKL HLQQQKGSSS
