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 24-JAN-2024, entry version 166. 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}. 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; 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. DR PDB; 3EAY; X-ray; 2.40 A; A=728-1050. DR PDB; 7R2E; X-ray; 1.74 A; A/B=729-1050. DR PDBsum; 3EAY; -. DR PDBsum; 7R2E; -. DR AlphaFoldDB; Q9BQF6; -. DR SMR; Q9BQF6; -. DR BioGRID; 121491; 26. DR IntAct; Q9BQF6; 12. DR MINT; Q9BQF6; -. DR STRING; 9606.ENSP00000377655; -. DR BindingDB; Q9BQF6; -. DR ChEMBL; CHEMBL1741213; -. DR MEROPS; C48.009; -. DR GlyGen; Q9BQF6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BQF6; -. DR PhosphoSitePlus; Q9BQF6; -. DR SwissPalm; Q9BQF6; -. DR BioMuta; SENP7; -. DR DMDM; 300669717; -. DR EPD; Q9BQF6; -. DR jPOST; Q9BQF6; -. DR MassIVE; Q9BQF6; -. DR MaxQB; Q9BQF6; -. DR PaxDb; 9606-ENSP00000377655; -. DR PeptideAtlas; 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 Pumba; Q9BQF6; -. DR Antibodypedia; 15887; 274 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 AGR; HGNC:30402; -. 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; VMLTNIL; -. DR OrthoDB; 1068193at2759; -. DR PhylomeDB; Q9BQF6; -. DR TreeFam; TF350136; -. DR BRENDA; 3.4.22.B75; 2681. DR PathwayCommons; Q9BQF6; -. DR SignaLink; Q9BQF6; -. DR BioGRID-ORCS; 57337; 14 hits in 1162 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 173 other cell types or tissues. DR ExpressionAtlas; Q9BQF6; baseline and differential. 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 1.10.418.20; -; 1. DR Gene3D; 3.30.310.130; Ubiquitin-related; 1. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR003653; Peptidase_C48_C. DR PANTHER; PTHR46896; SENTRIN-SPECIFIC PROTEASE; 1. DR PANTHER; PTHR46896:SF2; SENTRIN-SPECIFIC PROTEASE 7; 1. DR Pfam; PF02902; Peptidase_C48; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS50600; ULP_PROTEASE; 1. DR Genevisible; Q9BQF6; HS. 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:7R2E" FT STRAND 756..758 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 760..763 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 764..767 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 768..770 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 778..791 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 795..800 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 801..803 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 808..812 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 828..835 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 836..840 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 845..847 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 849..856 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 861..867 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 934..938 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 946..965 FT /evidence="ECO:0007829|PDB:7R2E" FT TURN 973..975 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 976..979 FT /evidence="ECO:0007829|PDB:7R2E" FT STRAND 987..990 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 992..1005 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 1023..1027 FT /evidence="ECO:0007829|PDB:7R2E" FT HELIX 1029..1046 FT /evidence="ECO:0007829|PDB:7R2E" 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 //