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INT9_HUMAN
ID   INT9_HUMAN              Reviewed;         658 AA.
AC   Q9NV88; B7Z560; B7Z6M5; O00224; Q8TB16;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Integrator complex subunit 9;
DE            Short=Int9;
DE   AltName: Full=Protein related to CPSF subunits of 74 kDa;
DE            Short=RC-74;
GN   Name=INTS9; Synonyms=RC74;
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] (ISOFORMS 1; 2 AND 3).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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 [LARGE SCALE GENOMIC DNA] OF 163-658.
RA   Adams M.D.;
RT   "Human chromosome 8 BAC clone CIT987SK-2A8 complete sequence.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE INTEGRATOR
RP   COMPLEX.
RX   PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA   Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA   Shiekhattar R.;
RT   "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT   associates with the C-terminal repeat of RNA polymerase II.";
RL   Cell 123:265-276(2005).
RN   [6]
RP   IDENTIFICATION, SUBCELLULAR LOCATION, AND INTERACTION WITH CPSF3L.
RX   PubMed=15684398; DOI=10.1128/mcb.25.4.1489-1500.2005;
RA   Dominski Z., Yang X.-C., Purdy M., Wagner E.J., Marzluff W.F.;
RT   "A CPSF-73 homologue is required for cell cycle progression but not cell
RT   growth and interacts with a protein having features of CPSF-100.";
RL   Mol. Cell. Biol. 25:1489-1500(2005).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
RA   Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
RA   Reversade B., Wagner E.J., Lee L.A.;
RT   "Nuclear-localized Asunder regulates cytoplasmic dynein localization via
RT   its role in the integrator complex.";
RL   Mol. Biol. Cell 24:2954-2965(2013).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Component of the Integrator (INT) complex, a complex involved
CC       in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their
CC       3'-box-dependent processing. The Integrator complex is associated with
CC       the C-terminal domain (CTD) of RNA polymerase II largest subunit
CC       (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable).
CC       Mediates recruitment of cytoplasmic dynein to the nuclear envelope,
CC       probably as component of the INT complex (PubMed:23904267).
CC       {ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
CC   -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC       composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC       INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12 (PubMed:16239144).
CC       Interacts with ESRRB, ESRRB is probably not a core component of the
CC       multiprotein complex Integrator and this association is a bridge for
CC       the interaction with the multiprotein complex Integrator; attracts the
CC       transcriptional machinery (By similarity).
CC       {ECO:0000250|UniProtKB:Q8K114, ECO:0000269|PubMed:16239144}.
CC   -!- INTERACTION:
CC       Q9NV88; Q5TA45: INTS11; NbExp=16; IntAct=EBI-2866634, EBI-748258;
CC       Q9NV88; Q96HW7: INTS4; NbExp=2; IntAct=EBI-2866634, EBI-5663129;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15684398,
CC       ECO:0000269|PubMed:23904267}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9NV88-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NV88-2; Sequence=VSP_043011;
CC       Name=3;
CC         IsoId=Q9NV88-3; Sequence=VSP_044306;
CC   -!- MISCELLANEOUS: Although strongly related to RNA-specific endonuclease
CC       proteins, it lacks the HXHXDH motif that binds zinc and participates in
CC       the catalytic center. Its function as endonuclease is therefore unsure.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. INTS9 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB67601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK001733; BAA91867.1; -; mRNA.
DR   EMBL; AK298468; BAH12796.1; -; mRNA.
DR   EMBL; AK300593; BAH13311.1; -; mRNA.
DR   EMBL; AC040975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025267; AAH25267.1; -; mRNA.
DR   EMBL; U96629; AAB67601.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK005726; DAA05726.1; -; mRNA.
DR   EMBL; BK005674; DAA05670.1; -; mRNA.
DR   CCDS; CCDS34873.1; -. [Q9NV88-1]
DR   CCDS; CCDS55215.1; -. [Q9NV88-3]
DR   CCDS; CCDS55216.1; -. [Q9NV88-2]
DR   RefSeq; NP_001138631.1; NM_001145159.2. [Q9NV88-2]
DR   RefSeq; NP_001166033.1; NM_001172562.1. [Q9NV88-3]
DR   RefSeq; NP_060720.2; NM_018250.3. [Q9NV88-1]
DR   PDB; 5V8W; X-ray; 2.10 A; A/C/E/G=581-658.
DR   PDB; 7BFP; EM; 3.50 A; A=1-658.
DR   PDB; 7BFQ; EM; 3.50 A; A=1-658.
DR   PDB; 7CUN; EM; 3.50 A; I=1-658.
DR   PDB; 7PKS; EM; 3.60 A; i=1-658.
DR   PDBsum; 5V8W; -.
DR   PDBsum; 7BFP; -.
DR   PDBsum; 7BFQ; -.
DR   PDBsum; 7CUN; -.
DR   PDBsum; 7PKS; -.
DR   AlphaFoldDB; Q9NV88; -.
DR   SMR; Q9NV88; -.
DR   BioGRID; 120874; 64.
DR   ComplexPortal; CPX-6441; Integrator complex.
DR   CORUM; Q9NV88; -.
DR   IntAct; Q9NV88; 15.
DR   MINT; Q9NV88; -.
DR   STRING; 9606.ENSP00000429065; -.
DR   iPTMnet; Q9NV88; -.
DR   PhosphoSitePlus; Q9NV88; -.
DR   BioMuta; INTS9; -.
DR   DMDM; 119371246; -.
DR   EPD; Q9NV88; -.
DR   jPOST; Q9NV88; -.
DR   MassIVE; Q9NV88; -.
DR   MaxQB; Q9NV88; -.
DR   PaxDb; Q9NV88; -.
DR   PeptideAtlas; Q9NV88; -.
DR   PRIDE; Q9NV88; -.
DR   ProteomicsDB; 6659; -.
DR   ProteomicsDB; 82760; -. [Q9NV88-1]
DR   ProteomicsDB; 82761; -. [Q9NV88-2]
DR   Antibodypedia; 23131; 140 antibodies from 24 providers.
DR   DNASU; 55756; -.
DR   Ensembl; ENST00000416984.6; ENSP00000398208.2; ENSG00000104299.15. [Q9NV88-2]
DR   Ensembl; ENST00000521022.6; ENSP00000429065.1; ENSG00000104299.15. [Q9NV88-1]
DR   Ensembl; ENST00000521777.5; ENSP00000430943.1; ENSG00000104299.15. [Q9NV88-3]
DR   GeneID; 55756; -.
DR   KEGG; hsa:55756; -.
DR   MANE-Select; ENST00000521022.6; ENSP00000429065.1; NM_018250.4; NP_060720.2.
DR   UCSC; uc003xha.4; human. [Q9NV88-1]
DR   CTD; 55756; -.
DR   DisGeNET; 55756; -.
DR   GeneCards; INTS9; -.
DR   HGNC; HGNC:25592; INTS9.
DR   HPA; ENSG00000104299; Low tissue specificity.
DR   MIM; 611352; gene.
DR   neXtProt; NX_Q9NV88; -.
DR   OpenTargets; ENSG00000104299; -.
DR   PharmGKB; PA162392192; -.
DR   VEuPathDB; HostDB:ENSG00000104299; -.
DR   eggNOG; KOG1138; Eukaryota.
DR   GeneTree; ENSGT00390000001445; -.
DR   InParanoid; Q9NV88; -.
DR   OMA; CADSIKD; -.
DR   OrthoDB; 617493at2759; -.
DR   PhylomeDB; Q9NV88; -.
DR   TreeFam; TF314100; -.
DR   PathwayCommons; Q9NV88; -.
DR   Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR   SignaLink; Q9NV88; -.
DR   SIGNOR; Q9NV88; -.
DR   BioGRID-ORCS; 55756; 796 hits in 1086 CRISPR screens.
DR   ChiTaRS; INTS9; human.
DR   GeneWiki; INTS9; -.
DR   GenomeRNAi; 55756; -.
DR   Pharos; Q9NV88; Tbio.
DR   PRO; PR:Q9NV88; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9NV88; protein.
DR   Bgee; ENSG00000104299; Expressed in secondary oocyte and 145 other tissues.
DR   ExpressionAtlas; Q9NV88; baseline and differential.
DR   Genevisible; Q9NV88; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR   GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR022712; Beta_Casp.
DR   InterPro; IPR027074; Integrator_9su.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR46094; PTHR46094; 1.
DR   Pfam; PF16661; Lactamase_B_6; 1.
DR   SMART; SM01027; Beta-Casp; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Isopeptide bond; Nucleus;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..658
FT                   /note="Integrator complex subunit 9"
FT                   /id="PRO_0000259557"
FT   REGION          548..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        58
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..24
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044306"
FT   VAR_SEQ         67..87
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043011"
FT   CONFLICT        324
FT                   /note="V -> A (in Ref. 1; BAA91867)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           33..37
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           47..51
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           110..116
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          121..125
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           127..145
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           159..164
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           167..170
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           184..193
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   TURN            206..208
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          209..215
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          223..228
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          233..237
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   TURN            252..255
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           274..291
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          295..298
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          301..303
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           304..319
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          326..329
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           333..342
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          349..352
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           363..367
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   HELIX           369..372
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   STRAND          373..378
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   TURN            379..381
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           382..386
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          392..396
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          398..404
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           405..413
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:7CUN"
FT   STRAND          419..422
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          425..427
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           429..433
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   TURN            434..436
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          441..445
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           454..464
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          467..472
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           473..476
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          501..504
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          511..516
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   TURN            518..520
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           521..524
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          529..534
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          536..539
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          542..547
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   STRAND          550..554
FT                   /evidence="ECO:0007829|PDB:7BFP"
FT   HELIX           591..600
FT                   /evidence="ECO:0007829|PDB:5V8W"
FT   STRAND          607..610
FT                   /evidence="ECO:0007829|PDB:5V8W"
FT   STRAND          612..619
FT                   /evidence="ECO:0007829|PDB:5V8W"
FT   HELIX           621..623
FT                   /evidence="ECO:0007829|PDB:5V8W"
FT   STRAND          624..629
FT                   /evidence="ECO:0007829|PDB:5V8W"
FT   STRAND          632..639
FT                   /evidence="ECO:0007829|PDB:5V8W"
FT   HELIX           641..652
FT                   /evidence="ECO:0007829|PDB:5V8W"
FT   STRAND          655..657
FT                   /evidence="ECO:0007829|PDB:5V8W"
SQ   SEQUENCE   658 AA;  73814 MW;  81F1A24B99704684 CRC64;
     MKLYCLSGHP TLPCNVLKFK STTIMLDCGL DMTSTLNFLP LPLVQSPRLS NLPGWSLKDG
     NAFLDKELKE CSGHVFVDSV PEFCLPETEL IDLSTVDVIL ISNYHCMMAL PYITEHTGFT
     GTVYATEPTV QIGRLLMEEL VNFIERVPKA QSASLWKNKD IQRLLPSPLK DAVEVSTWRR
     CYTMQEVNSA LSKIQLVGYS QKIELFGAVQ VTPLSSGYAL GSSNWIIQSH YEKVSYVSGS
     SLLTTHPQPM DQASLKNSDV LVLTGLTQIP TANPDGMVGE FCSNLALTVR NGGNVLVPCY
     PSGVIYDLLE CLYQYIDSAG LSSVPLYFIS PVANSSLEFS QIFAEWLCHN KQSKVYLPEP
     PFPHAELIQT NKLKHYPSIH GDFSNDFRQP CVVFTGHPSL RFGDVVHFME LWGKSSLNTV
     IFTEPDFSYL EALAPYQPLA MKCIYCPIDT RLNFIQVSKL LKEVQPLHVV CPEQYTQPPP
     AQSHRMDLMI DCQPPAMSYR RAEVLALPFK RRYEKIEIMP ELADSLVPME IKPGISLATV
     SAVLHTKDNK HLLQPPPRPA QPTSGKKRKR VSDDVPDCKV LKPLLSGSIP VEQFVQTLEK
     HGFSDIKVED TAKGHIVLLQ EAETLIQIEE DSTHIICDND EMLRVRLRDL VLKFLQKF
 
 
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