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 27-MAR-2024, entry version 156. 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=20; IntAct=EBI-2866634, EBI-748258; CC Q9NV88; Q96HW7: INTS4; NbExp=3; 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}; 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; 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 PDB; 7YCX; EM; 4.18 A; I=1-658. DR PDBsum; 5V8W; -. DR PDBsum; 7BFP; -. DR PDBsum; 7BFQ; -. DR PDBsum; 7CUN; -. DR PDBsum; 7PKS; -. DR PDBsum; 7YCX; -. DR AlphaFoldDB; Q9NV88; -. DR EMDB; EMD-12159; -. DR EMDB; EMD-12163; -. DR EMDB; EMD-12164; -. DR EMDB; EMD-12165; -. DR EMDB; EMD-12166; -. DR EMDB; EMD-13479; -. DR EMDB; EMD-30473; -. DR EMDB; EMD-33741; -. DR SMR; Q9NV88; -. DR BioGRID; 120874; 87. 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; 9606-ENSP00000429065; -. DR PeptideAtlas; Q9NV88; -. DR ProteomicsDB; 6659; -. DR ProteomicsDB; 82760; -. [Q9NV88-1] DR ProteomicsDB; 82761; -. [Q9NV88-2] DR Pumba; Q9NV88; -. DR Antibodypedia; 23131; 152 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 AGR; HGNC:25592; -. 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; EPFPHAF; -. DR OrthoDB; 2874386at2759; -. 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; 827 hits in 1164 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 147 other cell types or tissues. DR ExpressionAtlas; Q9NV88; baseline and differential. 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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:FlyBase. DR GO; GO:0034243; P:regulation of transcription elongation by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central. DR GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL. DR CDD; cd16294; Int9-like_MBL-fold; 1. DR Gene3D; 3.40.50.10890; -; 1. DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1. DR InterPro; IPR022712; Beta_Casp. DR InterPro; IPR027074; Integrator_9su. DR InterPro; IPR048660; IntS9-like_C. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro. DR PANTHER; PTHR46094; INTEGRATOR COMPLEX SUBUNIT 9; 1. DR PANTHER; PTHR46094:SF1; INTEGRATOR COMPLEX SUBUNIT 9; 1. DR Pfam; PF10996; Beta-Casp; 1. DR Pfam; PF21382; IntS9_C; 1. DR Pfam; PF16661; Lactamase_B_6; 1. DR SMART; SM01027; Beta-Casp; 1. DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1. DR Genevisible; Q9NV88; HS. 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 //