ID INT8_HUMAN Reviewed; 995 AA. AC Q75QN2; B2RN92; Q5RKZ3; Q6P1R5; Q7Z314; Q9NVS6; Q9NWY7; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-OCT-2024, entry version 161. DE RecName: Full=Integrator complex subunit 8; DE Short=Int8; DE AltName: Full=Protein kaonashi-1; GN Name=INTS8; Synonyms=C8orf52; 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 1). RC TISSUE=Brain; RA Atsushi S., Asakawa S., Shimizu N.; RT "Novel gene with no significant domain."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Testis, and Uterus; 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 MRNA] OF 180-995 (ISOFORM 2). RC TISSUE=Rectum tumor; 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 MRNA] OF 307-995 (ISOFORM 1). RC TISSUE=Carcinoma, and 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 [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY RP 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 [8] RP VARIANTS NEDCHS GLY-298 AND 973-GLU--LEU-975 DEL, CHARACTERIZATION OF RP VARIANTS NEDCHS GLY-298 AND 973-GLU--LEU-975 DEL, DEVELOPMENTAL STAGE, AND RP FUNCTION. RX PubMed=28542170; DOI=10.1371/journal.pgen.1006809; RA Oegema R., Baillat D., Schot R., van Unen L.M., Brooks A., Kia S.K., RA Hoogeboom A.J.M., Xia Z., Li W., Cesaroni M., Lequin M.H., RA van Slegtenhorst M., Dobyns W.B., de Coo I.F.M., Verheijen F.W., Kremer A., RA van der Spek P.J., Heijsman D., Wagner E.J., Fornerod M., Mancini G.M.S.; RT "Human mutations in integrator complex subunits link transcriptome RT integrity to brain development."; RL PLoS Genet. 13:e1006809-e1006809(2017). CC -!- FUNCTION: Component of the Integrator complex, a complex involved in CC the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'- CC box-dependent processing. The Integrator complex is associated with the CC C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) CC and is recruited to the U1 and U2 snRNAs genes. CC {ECO:0000269|PubMed:28542170}. 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. CC {ECO:0000269|PubMed:16239144}. CC -!- INTERACTION: CC Q75QN2; Q6P9B9: INTS5; NbExp=4; IntAct=EBI-2340089, EBI-7600112; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q75QN2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q75QN2-2; Sequence=VSP_021469; CC -!- DEVELOPMENTAL STAGE: Highly expressed in the brain in the ventricular CC and subventricular zones, caudal and lateral ganglionic eminences and CC cerebellar primordium at 16-21 postconceptional week. CC {ECO:0000269|PubMed:28542170}. CC -!- DISEASE: Neurodevelopmental disorder with cerebellar hypoplasia and CC spasticity (NEDCHS) [MIM:618572]: An autosomal recessive CC neurodevelopmental disorder characterized by global developmental CC delay, profound intellectual disability, seizures, absent speech, CC spasticity, facial and limb dysmorphism, and subtle structural brain CC abnormalities including cerebellar hypoplasia. CC {ECO:0000269|PubMed:28542170}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the Integrator subunit 8 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50536.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA91238.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA91671.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AB161944; BAD10863.1; -; mRNA. DR EMBL; CH471060; EAW91726.1; -; Genomic_DNA. DR EMBL; BC050536; AAH50536.1; ALT_FRAME; mRNA. DR EMBL; BC064915; AAH64915.1; -; mRNA. DR EMBL; BC136754; AAI36755.1; -; mRNA. DR EMBL; BX538203; CAD98067.1; -; mRNA. DR EMBL; AK000537; BAA91238.1; ALT_INIT; mRNA. DR EMBL; AK001403; BAA91671.1; ALT_INIT; mRNA. DR EMBL; BK005731; DAA05731.1; -; mRNA. DR CCDS; CCDS34925.1; -. [Q75QN2-1] DR RefSeq; NP_060334.2; NM_017864.3. [Q75QN2-1] DR RefSeq; XP_016869108.1; XM_017013619.1. DR PDB; 7CUN; EM; 3.50 A; H=1-995. DR PDB; 7PKS; EM; 3.60 A; h=1-995. DR PDB; 7YCX; EM; 4.18 A; H=1-995. DR PDB; 8RBX; EM; 4.10 A; h=1-995. DR PDB; 8RBZ; EM; 3.70 A; h=1-995. DR PDB; 8RC4; EM; 3.10 A; h=1-995. DR PDB; 9EOF; EM; 7.70 A; F=1-995. DR PDB; 9EP4; EM; 3.20 A; A=1-995. DR PDBsum; 7CUN; -. DR PDBsum; 7PKS; -. DR PDBsum; 7YCX; -. DR PDBsum; 8RBX; -. DR PDBsum; 8RBZ; -. DR PDBsum; 8RC4; -. DR PDBsum; 9EOF; -. DR PDBsum; 9EP4; -. DR AlphaFoldDB; Q75QN2; -. DR EMDB; EMD-13479; -. DR EMDB; EMD-19038; -. DR EMDB; EMD-19040; -. DR EMDB; EMD-19047; -. DR EMDB; EMD-19853; -. DR EMDB; EMD-19872; -. DR EMDB; EMD-30473; -. DR EMDB; EMD-33741; -. DR SMR; Q75QN2; -. DR BioGRID; 120788; 65. DR ComplexPortal; CPX-6441; Integrator complex. DR CORUM; Q75QN2; -. DR IntAct; Q75QN2; 44. DR MINT; Q75QN2; -. DR STRING; 9606.ENSP00000430338; -. DR iPTMnet; Q75QN2; -. DR PhosphoSitePlus; Q75QN2; -. DR BioMuta; INTS8; -. DR DMDM; 74712892; -. DR jPOST; Q75QN2; -. DR MassIVE; Q75QN2; -. DR PaxDb; 9606-ENSP00000430338; -. DR PeptideAtlas; Q75QN2; -. DR ProteomicsDB; 68647; -. [Q75QN2-1] DR ProteomicsDB; 68648; -. [Q75QN2-2] DR Pumba; Q75QN2; -. DR Antibodypedia; 25892; 55 antibodies from 18 providers. DR DNASU; 55656; -. DR Ensembl; ENST00000523731.6; ENSP00000430338.1; ENSG00000164941.14. [Q75QN2-1] DR GeneID; 55656; -. DR KEGG; hsa:55656; -. DR MANE-Select; ENST00000523731.6; ENSP00000430338.1; NM_017864.4; NP_060334.2. DR UCSC; uc003yhb.5; human. [Q75QN2-1] DR AGR; HGNC:26048; -. DR CTD; 55656; -. DR DisGeNET; 55656; -. DR GeneCards; INTS8; -. DR HGNC; HGNC:26048; INTS8. DR HPA; ENSG00000164941; Low tissue specificity. DR MalaCards; INTS8; -. DR MIM; 611351; gene. DR MIM; 618572; phenotype. DR neXtProt; NX_Q75QN2; -. DR OpenTargets; ENSG00000164941; -. DR PharmGKB; PA142672371; -. DR VEuPathDB; HostDB:ENSG00000164941; -. DR eggNOG; ENOG502QQS8; Eukaryota. DR GeneTree; ENSGT00390000007597; -. DR HOGENOM; CLU_012129_0_0_1; -. DR InParanoid; Q75QN2; -. DR OMA; ASLSDWM; -. DR OrthoDB; 5476785at2759; -. DR PhylomeDB; Q75QN2; -. DR TreeFam; TF324241; -. DR PathwayCommons; Q75QN2; -. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR SignaLink; Q75QN2; -. DR SIGNOR; Q75QN2; -. DR BioGRID-ORCS; 55656; 719 hits in 1167 CRISPR screens. DR ChiTaRS; INTS8; human. DR GeneWiki; INTS8; -. DR GenomeRNAi; 55656; -. DR Pharos; Q75QN2; Tdark. DR PRO; PR:Q75QN2; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q75QN2; protein. DR Bgee; ENSG00000164941; Expressed in secondary oocyte and 200 other cell types or tissues. DR ExpressionAtlas; Q75QN2; baseline and differential. DR GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. 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 InterPro; IPR038751; Int8. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR13350:SF1; INTEGRATOR COMPLEX SUBUNIT 8; 1. DR PANTHER; PTHR13350; UNCHARACTERIZED; 1. DR SUPFAM; SSF48452; TPR-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; KW Intellectual disability; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; TPR repeat. FT CHAIN 1..995 FT /note="Integrator complex subunit 8" FT /id="PRO_0000259553" FT REPEAT 250..288 FT /note="TPR 1" FT REPEAT 320..356 FT /note="TPR 2" FT REPEAT 570..603 FT /note="TPR 3" FT REPEAT 833..866 FT /note="TPR 4" FT MOD_RES 18 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983" FT VAR_SEQ 879..895 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_021469" FT VARIANT 298 FT /note="D -> G (in NEDCHS; occurs in a splice site resulting FT in altered splicing and probable nonsense-mediated mRNA FT decay; dbSNP:rs1586479593)" FT /evidence="ECO:0000269|PubMed:28542170" FT /id="VAR_083358" FT VARIANT 973..975 FT /note="Missing (in NEDCHS; alters the assembly of the FT Integrator complex)" FT /evidence="ECO:0000269|PubMed:28542170" FT /id="VAR_083359" FT CONFLICT 778 FT /note="V -> A (in Ref. 5; BAA91238)" FT /evidence="ECO:0000305" FT CONFLICT 832 FT /note="N -> S (in Ref. 4; CAD98067)" FT /evidence="ECO:0000305" FT HELIX 25..29 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 33..38 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 47..59 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 61..69 FT /evidence="ECO:0007829|PDB:7CUN" FT HELIX 76..91 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 96..102 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 105..118 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 127..129 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 137..158 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 171..193 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 195..205 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 217..224 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 235..237 FT /evidence="ECO:0007829|PDB:7CUN" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 245..264 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 271..288 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 299..312 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 316..320 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 325..335 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 338..351 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 356..372 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 377..394 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 401..406 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 412..426 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 428..430 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 433..448 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 451..453 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 454..460 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 463..468 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 471..484 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 505..518 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 522..535 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 536..538 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 541..543 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 552..559 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 564..582 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 586..600 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 601..603 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 605..625 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 626..631 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 636..647 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 651..653 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 657..669 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 673..678 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 682..687 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 689..702 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 703..705 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 707..724 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 736..738 FT /evidence="ECO:0007829|PDB:7CUN" FT TURN 741..743 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 745..747 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 750..752 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 754..761 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 767..782 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 786..788 FT /evidence="ECO:0007829|PDB:7CUN" FT STRAND 797..799 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 806..808 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 811..828 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 833..845 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 849..862 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 863..868 FT /evidence="ECO:0007829|PDB:8RC4" FT TURN 873..875 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 878..890 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 894..900 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 901..903 FT /evidence="ECO:0007829|PDB:8RC4" FT STRAND 904..906 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 909..916 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 925..931 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 935..947 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 951..961 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 964..966 FT /evidence="ECO:0007829|PDB:8RC4" FT HELIX 972..994 FT /evidence="ECO:0007829|PDB:8RC4" SQ SEQUENCE 995 AA; 113088 MW; 24D06E11821BD4D5 CRC64; MSAEAADREA ATSSRPCTPP QTCWFEFLLE ESLLEKHLRK PCPDPAPVQL IVQFLEQASK PSVNEQNQVQ PPPDNKRNRI LKLLALKVAA HLKWDLDILE KSLSVPVLNM LLNELLCISK VPPGTKHVDM DLATLPPTTA MAVLLYNRWA IRTIVQSSFP VKQAKPGPPQ LSVMNQMQQE KELTENILKV LKEQAADSIL VLEAALKLNK DLYVHTMRTL DLLAMEPGMV NGETESSTAG LKVKTEEMQC QVCYDLGAAY FQQGSTNSAV YENAREKFFR TKELIAEIGS LSLHCTIDEK RLAGYCQACD VLVPSSDSTS QQLTPYSQVH ICLRSGNYQE VIQIFIEDNL TLSLPVQFRQ SVLRELFKKA QQGNEALDEI CFKVCACNTV RDILEGRTIS VQFNQLFLRP NKEKIDFLLE VCSRSVNLEK ASESLKGNMA AFLKNVCLGL EDLQYVFMIS SHELFITLLK DEERKLLVDQ MRKRSPRVNL CIKPVTSFYD IPASASVNIG QLEHQLILSV DPWRIRQILI ELHGMTSERQ FWTVSNKWEV PSVYSGVILG IKDNLTRDLV YILMAKGLHC STVKDFSHAK QLFAACLELV TEFSPKLRQV MLNEMLLLDI HTHEAGTGQA GERPPSDLIS RVRGYLEMRL PDIPLRQVIA EECVAFMLNW RENEYLTLQV PAFLLQSNPY VKLGQLLAAT CKELPGPKES RRTAKDLWEV VVQICSVSSQ HKRGNDGRVS LIKQRESTLG IMYRSELLSF IKKLREPLVL TIILSLFVKL HNVREDIVND ITAEHISIWP SSIPNLQSVD FEAVAITVKE LVRYTLSINP NNHSWLIIQA DIYFATNQYS AALHYYLQAG AVCSDFFNKA VPPDVYTDQV IKRMIKCCSL LNCHTQVAIL CQFLREIDYK TAFKSLQEQN SHDAMDSYYD YIWDVTILEY LTYLHHKRGE TDKRQIAIKA IGQTELNASN PEEVLQLAAQ RRKKKFLQAM AKLYF //