ID MEMO1_HUMAN Reviewed; 297 AA. AC Q9Y316; B4DLS0; D6W575; Q5R2V8; Q5R2V9; Q6NSL5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=Protein MEMO1; DE AltName: Full=C21orf19-like protein; DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 7; DE Short=HCV NS5A-transactivated protein 7; DE AltName: Full=Mediator of ErbB2-driven cell motility 1; DE Short=Mediator of cell motility 1; DE Short=Memo-1; GN Name=MEMO1; Synonyms=C2orf4, MEMO, NS5ATP7; ORFNames=CGI-27; 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). RX PubMed=11707072; DOI=10.1006/geno.2001.6640; RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S., RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.; RT "From PREDs and open reading frames to cDNA isolation: revisiting the human RT chromosome 21 transcription map."; RL Genomics 78:46-54(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Heart, and Skeletal muscle; RA Shibuya K., Kudoh J., Shimizu N.; RT "Cloning of two isoforms of C2orf4 gene."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.; RT "Cloning and identification of human gene 7 transactivated by hepatitis C RT virus NS5A protein."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-cell, PNS, and Testis; 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 [9] RP FUNCTION, AND INTERACTION WITH ERBB2. RX PubMed=15156151; DOI=10.1038/ncb1134; RA Marone R., Hess D., Dankort D., Muller W.J., Hynes N.E., Badache A.; RT "Memo mediates ErbB2-driven cell motility."; RL Nat. Cell Biol. 6:515-522(2004). RN [10] RP FUNCTION. RX PubMed=20937854; DOI=10.1073/pnas.1000975107; RA Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.; RT "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the RT plasma membrane of migrating cells."; RL Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-297, INTERACTION WITH ERBB2, AND RP MUTAGENESIS OF TRP-16; HIS-49; TYR-54; HIS-81; HIS-192 AND CYS-244. RX PubMed=18045866; DOI=10.1074/jbc.m703523200; RA Qiu C., Lienhard S., Hynes N.E., Badache A., Leahy D.J.; RT "Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived RT phosphopeptide in its vestigial active site."; RL J. Biol. Chem. 283:2734-2740(2008). CC -!- FUNCTION: May control cell migration by relaying extracellular CC chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 CC signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important CC role in ERBB2-dependent stabilization of microtubules at the cell CC cortex. It controls the localization of APC and CLASP2 to the cell CC membrane, via the regulation of GSK3B activity. In turn, membrane-bound CC APC allows the localization of the MACF1 to the cell membrane, which is CC required for microtubule capture and stabilization. Is required for CC breast carcinoma cell migration. {ECO:0000269|PubMed:15156151, CC ECO:0000269|PubMed:20937854}. CC -!- SUBUNIT: Interacts with ERBB2 phosphorylated on 'Tyr-1248'. CC {ECO:0000269|PubMed:15156151, ECO:0000269|PubMed:18045866}. CC -!- INTERACTION: CC Q9Y316; O94983-5: CAMTA2; NbExp=3; IntAct=EBI-1104564, EBI-10176008; CC Q9Y316; Q8WUE5: CT55; NbExp=3; IntAct=EBI-1104564, EBI-6873363; CC Q9Y316; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1104564, EBI-742054; CC Q9Y316; Q9NT22: EMILIN3; NbExp=3; IntAct=EBI-1104564, EBI-3197883; CC Q9Y316; P04626: ERBB2; NbExp=6; IntAct=EBI-1104564, EBI-641062; CC Q9Y316; Q9UJY4: GGA2; NbExp=3; IntAct=EBI-1104564, EBI-447646; CC Q9Y316; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-1104564, EBI-739832; CC Q9Y316; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1104564, EBI-741037; CC Q9Y316; Q8IUH3: RBM45; NbExp=3; IntAct=EBI-1104564, EBI-2512147; CC Q9Y316; Q04864: REL; NbExp=3; IntAct=EBI-1104564, EBI-307352; CC Q9Y316; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-1104564, EBI-746118; CC Q9Y316; O75410: TACC1; NbExp=4; IntAct=EBI-1104564, EBI-624237; CC Q9Y316; O75410-7: TACC1; NbExp=3; IntAct=EBI-1104564, EBI-12007872; CC Q9Y316; P15884: TCF4; NbExp=3; IntAct=EBI-1104564, EBI-533224; CC Q9Y316; P15884-3: TCF4; NbExp=3; IntAct=EBI-1104564, EBI-13636688; CC Q9Y316; P14373: TRIM27; NbExp=3; IntAct=EBI-1104564, EBI-719493; CC Q9Y316; Q15654: TRIP6; NbExp=3; IntAct=EBI-1104564, EBI-742327; CC Q9Y316; O15209: ZBTB22; NbExp=3; IntAct=EBI-1104564, EBI-723574; CC Q9Y316; Q8N720: ZNF655; NbExp=3; IntAct=EBI-1104564, EBI-625509; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Y316-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y316-2; Sequence=VSP_041092; CC Name=3; CC IsoId=Q9Y316-3; Sequence=VSP_047693; CC -!- SIMILARITY: Belongs to the MEMO1 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; AF363446; AAL34462.1; -; mRNA. DR EMBL; AB041018; BAD74066.1; -; mRNA. DR EMBL; AB041019; BAD74067.1; -; mRNA. DR EMBL; AF529368; AAQ09602.1; -; mRNA. DR EMBL; AF132961; AAD27736.1; -; mRNA. DR EMBL; AK297128; BAG59632.1; -; mRNA. DR EMBL; AL121652; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121655; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471053; EAX00467.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00469.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00470.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00472.1; -; Genomic_DNA. DR EMBL; BC018733; AAH18733.1; -; mRNA. DR EMBL; BC070046; AAH70046.1; -; mRNA. DR EMBL; BC094681; AAH94681.1; -; mRNA. DR CCDS; CCDS1776.1; -. [Q9Y316-1] DR CCDS; CCDS46255.1; -. [Q9Y316-2] DR RefSeq; NP_001131074.1; NM_001137602.2. [Q9Y316-2] DR RefSeq; NP_001288762.1; NM_001301833.1. [Q9Y316-1] DR RefSeq; NP_001288781.1; NM_001301852.1. DR RefSeq; NP_057039.1; NM_015955.3. [Q9Y316-1] DR RefSeq; XP_011531194.1; XM_011532892.2. DR RefSeq; XP_016859744.1; XM_017004255.1. DR PDB; 3BCZ; X-ray; 2.10 A; A/B/C/D=5-297. DR PDB; 3BD0; X-ray; 3.01 A; A/B/C/D=5-297. DR PDB; 7KQ8; X-ray; 2.15 A; A/B/C/D=4-297. DR PDB; 7L5C; X-ray; 2.55 A; A/B/C/D=4-297. DR PDB; 7M8H; X-ray; 1.75 A; A/B/C/D=4-297. DR PDBsum; 3BCZ; -. DR PDBsum; 3BD0; -. DR PDBsum; 7KQ8; -. DR PDBsum; 7L5C; -. DR PDBsum; 7M8H; -. DR AlphaFoldDB; Q9Y316; -. DR SMR; Q9Y316; -. DR BioGRID; 119263; 62. DR CORUM; Q9Y316; -. DR IntAct; Q9Y316; 30. DR MINT; Q9Y316; -. DR STRING; 9606.ENSP00000295065; -. DR GlyGen; Q9Y316; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y316; -. DR PhosphoSitePlus; Q9Y316; -. DR BioMuta; MEMO1; -. DR DMDM; 7388490; -. DR EPD; Q9Y316; -. DR jPOST; Q9Y316; -. DR MassIVE; Q9Y316; -. DR MaxQB; Q9Y316; -. DR PaxDb; 9606-ENSP00000295065; -. DR PeptideAtlas; Q9Y316; -. DR ProteomicsDB; 63699; -. DR ProteomicsDB; 85960; -. [Q9Y316-1] DR ProteomicsDB; 85961; -. [Q9Y316-2] DR Pumba; Q9Y316; -. DR Antibodypedia; 47374; 180 antibodies from 26 providers. DR DNASU; 51072; -. DR Ensembl; ENST00000295065.9; ENSP00000295065.4; ENSG00000162959.14. [Q9Y316-1] DR Ensembl; ENST00000379383.7; ENSP00000368691.3; ENSG00000162959.14. [Q9Y316-3] DR Ensembl; ENST00000404530.6; ENSP00000385557.1; ENSG00000162959.14. [Q9Y316-1] DR Ensembl; ENST00000426310.6; ENSP00000400795.2; ENSG00000162959.14. [Q9Y316-2] DR GeneID; 51072; -. DR KEGG; hsa:51072; -. DR MANE-Select; ENST00000404530.6; ENSP00000385557.1; NM_001301833.4; NP_001288762.1. DR UCSC; uc002rnx.4; human. [Q9Y316-1] DR AGR; HGNC:14014; -. DR CTD; 51072; -. DR DisGeNET; 51072; -. DR GeneCards; MEMO1; -. DR HGNC; HGNC:14014; MEMO1. DR HPA; ENSG00000162959; Low tissue specificity. DR MIM; 611786; gene. DR neXtProt; NX_Q9Y316; -. DR OpenTargets; ENSG00000162959; -. DR PharmGKB; PA162395745; -. DR VEuPathDB; HostDB:ENSG00000162959; -. DR eggNOG; KOG3086; Eukaryota. DR GeneTree; ENSGT00390000006408; -. DR HOGENOM; CLU_038085_0_1_1; -. DR InParanoid; Q9Y316; -. DR OMA; EQEAQYG; -. DR OrthoDB; 5486826at2759; -. DR PhylomeDB; Q9Y316; -. DR TreeFam; TF300014; -. DR PathwayCommons; Q9Y316; -. DR Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility. DR SignaLink; Q9Y316; -. DR BioGRID-ORCS; 51072; 42 hits in 675 CRISPR screens. DR ChiTaRS; MEMO1; human. DR EvolutionaryTrace; Q9Y316; -. DR GenomeRNAi; 51072; -. DR Pharos; Q9Y316; Tbio. DR PRO; PR:Q9Y316; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9Y316; Protein. DR Bgee; ENSG00000162959; Expressed in left testis and 98 other cell types or tissues. DR ExpressionAtlas; Q9Y316; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB. DR CDD; cd07361; MEMO_like; 1. DR Gene3D; 3.40.830.10; LigB-like; 1. DR HAMAP; MF_00055; MEMO1; 1. DR InterPro; IPR002737; MEMO1_fam. DR NCBIfam; TIGR04336; AmmeMemoSam_B; 1. DR PANTHER; PTHR11060; PROTEIN MEMO1; 1. DR PANTHER; PTHR11060:SF0; PROTEIN MEMO1; 1. DR Pfam; PF01875; Memo; 1. DR Genevisible; Q9Y316; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome. FT CHAIN 1..297 FT /note="Protein MEMO1" FT /id="PRO_0000134394" FT MOD_RES 210 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q91VH6" FT VAR_SEQ 1..20 FT /note="MSNRVVCREASHAGSWYTAS -> MPLWRADKCQDVQSASWRPRRAD (in FT isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_047693" FT VAR_SEQ 49..71 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041092" FT MUTAGEN 16 FT /note="W->A: Abolishes interaction with ERBB2." FT /evidence="ECO:0000269|PubMed:18045866" FT MUTAGEN 49 FT /note="H->A: Abolishes interaction with ERBB2." FT /evidence="ECO:0000269|PubMed:18045866" FT MUTAGEN 54 FT /note="Y->A: Diminishes interaction with ERBB2." FT /evidence="ECO:0000269|PubMed:18045866" FT MUTAGEN 81 FT /note="H->A: Abolishes interaction with ERBB2." FT /evidence="ECO:0000269|PubMed:18045866" FT MUTAGEN 192 FT /note="H->A: Abolishes interaction with ERBB2." FT /evidence="ECO:0000269|PubMed:18045866" FT MUTAGEN 244 FT /note="C->A: Abolishes interaction with ERBB2." FT /evidence="ECO:0000269|PubMed:18045866" FT CONFLICT 23 FT /note="Q -> H (in Ref. 8; AAH70046)" FT /evidence="ECO:0000305" FT CONFLICT 172 FT /note="L -> P (in Ref. 5; BAG59632)" FT /evidence="ECO:0000305" FT TURN 11..15 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 21..33 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 52..63 FT /evidence="ECO:0007829|PDB:7M8H" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 73..79 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 86..90 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 107..115 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 124..129 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 137..143 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 163..177 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 209..225 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 229..239 FT /evidence="ECO:0007829|PDB:7M8H" FT HELIX 246..261 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 266..277 FT /evidence="ECO:0007829|PDB:7M8H" FT STRAND 286..296 FT /evidence="ECO:0007829|PDB:7M8H" SQ SEQUENCE 297 AA; 33733 MW; E315FD5587776211 CRC64; MSNRVVCREA SHAGSWYTAS GPQLNAQLEG WLSQVQSTKR PARAIIAPHA GYTYCGSCAA HAYKQVDPSI TRRIFILGPS HHVPLSRCAL SSVDIYRTPL YDLRIDQKIY GELWKTGMFE RMSLQTDEDE HSIEMHLPYT AKAMESHKDE FTIIPVLVGA LSESKEQEFG KLFSKYLADP SNLFVVSSDF CHWGQRFRYS YYDESQGEIY RSIEHLDKMG MSIIEQLDPV SFSNYLKKYH NTICGRHPIG VLLNAITELQ KNGMNMSFSF LNYAQSSQCR NWQDSSVSYA AGALTVH //