MEMO1_HUMAN
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 03-AUG-2022, entry version 172.
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}.
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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; 56.
DR CORUM; Q9Y316; -.
DR IntAct; Q9Y316; 29.
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; Q9Y316; -.
DR PeptideAtlas; Q9Y316; -.
DR PRIDE; Q9Y316; -.
DR ProteomicsDB; 63699; -.
DR ProteomicsDB; 85960; -. [Q9Y316-1]
DR ProteomicsDB; 85961; -. [Q9Y316-2]
DR Antibodypedia; 47374; 167 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 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; 1057950at2759; -.
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; 30 hits in 601 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 96 other tissues.
DR ExpressionAtlas; Q9Y316; baseline and differential.
DR Genevisible; Q9Y316; HS.
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 HAMAP; MF_00055; MEMO1; 1.
DR InterPro; IPR002737; MEMO1_fam.
DR PANTHER; PTHR11060; PTHR11060; 1.
DR Pfam; PF01875; Memo; 1.
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:3BCZ"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:3BCZ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 209..225
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:3BCZ"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 266..277
FT /evidence="ECO:0007829|PDB:3BCZ"
FT STRAND 286..296
FT /evidence="ECO:0007829|PDB:3BCZ"
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
