COPE_HUMAN
ID COPE_HUMAN Reviewed; 308 AA.
AC O14579; A6NE29; A6NKA3; O76097; Q6IBB8; Q9UGP6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Coatomer subunit epsilon;
DE AltName: Full=Epsilon-coat protein;
DE Short=Epsilon-COP;
GN Name=COPE;
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], AND VARIANT ILE-117.
RC TISSUE=Brain;
RX PubMed=10469566; DOI=10.1016/s0960-9822(99)80365-0;
RA Shima D.T., Scales S.J., Kreis T.E., Pepperkok R.;
RT "Segregation of COPI-rich and anterograde-cargo-rich domains in
RT endoplasmic-reticulum-to-Golgi transport complexes.";
RL Curr. Biol. 9:821-824(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Baehr C., Herzog A., Haeussermann S., Marks F., Gschwendt M.;
RT "Cloning, expression, and phosphorylation by protein kinase A of human
RT epsilon-COP.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-117.
RC TISSUE=Testis, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Embryonic carcinoma, Lymph, and Skin;
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 PROTEIN SEQUENCE OF 2-23; 66-85 AND 172-211, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP UBIQUITINATION BY RCHY1.
RX PubMed=17721809; DOI=10.1007/s11010-007-9586-3;
RA Maruyama S., Miyajima N., Bohgaki M., Tsukiyama T., Shigemura M.,
RA Nonomura K., Hatakeyama S.;
RT "Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of
RT PSA.";
RL Mol. Cell. Biochem. 307:73-82(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-45 AND SER-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
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).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC dilysine motifs and reversibly associates with Golgi non-clathrin-
CC coated vesicles, which further mediate biosynthetic protein transport
CC from the ER, via the Golgi up to the trans Golgi network. The coatomer
CC complex is required for budding from Golgi membranes, and is essential
CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC In mammals, the coatomer can only be recruited by membranes associated
CC with ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC -!- INTERACTION:
CC O14579; Q9UKI2: CDC42EP3; NbExp=3; IntAct=EBI-711301, EBI-723480;
CC O14579; Q5JST6: EFHC2; NbExp=6; IntAct=EBI-711301, EBI-2349927;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC originating from it. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14579-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14579-2; Sequence=VSP_042770, VSP_042771;
CC Name=3;
CC IsoId=O14579-3; Sequence=VSP_045070;
CC -!- PTM: Phosphorylated by PKA.
CC -!- PTM: Polyubiquitinated by RCHY1 in the presence of androgen, leading to
CC proteasomal degradation. {ECO:0000269|PubMed:17721809}.
CC -!- SIMILARITY: Belongs to the COPE family. {ECO:0000305}.
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DR EMBL; AJ131182; CAA10316.1; -; mRNA.
DR EMBL; AJ249366; CAB55628.1; -; mRNA.
DR EMBL; AL136928; CAB66862.1; -; mRNA.
DR EMBL; AK126476; BAG54333.1; -; mRNA.
DR EMBL; AK315281; BAG37690.1; -; mRNA.
DR EMBL; CR456886; CAG33167.1; -; mRNA.
DR EMBL; AC002985; AAB81543.1; -; Genomic_DNA.
DR EMBL; AC005197; AAC24612.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84749.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84752.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84756.1; -; Genomic_DNA.
DR EMBL; BC003155; AAH03155.1; -; mRNA.
DR EMBL; BC007250; AAH07250.1; -; mRNA.
DR EMBL; BC017285; AAH17285.1; -; mRNA.
DR EMBL; BM454494; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS12387.1; -. [O14579-1]
DR CCDS; CCDS12388.1; -. [O14579-2]
DR CCDS; CCDS12389.1; -. [O14579-3]
DR RefSeq; NP_009194.2; NM_007263.3. [O14579-1]
DR RefSeq; NP_955474.1; NM_199442.1. [O14579-2]
DR RefSeq; NP_955476.1; NM_199444.1. [O14579-3]
DR PDB; 6TZT; X-ray; 3.06 A; A/C=1-308.
DR PDB; 6U3V; X-ray; 2.96 A; A/C=1-308.
DR PDBsum; 6TZT; -.
DR PDBsum; 6U3V; -.
DR AlphaFoldDB; O14579; -.
DR SMR; O14579; -.
DR BioGRID; 116447; 218.
DR IntAct; O14579; 54.
DR MINT; O14579; -.
DR STRING; 9606.ENSP00000262812; -.
DR iPTMnet; O14579; -.
DR MetOSite; O14579; -.
DR PhosphoSitePlus; O14579; -.
DR SwissPalm; O14579; -.
DR BioMuta; COPE; -.
DR OGP; O14579; -.
DR EPD; O14579; -.
DR jPOST; O14579; -.
DR MassIVE; O14579; -.
DR MaxQB; O14579; -.
DR PaxDb; O14579; -.
DR PeptideAtlas; O14579; -.
DR PRIDE; O14579; -.
DR ProteomicsDB; 48098; -. [O14579-1]
DR ProteomicsDB; 48099; -. [O14579-2]
DR ProteomicsDB; 957; -.
DR Antibodypedia; 28232; 180 antibodies from 28 providers.
DR DNASU; 11316; -.
DR Ensembl; ENST00000262812.9; ENSP00000262812.3; ENSG00000105669.14. [O14579-1]
DR Ensembl; ENST00000349893.8; ENSP00000343134.3; ENSG00000105669.14. [O14579-3]
DR Ensembl; ENST00000351079.8; ENSP00000345674.3; ENSG00000105669.14. [O14579-2]
DR GeneID; 11316; -.
DR KEGG; hsa:11316; -.
DR MANE-Select; ENST00000262812.9; ENSP00000262812.3; NM_007263.4; NP_009194.2.
DR UCSC; uc002nkk.4; human. [O14579-1]
DR CTD; 11316; -.
DR DisGeNET; 11316; -.
DR GeneCards; COPE; -.
DR HGNC; HGNC:2234; COPE.
DR HPA; ENSG00000105669; Low tissue specificity.
DR MIM; 606942; gene.
DR neXtProt; NX_O14579; -.
DR OpenTargets; ENSG00000105669; -.
DR PharmGKB; PA26750; -.
DR VEuPathDB; HostDB:ENSG00000105669; -.
DR eggNOG; KOG3081; Eukaryota.
DR GeneTree; ENSGT00390000003478; -.
DR HOGENOM; CLU_049363_0_0_1; -.
DR InParanoid; O14579; -.
DR OMA; MIVLSQH; -.
DR OrthoDB; 303947at2759; -.
DR PhylomeDB; O14579; -.
DR TreeFam; TF313390; -.
DR PathwayCommons; O14579; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; O14579; -.
DR BioGRID-ORCS; 11316; 734 hits in 1073 CRISPR screens.
DR ChiTaRS; COPE; human.
DR GeneWiki; COPE_(gene); -.
DR GenomeRNAi; 11316; -.
DR Pharos; O14579; Tbio.
DR PRO; PR:O14579; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14579; protein.
DR Bgee; ENSG00000105669; Expressed in right testis and 197 other tissues.
DR ExpressionAtlas; O14579; baseline and differential.
DR Genevisible; O14579; HS.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0099612; P:protein localization to axon; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006822; Coatomer_esu.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10805; PTHR10805; 1.
DR PIRSF; PIRSF016478; Coatomer_esu; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9"
FT CHAIN 2..308
FT /note="Coatomer subunit epsilon"
FT /id="PRO_0000193851"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 97
FT /note="R -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042770"
FT VAR_SEQ 98..148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042771"
FT VAR_SEQ 194..245
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045070"
FT VARIANT 13
FT /note="S -> C (in dbSNP:rs2231987)"
FT /id="VAR_054032"
FT VARIANT 117
FT /note="T -> I (in dbSNP:rs10330)"
FT /evidence="ECO:0000269|PubMed:10469566,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_054033"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:6U3V"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:6U3V"
FT HELIX 286..304
FT /evidence="ECO:0007829|PDB:6U3V"
SQ SEQUENCE 308 AA; 34482 MW; A71146F3332F6BA9 CRC64;
MAPPAPGPAS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPERDV ERDVFLYRAY
LAQRKFGVVL DEIKPSSAPE LQAVRMFADY LAHESRRDSI VAELDREMSR SVDVTNTTFL
LMAASIYLHD QNPDAALRAL HQGDSLECTA MTVQILLKLD RLDLARKELK RMQDLDEDAT
LTQLATAWVS LATGGEKLQD AYYIFQEMAD KCSPTLLLLN GQAACHMAQG RWEAAEGLLQ
EALDKDSGYP ETLVNLIVLS QHLGKPPEVT NRYLSQLKDA HRSHPFIKEY QAKENDFDRL
VLQYAPSA
