ATLA3_HUMAN
ID ATLA3_HUMAN Reviewed; 541 AA.
AC Q6DD88; Q8N7W5; Q9H8Q5; Q9UFL1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Atlastin-3;
DE EC=3.6.5.-;
GN Name=ATL3;
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].
RC TISSUE=Ovary, and Testis;
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 MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 IDENTIFICATION.
RX PubMed=14506257; DOI=10.1074/jbc.m306702200;
RA Zhu P.-P., Patterson A., Lavoie B., Stadler J., Shoeb M., Patel R.,
RA Blackstone C.;
RT "Cellular localization, oligomerization, and membrane association of the
RT hereditary spastic paraplegia 3A (SPG3A) protein atlastin.";
RL J. Biol. Chem. 278:49063-49071(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, 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 [6]
RP FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-73 AND
RP ARG-213, AND TISSUE SPECIFICITY.
RX PubMed=18270207; DOI=10.1093/hmg/ddn046;
RA Rismanchi N., Soderblom C., Stadler J., Zhu P.-P., Blackstone C.;
RT "Atlastin GTPases are required for Golgi apparatus and ER morphogenesis.";
RL Hum. Mol. Genet. 17:1591-1604(2008).
RN [7]
RP FUNCTION.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the tubular
RT ER network.";
RL Cell 138:549-561(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ZFYVE27.
RX PubMed=23969831; DOI=10.1073/pnas.1307391110;
RA Chang J., Lee S., Blackstone C.;
RT "Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and
RT regulates network formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT HSN1F CYS-192, AND
RP CHARACTERIZATION OF VARIANT HSN1F CYS-192.
RX PubMed=24459106; DOI=10.1093/brain/awt357;
RA Kornak U., Mademan I., Schinke M., Voigt M., Krawitz P., Hecht J.,
RA Barvencik F., Schinke T., Giesselmann S., Beil F.T., Pou-Serradell A.,
RA Vilchez J.J., Beetz C., Deconinck T., Timmerman V., Kaether C.,
RA De Jonghe P., Huebner C.A., Gal A., Amling M., Mundlos S., Baets J.,
RA Kurth I.;
RT "Sensory neuropathy with bone destruction due to a mutation in the
RT membrane-shaping atlastin GTPase 3.";
RL Brain 137:683-692(2014).
RN [13]
RP IDENTIFICATION BY 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 [14]
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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-73 AND ARG-213.
RX PubMed=27619977; DOI=10.7554/elife.18605;
RA Wang S., Tukachinsky H., Romano F.B., Rapoport T.A.;
RT "Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons
RT to generate a tubular membrane network.";
RL Elife 5:0-0(2016).
RN [16]
RP INTERACTION WITH REEP5.
RX PubMed=32075961; DOI=10.1038/s41467-019-14143-9;
RA Lee S.H., Hadipour-Lakmehsari S., Murthy H.R., Gibb N., Miyake T.,
RA Teng A.C.T., Cosme J., Yu J.C., Moon M., Lim S., Wong V., Liu P.,
RA Billia F., Fernandez-Gonzalez R., Stagljar I., Sharma P., Kislinger T.,
RA Scott I.C., Gramolini A.O.;
RT "REEP5 depletion causes sarco-endoplasmic reticulum vacuolization and
RT cardiac functional defects.";
RL Nat. Commun. 11:965-965(2020).
CC -!- FUNCTION: GTPase tethering membranes through formation of trans-
CC homooligomers and mediating homotypic fusion of endoplasmic reticulum
CC membranes. Functions in endoplasmic reticulum tubular network
CC biogenesis (PubMed:18270207, PubMed:19665976, PubMed:27619977).
CC {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976,
CC ECO:0000269|PubMed:27619977}.
CC -!- SUBUNIT: Interacts with ZFYVE27 (PubMed:23969831). Interacts with REEP5
CC (PubMed:32075961). {ECO:0000269|PubMed:23969831,
CC ECO:0000269|PubMed:32075961}.
CC -!- INTERACTION:
CC Q6DD88; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-6165882, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:24459106,
CC ECO:0000269|PubMed:27619977}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:24459106}.
CC Note=Localizes to endoplasmic reticulum tubules and accumulates in
CC punctuate structures corresponding to 3-way junctions, which represent
CC crossing-points at which the tubules build a polygonal network.
CC {ECO:0000269|PubMed:23969831, ECO:0000269|PubMed:24459106,
CC ECO:0000269|PubMed:27619977}.
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system and in
CC dorsal root ganglia neurons. Expressed in peripheral tissues (at
CC protein level). {ECO:0000269|PubMed:18270207,
CC ECO:0000269|PubMed:24459106}.
CC -!- DISEASE: Neuropathy, hereditary sensory, 1F (HSN1F) [MIM:615632]: An
CC autosomal dominant sensory neuropathy affecting the lower limbs. Distal
CC sensory impairment becomes apparent during the second or third decade
CC of life, resulting in painless ulceration of the feet with poor
CC healing, which can progress to osteomyelitis, bone destruction, and
CC amputation. There is no autonomic involvement, spasticity, or cognitive
CC impairment. {ECO:0000269|PubMed:24459106}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05111.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AK097588; BAC05111.1; ALT_SEQ; mRNA.
DR EMBL; AK023383; BAB14552.1; -; mRNA.
DR EMBL; AL117600; CAB56010.2; -; mRNA.
DR EMBL; BC077727; AAH77727.1; -; mRNA.
DR CCDS; CCDS41663.1; -.
DR PIR; T17320; T17320.
DR RefSeq; NP_001276977.1; NM_001290048.1.
DR RefSeq; NP_056274.3; NM_015459.4.
DR PDB; 5VGR; X-ray; 2.10 A; A/B=21-442.
DR PDB; 6XJO; X-ray; 2.10 A; A/B=1-334.
DR PDBsum; 5VGR; -.
DR PDBsum; 6XJO; -.
DR AlphaFoldDB; Q6DD88; -.
DR SMR; Q6DD88; -.
DR BioGRID; 117423; 188.
DR CORUM; Q6DD88; -.
DR IntAct; Q6DD88; 78.
DR MINT; Q6DD88; -.
DR STRING; 9606.ENSP00000381844; -.
DR TCDB; 9.B.390.1.2; the tmcc/tex28 (tm-tex) family.
DR GlyGen; Q6DD88; 1 site.
DR iPTMnet; Q6DD88; -.
DR MetOSite; Q6DD88; -.
DR PhosphoSitePlus; Q6DD88; -.
DR SwissPalm; Q6DD88; -.
DR BioMuta; ATL3; -.
DR DMDM; 74736374; -.
DR EPD; Q6DD88; -.
DR jPOST; Q6DD88; -.
DR MassIVE; Q6DD88; -.
DR MaxQB; Q6DD88; -.
DR PaxDb; Q6DD88; -.
DR PeptideAtlas; Q6DD88; -.
DR PRIDE; Q6DD88; -.
DR ProteomicsDB; 66223; -.
DR TopDownProteomics; Q6DD88; -.
DR Antibodypedia; 28987; 240 antibodies from 27 providers.
DR DNASU; 25923; -.
DR Ensembl; ENST00000398868.8; ENSP00000381844.3; ENSG00000184743.13.
DR GeneID; 25923; -.
DR KEGG; hsa:25923; -.
DR MANE-Select; ENST00000398868.8; ENSP00000381844.3; NM_015459.5; NP_056274.3.
DR UCSC; uc001nxk.2; human.
DR CTD; 25923; -.
DR DisGeNET; 25923; -.
DR GeneCards; ATL3; -.
DR HGNC; HGNC:24526; ATL3.
DR HPA; ENSG00000184743; Low tissue specificity.
DR MalaCards; ATL3; -.
DR MIM; 609369; gene.
DR MIM; 615632; phenotype.
DR neXtProt; NX_Q6DD88; -.
DR OpenTargets; ENSG00000184743; -.
DR Orphanet; 36386; Hereditary sensory and autonomic neuropathy type 1.
DR PharmGKB; PA164716353; -.
DR VEuPathDB; HostDB:ENSG00000184743; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000158566; -.
DR InParanoid; Q6DD88; -.
DR OMA; QYQKNME; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; Q6DD88; -.
DR TreeFam; TF105251; -.
DR PathwayCommons; Q6DD88; -.
DR SignaLink; Q6DD88; -.
DR BioGRID-ORCS; 25923; 23 hits in 1083 CRISPR screens.
DR ChiTaRS; ATL3; human.
DR GenomeRNAi; 25923; -.
DR Pharos; Q6DD88; Tbio.
DR PRO; PR:Q6DD88; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6DD88; protein.
DR Bgee; ENSG00000184743; Expressed in upper arm skin and 197 other tissues.
DR ExpressionAtlas; Q6DD88; baseline and differential.
DR Genevisible; Q6DD88; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR003191; Guanylate-bd/ATL_C.
DR InterPro; IPR036543; Guanylate-bd_C_sf.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF02841; GBP_C; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Endoplasmic reticulum;
KW GTP-binding; Hydrolase; Membrane; Neuropathy; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..541
FT /note="Atlastin-3"
FT /id="PRO_0000287109"
FT TOPO_DOM 1..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18270207"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18270207"
FT DOMAIN 57..305
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT BINDING 67..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 114..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 213..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 272..275
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 391
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 192
FT /note="Y -> C (in HSN1F; causes mislocalization of the
FT protein; the mutant protein accumulates in condensed
FT structures near the nucleus and localizes to unbranched
FT tubules; has a dominant-negative disruptive effect on the
FT regular structure of the endoplasmic reticulum;
FT dbSNP:rs587777108)"
FT /evidence="ECO:0000269|PubMed:24459106"
FT /id="VAR_070973"
FT MUTAGEN 73
FT /note="K->A: Alters endoplasmic reticulum morphogenesis."
FT /evidence="ECO:0000269|PubMed:18270207,
FT ECO:0000269|PubMed:27619977"
FT MUTAGEN 213
FT /note="R->Q: Alters endoplasmic reticulum morphogenesis."
FT /evidence="ECO:0000269|PubMed:18270207,
FT ECO:0000269|PubMed:27619977"
FT CONFLICT 49
FT /note="I -> T (in Ref. 1; BAB14552)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> A (in Ref. 2; CAB56010)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="N -> S (in Ref. 1; BAC05111)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Q -> R (in Ref. 2; CAB56010)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="W -> R (in Ref. 2; CAB56010)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="N -> Y (in Ref. 2; CAB56010)"
FT /evidence="ECO:0000305"
FT HELIX 4..21
FT /evidence="ECO:0007829|PDB:6XJO"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6XJO"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:5VGR"
FT TURN 53..57
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 58..68
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6XJO"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:5VGR"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:5VGR"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:5VGR"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 340..371
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 380..400
FT /evidence="ECO:0007829|PDB:5VGR"
FT HELIX 407..434
FT /evidence="ECO:0007829|PDB:5VGR"
SQ SEQUENCE 541 AA; 60542 MW; E5C58A53F93B42D0 CRC64;
MLSPQRVAAA ASRGADDAME SSKPGPVQVV LVQKDQHSFE LDEKALASIL LQDHIRDLDV
VVVSVAGAFR KGKSFILDFM LRYLYSQKES GHSNWLGDPE EPLTGFSWRG GSDPETTGIQ
IWSEVFTVEK PGGKKVAVVL MDTQGAFDSQ STVKDCATIF ALSTMTSSVQ IYNLSQNIQE
DDLQQLQLFT EYGRLAMDEI FQKPFQTLMF LVRDWSFPYE YSYGLQGGMA FLDKRLQVKE
HQHEEIQNVR NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKDIAGEFK EQLQALIPYV
LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA NNLAAAASAK
DIYYNNMEEV CGGEKPYLSP DILEEKHCEF KQLALDHFKK TKKMGGKDFS FRYQQELEEE
IKELYENFCK HNGSKNVFST FRTPAVLFTG IVALYIASGL TGFIGLEVVA QLFNCMVGLL
LIALLTWGYI RYSGQYRELG GAIDFGAAYV LEQASSHIGN STQATVRDAV VGRPSMDKKA
Q
