ATG12_YEAST
ID ATG12_YEAST Reviewed; 186 AA.
AC P38316; D6VQL3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ubiquitin-like protein ATG12;
DE AltName: Full=Autophagy-related protein 12;
GN Name=ATG12; Synonyms=APG12; OrderedLocusNames=YBR217W; ORFNames=YBR1506;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, CONJUGATION
RP TO ATG5, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-186.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=9759731; DOI=10.1038/26506;
RA Mizushima N., Noda T., Yoshimori T., Tanaka Y., Ishii T., George M.D.,
RA Klionsky D.J., Ohsumi M., Ohsumi Y.;
RT "A protein conjugation system essential for autophagy.";
RL Nature 395:395-398(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=8224160; DOI=10.1016/0014-5793(93)80398-e;
RA Tsukada M., Ohsumi Y.;
RT "Isolation and characterization of autophagy-defective mutants of
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 333:169-174(1993).
RN [6]
RP INTERACTION WITH ATG10.
RX PubMed=10508157; DOI=10.1093/emboj/18.19.5234;
RA Shintani T., Mizushima N., Ogawa Y., Matsuura A., Noda T., Ohsumi Y.;
RT "Apg10p, a novel protein-conjugating enzyme essential for autophagy in
RT yeast.";
RL EMBO J. 18:5234-5241(1999).
RN [7]
RP INTERACTION WITH ATG7.
RX PubMed=10233150; DOI=10.1091/mbc.10.5.1367;
RA Tanida I., Mizushima N., Kiyooka M., Ohsumi M., Ueno T., Ohsumi Y.,
RA Kominami E.;
RT "Apg7p/Cvt2p: a novel protein-activating enzyme essential for autophagy.";
RL Mol. Biol. Cell 10:1367-1379(1999).
RN [8]
RP INTERACTION WITH ATG5, AND SUBCELLULAR LOCATION.
RX PubMed=10712513; DOI=10.1091/mbc.11.3.969;
RA George M.D., Baba M., Scott S.V., Mizushima N., Garrison B.S., Ohsumi Y.,
RA Klionsky D.J.;
RT "Apg5p functions in the sequestration step in the cytoplasm-to-vacuole
RT targeting and macroautophagy pathways.";
RL Mol. Biol. Cell 11:969-982(2000).
RN [9]
RP FUNCTION.
RX PubMed=11689437; DOI=10.1093/emboj/20.21.5971;
RA Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.;
RT "The pre-autophagosomal structure organized by concerted functions of APG
RT genes is essential for autophagosome formation.";
RL EMBO J. 20:5971-5981(2001).
RN [10]
RP INTERACTION WITH ATG7.
RX PubMed=11139573; DOI=10.1074/jbc.m007737200;
RA Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.;
RT "The C-terminal region of an Apg7p/Cvt2p is required for homodimerization
RT and is essential for its E1 activity and E1-E2 complex formation.";
RL J. Biol. Chem. 276:9846-9854(2001).
RN [11]
RP FUNCTION.
RX PubMed=11149920; DOI=10.1083/jcb.152.1.51;
RA Kim J., Huang W.-P., Klionsky D.J.;
RT "Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole
RT targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation
RT complex.";
RL J. Cell Biol. 152:51-64(2001).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH ATG5 AND ATG16.
RX PubMed=11897782; DOI=10.1074/jbc.m111889200;
RA Kuma A., Mizushima N., Ishihara N., Ohsumi Y.;
RT "Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric
RT complex, mediated by Apg16 oligomerization, is essential for autophagy in
RT yeast.";
RL J. Biol. Chem. 277:18619-18625(2002).
RN [13]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
RN [14]
RP CONJUGATION TO ATG5.
RX PubMed=12965207; DOI=10.1016/s0014-5793(03)00899-8;
RA Yamazaki-Sato H., Tanida I., Ueno T., Kominami E.;
RT "The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8
RT lipidation, but not for Apg12 conjugation.";
RL FEBS Lett. 551:71-77(2003).
RN [15]
RP FUNCTION, CONJUGATION TO ATG5, AND MUTAGENESIS OF ILE-106; PHE-108; TYR-149
RP AND PHE-154.
RX PubMed=16874032; DOI=10.4161/auto.1.2.1858;
RA Hanada T., Ohsumi Y.;
RT "Structure-function relationship of Atg12, a ubiquitin-like modifier
RT essential for autophagy.";
RL Autophagy 1:110-118(2005).
RN [16]
RP FUNCTION.
RX PubMed=16901900; DOI=10.1074/jbc.m607007200;
RA Yorimitsu T., Nair U., Yang Z., Klionsky D.J.;
RT "Endoplasmic reticulum stress triggers autophagy.";
RL J. Biol. Chem. 281:30299-30304(2006).
RN [17]
RP FUNCTION.
RX PubMed=17404498; DOI=10.4161/auto.4127;
RA Zhang Y., Qi H., Taylor R., Xu W., Liu L.F., Jin S.;
RT "The role of autophagy in mitochondria maintenance: characterization of
RT mitochondrial functions in autophagy-deficient S. cerevisiae strains.";
RL Autophagy 3:337-346(2007).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17295840; DOI=10.1111/j.1365-2443.2007.01050.x;
RA Suzuki K., Kubota Y., Sekito T., Ohsumi Y.;
RT "Hierarchy of Atg proteins in pre-autophagosomal structure organization.";
RL Genes Cells 12:209-218(2007).
RN [19]
RP FUNCTION OF THE ATG12-ATG5 CONJUGATE, AND INTERACTION WITH ATG3.
RX PubMed=17986448; DOI=10.1074/jbc.c700195200;
RA Hanada T., Noda N.N., Satomi Y., Ichimura Y., Fujioka Y., Takao T.,
RA Inagaki F., Ohsumi Y.;
RT "The Atg12-Atg5 conjugate has a novel E3-like activity for protein
RT lipidation in autophagy.";
RL J. Biol. Chem. 282:37298-37302(2007).
RN [20]
RP FUNCTION.
RX PubMed=18971623; DOI=10.4161/auto.6962;
RA Cao Y., Klionsky D.J.;
RT "New insights into autophagy using a multiple knockout strain.";
RL Autophagy 4:1073-1075(2008).
RN [21]
RP CONJUGATION TO ATG5, AND FUNCTION OF THE ATG12-ATG5 CONJUGATE.
RX PubMed=18725539; DOI=10.1083/jcb.200801035;
RA Cao Y., Cheong H., Song H., Klionsky D.J.;
RT "In vivo reconstitution of autophagy in Saccharomyces cerevisiae.";
RL J. Cell Biol. 182:703-713(2008).
RN [22]
RP CRYSTALLIZATION OF THE ATG12-ATG5 CONJUGATE BOUND TO ATG16.
RX PubMed=18421155; DOI=10.1107/s0909049507054799;
RA Noda N.N., Fujioka Y., Ohsumi Y., Inagaki F.;
RT "Crystallization of the Atg12-Atg5 conjugate bound to Atg16 by the free-
RT interface diffusion method.";
RL J. Synchrotron Radiat. 15:266-268(2008).
RN [23]
RP FUNCTION.
RX PubMed=18701704; DOI=10.1091/mbc.e08-04-0363;
RA Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L.,
RA Millen J., Goldfarb D.S., Thumm M.;
RT "Piecemeal microautophagy of the nucleus requires the core macroautophagy
RT genes.";
RL Mol. Biol. Cell 19:4492-4505(2008).
RN [24]
RP INTERACTION WITH COG2.
RX PubMed=20065092; DOI=10.1083/jcb.200904075;
RA Yen W.L., Shintani T., Nair U., Cao Y., Richardson B.C., Li Z.,
RA Hughson F.M., Baba M., Klionsky D.J.;
RT "The conserved oligomeric Golgi complex is involved in double-membrane
RT vesicle formation during autophagy.";
RL J. Cell Biol. 188:101-114(2010).
RN [25]
RP CONJUGATION TO ATG5.
RX PubMed=21703229; DOI=10.1016/j.bbrc.2011.06.061;
RA Yamagata M., Obara K., Kihara A.;
RT "Sphingolipid synthesis is involved in autophagy in Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 410:786-791(2011).
RN [26]
RP SUBCELLULAR LOCATION, AND FUNCTION OF THE ATG5-ATG12/ATG16 COMPLEX.
RX PubMed=23064152; DOI=10.1038/emboj.2012.278;
RA Romanov J., Walczak M., Ibiricu I., Schuchner S., Ogris E., Kraft C.,
RA Martens S.;
RT "Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16
RT complex during autophagosome formation.";
RL EMBO J. 31:4304-4317(2012).
RN [27]
RP FUNCTION.
RX PubMed=22768199; DOI=10.1371/journal.pone.0040013;
RA Mijaljica D., Prescott M., Devenish R.J.;
RT "A late form of nucleophagy in Saccharomyces cerevisiae.";
RL PLoS ONE 7:E40013-E40013(2012).
RN [28]
RP SUBCELLULAR LOCATION.
RX PubMed=23549786; DOI=10.1242/jcs.122960;
RA Suzuki K., Akioka M., Kondo-Kakuta C., Yamamoto H., Ohsumi Y.;
RT "Fine mapping of autophagy-related proteins during autophagosome formation
RT in Saccharomyces cerevisiae.";
RL J. Cell Sci. 126:2534-2544(2013).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 100-186 IN CONJUGATION WITH ATG5.
RX PubMed=23238393; DOI=10.1038/embor.2012.208;
RA Noda N.N., Fujioka Y., Hanada T., Ohsumi Y., Inagaki F.;
RT "Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating
RT Atg8-PE conjugation.";
RL EMBO Rep. 14:206-211(2013).
CC -!- FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole
CC transport (Cvt), autophagy vesicles formation, mitophagy, and
CC nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating
CC system involving also ATG7 as an E1-like activating enzyme and ATG10 as
CC an E2-like conjugating enzyme, is essential for its function. The
CC ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for
CC lipidation of ATG8 and ATG8 association to the vesicle membranes.
CC ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2
CC activity. {ECO:0000269|PubMed:11149920, ECO:0000269|PubMed:11689437,
CC ECO:0000269|PubMed:16874032, ECO:0000269|PubMed:16901900,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:17404498,
CC ECO:0000269|PubMed:17986448, ECO:0000269|PubMed:18701704,
CC ECO:0000269|PubMed:18725539, ECO:0000269|PubMed:18971623,
CC ECO:0000269|PubMed:22768199, ECO:0000269|PubMed:23064152,
CC ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:9759731}.
CC -!- SUBUNIT: Forms a conjugate with ATG5. Forms a thioester bond with the
CC 'Cys-133' of ATG10. Interacts with the ATG7 C-terminal 40 amino acids
CC domain. The ATG12-ATG5 conjugate forms a complex with several units of
CC ATG16. The ATG12-ATG5 conjugate associates also with ATG3. Interacts
CC with COG2. {ECO:0000269|PubMed:10233150, ECO:0000269|PubMed:10508157,
CC ECO:0000269|PubMed:10712513, ECO:0000269|PubMed:11139573,
CC ECO:0000269|PubMed:11897782, ECO:0000269|PubMed:17986448,
CC ECO:0000269|PubMed:20065092}.
CC -!- INTERACTION:
CC P38316; Q03818: ATG16; NbExp=10; IntAct=EBI-2692, EBI-27344;
CC P38316; Q12380: ATG5; NbExp=9; IntAct=EBI-2692, EBI-2664;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:10712513, ECO:0000269|PubMed:17295840,
CC ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23549786,
CC ECO:0000269|PubMed:9759731}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10712513, ECO:0000269|PubMed:17295840,
CC ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23549786,
CC ECO:0000269|PubMed:9759731}. Note=Localizes to the isolation membrane
CC (IM), a membrane sac which is generated from the pre-autophagosomal
CC structure (PAS). Ultimately, the IM expands to become a mature
CC autophagosome. Localizes also to a dot at the junction between the IM
CC and the vacuolar membrane, termed the vacuole-IM contact site (VICS).
CC -!- MISCELLANEOUS: Small amount of ATG5-ATG12 conjugate is enough to
CC perform normal autophagy.
CC -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
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DR EMBL; AB017924; BAA33473.1; -; Genomic_DNA.
DR EMBL; Z36086; CAA85181.1; -; Genomic_DNA.
DR EMBL; AY557706; AAS56032.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07333.1; -; Genomic_DNA.
DR PIR; S46093; S46093.
DR RefSeq; NP_009776.1; NM_001178565.1.
DR PDB; 3W1S; X-ray; 2.60 A; C=100-186.
DR PDBsum; 3W1S; -.
DR AlphaFoldDB; P38316; -.
DR SMR; P38316; -.
DR BioGRID; 32914; 220.
DR ComplexPortal; CPX-1848; ATG12-ATG5 complex.
DR ComplexPortal; CPX-1849; ATG12-ATG5-ATG16 complex.
DR DIP; DIP-1189N; -.
DR IntAct; P38316; 139.
DR MINT; P38316; -.
DR STRING; 4932.YBR217W; -.
DR iPTMnet; P38316; -.
DR PaxDb; P38316; -.
DR PRIDE; P38316; -.
DR EnsemblFungi; YBR217W_mRNA; YBR217W; YBR217W.
DR GeneID; 852518; -.
DR KEGG; sce:YBR217W; -.
DR SGD; S000000421; ATG12.
DR VEuPathDB; FungiDB:YBR217W; -.
DR eggNOG; KOG3439; Eukaryota.
DR GeneTree; ENSGT00390000016654; -.
DR HOGENOM; CLU_106795_0_0_1; -.
DR InParanoid; P38316; -.
DR OMA; YCYINNS; -.
DR BioCyc; YEAST:G3O-29154-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:P38316; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38316; protein.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0000407; C:phagophore assembly site; IC:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:1990234; C:transferase complex; IDA:ComplexPortal.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0031386; F:protein tag; IPI:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IMP:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0006501; P:C-terminal protein lipidation; IDA:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IDA:ComplexPortal.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0006497; P:protein lipidation; IDA:ComplexPortal.
DR GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IMP:SGD.
DR IDEAL; IID50208; -.
DR InterPro; IPR007242; Atg12.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13385; PTHR13385; 1.
DR Pfam; PF04110; APG12; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Isopeptide bond; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation pathway.
FT CHAIN 1..186
FT /note="Ubiquitin-like protein ATG12"
FT /id="PRO_0000212485"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-149 in ATG5)"
FT MUTAGEN 106
FT /note="I->A: Decreases protein stability."
FT /evidence="ECO:0000269|PubMed:16874032"
FT MUTAGEN 108
FT /note="F->A: Decreases protein stability."
FT /evidence="ECO:0000269|PubMed:16874032"
FT MUTAGEN 149
FT /note="Y->A: Impairs conjugation to ATG5 and autophagic
FT activity."
FT /evidence="ECO:0000269|PubMed:16874032"
FT MUTAGEN 154
FT /note="F->A: Impairs conjugation to ATG5 and autophagic
FT activity."
FT /evidence="ECO:0000269|PubMed:16874032"
FT MUTAGEN 186
FT /note="G->A: Strong decrease of conjugation with ATG5."
FT /evidence="ECO:0000269|PubMed:9759731"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:3W1S"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3W1S"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:3W1S"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3W1S"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:3W1S"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:3W1S"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:3W1S"
SQ SEQUENCE 186 AA; 21106 MW; 74B3C9FD3CEA9265 CRC64;
MSRILESENE TESDESSIIS TNNGTAMERS RNNQELRSSP HTVQNRLELF SRRLSQLGLA
SDISVDQQVE DSSSGTYEQE ETIKTNAQTS KQKSHKDEKN IQKIQIKFQP IGSIGQLKPS
VCKISMSQSF AMVILFLKRR LKMDHVYCYI NNSFAPSPQQ NIGELWMQFK TNDELIVSYC
ASVAFG
