YKT6_HUMAN
ID YKT6_HUMAN Reviewed; 198 AA.
AC O15498; B4DR94; Q53F01; Q6FGU9; Q6IB15;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Synaptobrevin homolog YKT6;
DE EC=2.3.1.- {ECO:0000269|PubMed:15479160};
DE Flags: Precursor;
GN Name=YKT6;
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), AND FUNCTION.
RC TISSUE=Pancreas;
RX PubMed=9211930; DOI=10.1074/jbc.272.28.17776;
RA McNew J.A., Soegaard M., Lampen N.M., Machida S., Ye R.R., Lacomis L.,
RA Tempst P., Rothman J.E., Soellner T.H.;
RT "Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi
RT transport.";
RL J. Biol. Chem. 272:17776-17783(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [8]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-42; CYS-194 AND CYS-195, AND
RP PALMITOYLATION AT CYS-194.
RX PubMed=15479160; DOI=10.1042/bj20041474;
RA Veit M.;
RT "The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal
RT cysteine residues.";
RL Biochem. J. 384:233-237(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=14742712; DOI=10.1091/mbc.e03-08-0625;
RA Volchuk A., Ravazzola M., Perrelet A., Eng W.S., Di Liberto M.,
RA Varlamov O., Fukasawa M., Engel T., Sollner T.H., Rothman J.E., Orci L.;
RT "Countercurrent distribution of two distinct SNARE complexes mediating
RT transport within the Golgi stack.";
RL Mol. Biol. Cell 15:1506-1518(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15215310; DOI=10.1091/mbc.e03-12-0876;
RA Tai G., Lu L., Wang T.L., Tang B.L., Goud B., Johannes L., Hong W.;
RT "Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport
RT from the early/recycling endosome to the trans-Golgi network.";
RL Mol. Biol. Cell 15:4011-4022(2004).
RN [11]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-42; CYS-194 AND CYS-195,
RP ISOPRENYLATION AT CYS-195, AND PALMITOYLATION.
RX PubMed=15044687; DOI=10.1073/pnas.0401183101;
RA Fukasawa M., Varlamov O., Eng W.S., Soellner T.H., Rothman J.E.;
RT "Localization and activity of the SNARE Ykt6 determined by its regulatory
RT domain and palmitoylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4815-4820(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Vesicular soluble NSF attachment protein receptor (v-SNARE)
CC mediating vesicle docking and fusion to a specific acceptor cellular
CC compartment. Functions in endoplasmic reticulum to Golgi transport; as
CC part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in
CC early/recycling endosome to TGN transport; as part of a SNARE complex
CC composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase
CC activity. {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:9211930}.
CC -!- SUBUNIT: Identified in 2 different SNARE complexes; the first one
CC composed of GOSR1, GOSR2 and STX5 and the second one composed of BET1L,
CC GOSR1 and STX5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasmic vesicle membrane;
CC Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor;
CC Cytoplasmic side. Note=Probably cycles through vesicles between Golgi
CC and endosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15498-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15498-2; Sequence=VSP_056071;
CC -!- DOMAIN: The longin domain regulates palmitoylation and membrane
CC targeting.
CC -!- PTM: Palmitoylated; catalyzes its own palmitoylation. Palmitoylation is
CC required for Golgi targeting. {ECO:0000269|PubMed:15044687,
CC ECO:0000269|PubMed:15479160}.
CC -!- PTM: Farnesylation is required for Golgi targeting.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; U95735; AAB81131.1; -; mRNA.
DR EMBL; BT007078; AAP35741.1; -; mRNA.
DR EMBL; AK299158; BAG61206.1; -; mRNA.
DR EMBL; CR456989; CAG33270.1; -; mRNA.
DR EMBL; CR542008; CAG46805.1; -; mRNA.
DR EMBL; AK223488; BAD97208.1; -; mRNA.
DR EMBL; AC006454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007319; AAH07319.1; -; mRNA.
DR CCDS; CCDS5482.1; -. [O15498-1]
DR CCDS; CCDS87497.1; -. [O15498-2]
DR RefSeq; NP_006546.1; NM_006555.3. [O15498-1]
DR RefSeq; XP_016867171.1; XM_017011682.1.
DR PDB; 6J74; X-ray; 3.21 A; C=1-198.
DR PDB; 6J7F; X-ray; 2.88 A; C=1-195.
DR PDB; 6J7X; X-ray; 2.75 A; C=1-198.
DR PDBsum; 6J74; -.
DR PDBsum; 6J7F; -.
DR PDBsum; 6J7X; -.
DR AlphaFoldDB; O15498; -.
DR SMR; O15498; -.
DR BioGRID; 115895; 217.
DR IntAct; O15498; 38.
DR MINT; O15498; -.
DR STRING; 9606.ENSP00000223369; -.
DR TCDB; 1.F.1.3.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; O15498; -.
DR PhosphoSitePlus; O15498; -.
DR SwissPalm; O15498; -.
DR BioMuta; YKT6; -.
DR EPD; O15498; -.
DR jPOST; O15498; -.
DR MassIVE; O15498; -.
DR MaxQB; O15498; -.
DR PaxDb; O15498; -.
DR PeptideAtlas; O15498; -.
DR PRIDE; O15498; -.
DR ProteomicsDB; 48697; -. [O15498-1]
DR ProteomicsDB; 4936; -.
DR TopDownProteomics; O15498-1; -. [O15498-1]
DR Antibodypedia; 27085; 73 antibodies from 17 providers.
DR DNASU; 10652; -.
DR Ensembl; ENST00000223369.3; ENSP00000223369.2; ENSG00000106636.9. [O15498-1]
DR Ensembl; ENST00000496112.5; ENSP00000420805.1; ENSG00000106636.9. [O15498-2]
DR Ensembl; ENST00000679020.1; ENSP00000504623.1; ENSG00000106636.9. [O15498-1]
DR GeneID; 10652; -.
DR KEGG; hsa:10652; -.
DR MANE-Select; ENST00000223369.3; ENSP00000223369.2; NM_006555.4; NP_006546.1.
DR UCSC; uc003tkm.4; human. [O15498-1]
DR CTD; 10652; -.
DR DisGeNET; 10652; -.
DR GeneCards; YKT6; -.
DR HGNC; HGNC:16959; YKT6.
DR HPA; ENSG00000106636; Low tissue specificity.
DR MIM; 606209; gene.
DR neXtProt; NX_O15498; -.
DR OpenTargets; ENSG00000106636; -.
DR PharmGKB; PA145007308; -.
DR VEuPathDB; HostDB:ENSG00000106636; -.
DR eggNOG; KOG0861; Eukaryota.
DR GeneTree; ENSGT00390000015164; -.
DR HOGENOM; CLU_074848_3_0_1; -.
DR InParanoid; O15498; -.
DR OMA; ITDHEYP; -.
DR PhylomeDB; O15498; -.
DR TreeFam; TF105606; -.
DR PathwayCommons; O15498; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; O15498; -.
DR BioGRID-ORCS; 10652; 750 hits in 1086 CRISPR screens.
DR ChiTaRS; YKT6; human.
DR GeneWiki; YKT6; -.
DR GenomeRNAi; 10652; -.
DR Pharos; O15498; Tbio.
DR PRO; PR:O15498; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O15498; protein.
DR Bgee; ENSG00000106636; Expressed in stromal cell of endometrium and 189 other tissues.
DR ExpressionAtlas; O15498; baseline and differential.
DR Genevisible; O15498; HS.
DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
DR GO; GO:0097441; C:basal dendrite; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:HGNC-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HGNC-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; ISS:HGNC-UCL.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:HGNC-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC-UCL.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:HGNC-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:HGNC-UCL.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:HGNC-UCL.
DR GO; GO:0006903; P:vesicle targeting; IDA:HGNC-UCL.
DR CDD; cd14824; Longin; 1.
DR CDD; cd15867; R-SNARE_YKT6; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR045848; R-SNARE_YKT6.
DR InterPro; IPR042855; V_SNARE_CC.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Lipoprotein;
KW Membrane; Methylation; Palmitate; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transferase; Transport.
FT CHAIN 1..195
FT /note="Synaptobrevin homolog YKT6"
FT /id="PRO_0000280709"
FT PROPEP 196..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396661"
FT DOMAIN 8..126
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 138..198
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 194
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:15479160"
FT LIPID 195
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:15044687"
FT VAR_SEQ 154..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056071"
FT MUTAGEN 42
FT /note="F->E: Increases palmitoylation. Targeted to Golgi
FT membranes. Targeted to Golgi and cytosol; when associated
FT with S-194. Targeted to cytosol; when associated with S-
FT 195."
FT /evidence="ECO:0000269|PubMed:15044687,
FT ECO:0000269|PubMed:15479160"
FT MUTAGEN 194
FT /note="C->S: Decreases palmitoylation by 55%. Prevents
FT palmitoylation; when associated with S-195. Targeted to
FT Golgi and cytosol; when associated with E-42."
FT /evidence="ECO:0000269|PubMed:15044687,
FT ECO:0000269|PubMed:15479160"
FT MUTAGEN 195
FT /note="C->S: Prevents farnesylation. Targeted to cytosol;
FT when associated with E-42. Decreases palmitoylation by 13%.
FT Prevents palmitoylation; when associated with S-194."
FT /evidence="ECO:0000269|PubMed:15044687,
FT ECO:0000269|PubMed:15479160"
FT CONFLICT 63
FT /note="D -> N (in Ref. 4; CAG46805)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="P -> L (in Ref. 5; BAD97208)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="M -> I (in Ref. 4; CAG33270)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6J74"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6J7X"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6J7X"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6J7X"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6J7X"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:6J7X"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6J7X"
FT TURN 140..144
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6J7X"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:6J7X"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:6J7X"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6J7X"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:6J7X"
FT TURN 187..191
FT /evidence="ECO:0007829|PDB:6J7X"
SQ SEQUENCE 198 AA; 22418 MW; 2AB0C12832D1B943 CRC64;
MKLYSLSVLY KGEAKVVLLK AAYDVSSFSF FQRSSVQEFM TFTSQLIVER SSKGTRASVK
EQDYLCHVYV RNDSLAGVVI ADNEYPSRVA FTLLEKVLDE FSKQVDRIDW PVGSPATIHY
PALDGHLSRY QNPREADPMT KVQAELDETK IILHNTMESL LERGEKLDDL VSKSEVLGTQ
SKAFYKTARK QNSCCAIM
