STXB2_HUMAN
ID STXB2_HUMAN Reviewed; 593 AA.
AC Q15833; B4E175; E7EQD5; Q9BU65;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Syntaxin-binding protein 2;
DE AltName: Full=Protein unc-18 homolog 2;
DE Short=Unc18-2;
DE AltName: Full=Protein unc-18 homolog B;
DE Short=Unc-18B;
GN Name=STXBP2; Synonyms=UNC18B;
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 VARIANT VAL-526.
RX PubMed=8921365; DOI=10.1006/geno.1996.0515;
RA Ziegler S.F., Mortrud M.T., Swartz A.R., Baker E., Sutherland G.R.,
RA Burmeister M., Mulligan J.T.;
RT "Molecular characterization of a nonneuronal human UNC18 homolog.";
RL Genomics 37:19-23(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 3), AND VARIANT VAL-526.
RC TISSUE=Kidney;
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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [7]
RP FUNCTION, INTERACTION WITH STX11, VARIANTS FHL5 PRO-209; ILE-232 DEL;
RP HIS-292; TRP-405; GLN-405 AND LEU-477, AND CHARACTERIZATION OF VARIANTS
RP FHL5 ILE-232 DEL; HIS-292; TRP-405; GLN-405 AND LEU-477.
RX PubMed=19804848; DOI=10.1016/j.ajhg.2009.09.005;
RA zur Stadt U., Rohr J., Seifert W., Koch F., Grieve S., Pagel J.,
RA Strauss J., Kasper B., Nuernberg G., Becker C., Maul-Pavicic A., Beutel K.,
RA Janka G., Griffiths G., Ehl S., Hennies H.C.;
RT "Familial hemophagocytic lymphohistiocytosis type 5 (FHL-5) is caused by
RT mutations in Munc18-2 and impaired binding to syntaxin 11.";
RL Am. J. Hum. Genet. 85:482-492(2009).
RN [8]
RP FUNCTION, INTERACTION WITH STX11, AND VARIANT FHL5 LEU-477.
RX PubMed=19884660; DOI=10.1172/jci40732;
RA Cote M., Menager M.M., Burgess A., Mahlaoui N., Picard C., Schaffner C.,
RA Al-Manjomi F., Al-Harbi M., Alangari A., Le Deist F., Gennery A.R.,
RA Prince N., Cariou A., Nitschke P., Blank U., El-Ghazali G., Menasche G.,
RA Latour S., Fischer A., de Saint Basile G.;
RT "Munc18-2 deficiency causes familial hemophagocytic lymphohistiocytosis
RT type 5 and impairs cytotoxic granule exocytosis in patient NK cells.";
RL J. Clin. Invest. 119:3765-3773(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY 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).
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).
CC -!- FUNCTION: Involved in intracellular vesicle trafficking and vesicle
CC fusion with membranes. Contributes to the granule exocytosis machinery
CC through interaction with soluble N-ethylmaleimide-sensitive factor
CC attachment protein receptor (SNARE) proteins that regulate membrane
CC fusion. Regulates cytotoxic granule exocytosis in natural killer (NK)
CC cells. {ECO:0000269|PubMed:19804848, ECO:0000269|PubMed:19884660}.
CC -!- SUBUNIT: Interacts with STX1A, STX2 and STX3 (By similarity). Interacts
CC with STX11. {ECO:0000250, ECO:0000269|PubMed:19804848,
CC ECO:0000269|PubMed:19884660}.
CC -!- INTERACTION:
CC Q15833; O75558: STX11; NbExp=4; IntAct=EBI-4401015, EBI-714135;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15833-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15833-2; Sequence=VSP_040121;
CC Name=3;
CC IsoId=Q15833-3; Sequence=VSP_055157;
CC -!- TISSUE SPECIFICITY: Placenta, lung, liver, kidney and pancreas, as well
CC as in peripheral blood lymphocytes.
CC -!- DISEASE: Hemophagocytic lymphohistiocytosis, familial, 5, with or
CC without microvillus inclusion disease (FHL5) [MIM:613101]: A rare,
CC autosomal recessive disorder characterized by immune dysregulation with
CC hypercytokinemia, defective function of natural killer cell, and
CC massive infiltration of several organs by activated lymphocytes and
CC macrophages. The clinical features of the disease include fever,
CC hepatosplenomegaly, cytopenia, and less frequently neurological
CC abnormalities ranging from irritability and hypotonia to seizures,
CC cranial nerve deficits and ataxia. Some patients may present in early
CC infancy with severe diarrhea, prior to the onset of typical FHL
CC features, whereas others present later in childhood and have a more
CC protracted course without diarrhea. The early-onset diarrhea is due to
CC enteropathy reminiscent of microvillus inclusion disease.
CC {ECO:0000269|PubMed:19804848, ECO:0000269|PubMed:19884660}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; U63533; AAC50762.1; -; mRNA.
DR EMBL; BT006915; AAP35561.1; -; mRNA.
DR EMBL; AK303701; BAG64687.1; -; mRNA.
DR EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69018.1; -; Genomic_DNA.
DR EMBL; BC002869; AAH02869.1; -; mRNA.
DR CCDS; CCDS12181.1; -. [Q15833-1]
DR CCDS; CCDS45948.1; -. [Q15833-2]
DR CCDS; CCDS62522.1; -. [Q15833-3]
DR RefSeq; NP_001120868.1; NM_001127396.2. [Q15833-2]
DR RefSeq; NP_001258963.1; NM_001272034.1. [Q15833-3]
DR RefSeq; NP_008880.2; NM_006949.3. [Q15833-1]
DR PDB; 4CCA; X-ray; 2.60 A; A=1-593.
DR PDBsum; 4CCA; -.
DR AlphaFoldDB; Q15833; -.
DR SMR; Q15833; -.
DR BioGRID; 112682; 68.
DR IntAct; Q15833; 16.
DR STRING; 9606.ENSP00000413606; -.
DR iPTMnet; Q15833; -.
DR MetOSite; Q15833; -.
DR PhosphoSitePlus; Q15833; -.
DR BioMuta; STXBP2; -.
DR DMDM; 313104015; -.
DR OGP; Q15833; -.
DR EPD; Q15833; -.
DR jPOST; Q15833; -.
DR MassIVE; Q15833; -.
DR MaxQB; Q15833; -.
DR PaxDb; Q15833; -.
DR PeptideAtlas; Q15833; -.
DR PRIDE; Q15833; -.
DR ProteomicsDB; 17549; -.
DR ProteomicsDB; 60782; -. [Q15833-1]
DR ProteomicsDB; 60783; -. [Q15833-2]
DR Antibodypedia; 2787; 222 antibodies from 29 providers.
DR DNASU; 6813; -.
DR Ensembl; ENST00000221283.10; ENSP00000221283.4; ENSG00000076944.17. [Q15833-1]
DR Ensembl; ENST00000414284.6; ENSP00000409471.1; ENSG00000076944.17. [Q15833-2]
DR Ensembl; ENST00000441779.6; ENSP00000413606.2; ENSG00000076944.17. [Q15833-3]
DR GeneID; 6813; -.
DR KEGG; hsa:6813; -.
DR MANE-Select; ENST00000221283.10; ENSP00000221283.4; NM_006949.4; NP_008880.2.
DR UCSC; uc002mha.6; human. [Q15833-1]
DR CTD; 6813; -.
DR DisGeNET; 6813; -.
DR GeneCards; STXBP2; -.
DR GeneReviews; STXBP2; -.
DR HGNC; HGNC:11445; STXBP2.
DR HPA; ENSG00000076944; Tissue enhanced (bone).
DR MalaCards; STXBP2; -.
DR MIM; 601717; gene.
DR MIM; 613101; phenotype.
DR neXtProt; NX_Q15833; -.
DR OpenTargets; ENSG00000076944; -.
DR Orphanet; 540; Familial hemophagocytic lymphohistiocytosis.
DR PharmGKB; PA36242; -.
DR VEuPathDB; HostDB:ENSG00000076944; -.
DR eggNOG; KOG1300; Eukaryota.
DR GeneTree; ENSGT00940000160045; -.
DR InParanoid; Q15833; -.
DR OMA; WPFVSEP; -.
DR OrthoDB; 725424at2759; -.
DR PhylomeDB; Q15833; -.
DR TreeFam; TF313242; -.
DR PathwayCommons; Q15833; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR SignaLink; Q15833; -.
DR SIGNOR; Q15833; -.
DR BioGRID-ORCS; 6813; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; STXBP2; human.
DR GeneWiki; Syntaxin_binding_protein_2; -.
DR GenomeRNAi; 6813; -.
DR Pharos; Q15833; Tbio.
DR PRO; PR:Q15833; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q15833; protein.
DR Bgee; ENSG00000076944; Expressed in granulocyte and 144 other tissues.
DR ExpressionAtlas; Q15833; baseline and differential.
DR Genevisible; Q15833; HS.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0044194; C:cytolytic granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0070820; C:tertiary granule; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR GO; GO:0030348; F:syntaxin-3 binding; IPI:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0001909; P:leukocyte mediated cytotoxicity; IMP:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0043312; P:neutrophil degranulation; IEP:UniProtKB.
DR GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Exocytosis;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..593
FT /note="Syntaxin-binding protein 2"
FT /id="PRO_0000206281"
FT REGION 444..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 82
FT /note="K -> KAQAQRVIHLPQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055157"
FT VAR_SEQ 83..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_040121"
FT VARIANT 209
FT /note="L -> P (in FHL5; dbSNP:rs121918541)"
FT /evidence="ECO:0000269|PubMed:19804848"
FT /id="VAR_063814"
FT VARIANT 232
FT /note="Missing (in FHL5; leads to a complete loss of the
FT ability to interact with STX11)"
FT /evidence="ECO:0000269|PubMed:19804848"
FT /id="VAR_063815"
FT VARIANT 292
FT /note="R -> H (in FHL5; leads to a complete loss of the
FT ability to interact with STX11; dbSNP:rs746897867)"
FT /evidence="ECO:0000269|PubMed:19804848"
FT /id="VAR_063816"
FT VARIANT 405
FT /note="R -> Q (in FHL5; leads to a complete loss of the
FT ability to interact with STX11; dbSNP:rs773360200)"
FT /evidence="ECO:0000269|PubMed:19804848"
FT /id="VAR_063817"
FT VARIANT 405
FT /note="R -> W (in FHL5; leads to a complete loss of the
FT ability to interact with STX11; dbSNP:rs769717341)"
FT /evidence="ECO:0000269|PubMed:19804848"
FT /id="VAR_063818"
FT VARIANT 477
FT /note="P -> L (in FHL5; leads to a complete loss of the
FT ability to interact with STX11; dbSNP:rs121918540)"
FT /evidence="ECO:0000269|PubMed:19804848,
FT ECO:0000269|PubMed:19884660"
FT /id="VAR_063819"
FT VARIANT 526
FT /note="I -> V (in dbSNP:rs6791)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8921365"
FT /id="VAR_014934"
FT CONFLICT 348
FT /note="H -> R (in Ref. 3; BAG64687)"
FT /evidence="ECO:0000305"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:4CCA"
FT TURN 16..22
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:4CCA"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 196..215
FT /evidence="ECO:0007829|PDB:4CCA"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:4CCA"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 299..314
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 333..357
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 385..393
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 400..414
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:4CCA"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 544..556
FT /evidence="ECO:0007829|PDB:4CCA"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:4CCA"
FT STRAND 562..570
FT /evidence="ECO:0007829|PDB:4CCA"
FT HELIX 573..582
FT /evidence="ECO:0007829|PDB:4CCA"
SQ SEQUENCE 593 AA; 66453 MW; 98E27B55309168A9 CRC64;
MAPSGLKAVV GEKILSGVIR SVKKDGEWKV LIMDHPSMRI LSSCCKMSDI LAEGITIVED
INKRREPIPS LEAIYLLSPT EKSVQALIKD FQGTPTFTYK AAHIFFTDTC PEPLFSELGR
SRLAKVVKTL KEIHLAFLPY EAQVFSLDAP HSTYNLYCPF RAEERTRQLE VLAQQIATLC
ATLQEYPAIR YRKGPEDTAQ LAHAVLAKLN AFKADTPSLG EGPEKTRSQL LIMDRAADPV
SPLLHELTFQ AMAYDLLDIE QDTYRYETTG LSEAREKAVL LDEDDDLWVE LRHMHIADVS
KKVTELLRTF CESKRLTTDK ANIKDLSQIL KKMPQYQKEL NKYSTHLHLA DDCMKHFKGS
VEKLCSVEQD LAMGSDAEGE KIKDSMKLIV PVLLDAAVPA YDKIRVLLLY ILLRNGVSEE
NLAKLIQHAN VQAHSSLIRN LEQLGGTVTN PGGSGTSSRL EPRERMEPTY QLSRWTPVIK
DVMEDAVEDR LDRNLWPFVS DPAPTASSQA AVSARFGHWH KNKAGIEARA GPRLIVYVMG
GVAMSEMRAA YEVTRATEGK WEVLIGSSHI LTPTRFLDDL KALDKKLEDI ALP
