Protein transport protein Sec24A (SEC24-related protein A)

 SC24A_HUMAN             Reviewed;        1093 AA.
 O95486; A8MVW3; Q8WUV2; Q96GP7;
 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
 13-NOV-2007, sequence version 2.
 07-APR-2021, entry version 183.
 RecName: Full=Protein transport protein Sec24A {ECO:0000305};
 AltName: Full=SEC24-related protein A;
 Name=SEC24A {ECO:0000312|HGNC:HGNC:10703};
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
 Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
 Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
 Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
 Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
 Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
 Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
 Hunkapiller M.W., Myers E.W., Venter J.C.;
 Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
 [LARGE SCALE MRNA] OF 690-1093 (ISOFORM 1), AND VARIANTS ILE-302 AND
 MET-396.
 TISSUE=Brain, and Eye;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA] OF 16-1093 (ISOFORM 1).
 TISSUE=B-cell;
 PubMed=10075675; DOI=10.1074/jbc.274.12.7833;
 Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L., Orci L.,
 Paccaud J.-P.;
 "Sec24 proteins and sorting at the endoplasmic reticulum.";
 J. Biol. Chem. 274:7833-7840(1999).
 [4]
 FUNCTION, AND INTERACTION WITH TMED2.
 PubMed=20427317; DOI=10.1242/jcs.062950;
 Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
 "Selective export of human GPI-anchored proteins from the endoplasmic
 reticulum.";
 J. Cell Sci. 123:1705-1715(2010).
 [5]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21269460; DOI=10.1186/1752-0509-5-17;
 Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
 Bennett K.L., Superti-Furga G., Colinge J.;
 "Initial characterization of the human central proteome.";
 BMC Syst. Biol. 5:17-17(2011).
 [6]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
 Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
 phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [7]
 INTERACTION WITH TMEM39A AND SACM1L.
 PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
 Miao G., Zhang Y., Chen D., Zhang H.;
 "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
 by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
 Mol. Cell 0:0-0(2019).
 [8] {ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2NUT}
 X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 341-1093 IN COMPLEX WITH ZINC;
 SEC23A AND SEC22B, FUNCTION, INTERACTION WITH SEC22B, SUBUNIT, SUBCELLULAR
 LOCATION, AND MUTAGENESIS OF ARG-541.
 PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
 Mancias J.D., Goldberg J.;
 "The transport signal on Sec22 for packaging into COPII-coated vesicles is
 a conformational epitope.";
 Mol. Cell 26:403-414(2007).
 [9] {ECO:0007744|PDB:3EGD, ECO:0007744|PDB:3EGX}
 X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 346-1093 IN COMPLEX WITH CARGO
 PEPTIDES; SEC22B; SEC23A AND ZINC, AND FUNCTION.
 PubMed=18843296; DOI=10.1038/emboj.2008.208;
 Mancias J.D., Goldberg J.;
 "Structural basis of cargo membrane protein discrimination by the human
 COPII coat machinery.";
 EMBO J. 27:2918-2928(2008).
 [10]
 INTERACTION WITH STING1.
 PubMed=32690950; DOI=10.1038/s41590-020-0730-5;
 Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
 Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
 Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
 Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
 Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
 Thomsen M.K., Paludan S.R.;
 "STEEP mediates STING ER exit and activation of signaling.";
 Nat. Immunol. 21:868-879(2020).
 [11]
 ERRATUM OF PUBMED:32690950.
 PubMed=32929276; DOI=10.1038/s41590-020-0803-5;
 Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
 Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
 Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
 Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
 Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
 Thomsen M.K., Paludan S.R.;
 Nat. Immunol. 21:1468-1469(2020).
 -!- FUNCTION: Component of the coat protein complex II (COPII) which
     promotes the formation of transport vesicles from the endoplasmic
     reticulum (ER). The coat has two main functions, the physical
     deformation of the endoplasmic reticulum membrane into vesicles and the
     selection of cargo molecules for their transport to the Golgi complex
     (PubMed:20427317, PubMed:17499046, PubMed:18843296). Plays a central
     role in cargo selection within the COPII complex and together with
     SEC24B may have a different specificity compared to SEC24C and SEC24D.
     May package preferentially cargos with cytoplasmic DxE or LxxLE motifs
     and may also recognize conformational epitopes (PubMed:17499046,
     PubMed:18843296). {ECO:0000269|PubMed:17499046,
     ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
 -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
     complex, the Sec13/31 complex and Sar1 (PubMed:17499046). Interacts
     with TMED2 (PubMed:20427317). Interacts (as part of the Sec23/24
     complex) with SEC22B; recruits SEC22B into COPII-coated vesicles for
     its transport from the endoplasmic reticulum to the Golgi
     (PubMed:17499046). Interacts with STING1; promoting STING1
     translocation to COPII vesicles in a STEEP1-dependent manner
     (PubMed:32690950). Interacts with TMEM39A (PubMed:31806350). Interacts
     with SACM1L; this interaction is reduced in the absence of TMEM39A
     (PubMed:31806350). {ECO:0000269|PubMed:17499046,
     ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:31806350,
     ECO:0000269|PubMed:32690950}.
 -!- INTERACTION:
     O95486; Q01844: EWSR1; NbExp=3; IntAct=EBI-749911, EBI-739737;
     O95486; Q92734: TFG; NbExp=3; IntAct=EBI-749911, EBI-357061;
     O95486-2; Q03989: ARID5A; NbExp=3; IntAct=EBI-12320085, EBI-948603;
     O95486-2; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-12320085, EBI-724639;
     O95486-2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-12320085, EBI-11975223;
 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
     membrane {ECO:0000305|PubMed:17499046}; Peripheral membrane protein
     {ECO:0000305|PubMed:17499046}; Cytoplasmic side
     {ECO:0000305|PubMed:17499046}. Endoplasmic reticulum membrane
     {ECO:0000305|PubMed:17499046}; Peripheral membrane protein
     {ECO:0000305|PubMed:17499046}; Cytoplasmic side
     {ECO:0000305|PubMed:17499046}. Cytoplasm, cytosol
     {ECO:0000305|PubMed:17499046}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=O95486-1; Sequence=Displayed;
     Name=2;
       IsoId=O95486-2; Sequence=VSP_029571, VSP_029572;
 -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
     {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=CAA10334.1; Type=Frameshift; Evidence={ECO:0000305};
 -!- WEB RESOURCE: Name=Wikipedia; Note=COPII entry;
     URL="https://en.wikipedia.org/wiki/COPII";
 ---------------------------------------------------------------------------
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 EMBL; CH471062; EAW62246.1; -; Genomic_DNA.
 EMBL; BC009325; AAH09325.2; -; mRNA.
 EMBL; BC019341; AAH19341.1; -; mRNA.
 EMBL; AJ131244; CAA10334.1; ALT_FRAME; mRNA.
 CCDS; CCDS43363.1; -. [O95486-1]
 CCDS; CCDS58967.1; -. [O95486-2]
 RefSeq; NP_001239160.1; NM_001252231.1. [O95486-2]
 RefSeq; NP_068817.1; NM_021982.2. [O95486-1]
 PDB; 2NUP; X-ray; 2.80 A; B=341-1093.
 PDB; 2NUT; X-ray; 2.30 A; B=341-1093.
 PDB; 3EGD; X-ray; 2.70 A; B=346-1093.
 PDB; 3EGX; X-ray; 3.30 A; B=346-1093.
 PDB; 5VNE; X-ray; 2.70 A; B=346-1093.
 PDB; 5VNF; X-ray; 2.41 A; B=346-1093.
 PDB; 5VNG; X-ray; 2.60 A; B=346-1093.
 PDB; 5VNH; X-ray; 2.60 A; B=346-1093.
 PDB; 5VNI; X-ray; 2.79 A; B=346-1093.
 PDB; 5VNJ; X-ray; 2.81 A; B=346-1093.
 PDB; 5VNK; X-ray; 2.55 A; B=346-1093.
 PDB; 5VNL; X-ray; 2.39 A; B=346-1093.
 PDB; 5VNM; X-ray; 2.77 A; B=346-1093.
 PDB; 5VNN; X-ray; 2.50 A; B=346-1093.
 PDB; 5VNO; X-ray; 2.90 A; B=346-1093.
 PDBsum; 2NUP; -.
 PDBsum; 2NUT; -.
 PDBsum; 3EGD; -.
 PDBsum; 3EGX; -.
 PDBsum; 5VNE; -.
 PDBsum; 5VNF; -.
 PDBsum; 5VNG; -.
 PDBsum; 5VNH; -.
 PDBsum; 5VNI; -.
 PDBsum; 5VNJ; -.
 PDBsum; 5VNK; -.
 PDBsum; 5VNL; -.
 PDBsum; 5VNM; -.
 PDBsum; 5VNN; -.
 PDBsum; 5VNO; -.
 SMR; O95486; -.
 BioGRID; 116016; 122.
 IntAct; O95486; 25.
 STRING; 9606.ENSP00000381823; -.
 iPTMnet; O95486; -.
 MetOSite; O95486; -.
 PhosphoSitePlus; O95486; -.
 BioMuta; SEC24A; -.
 EPD; O95486; -.
 jPOST; O95486; -.
 MassIVE; O95486; -.
 MaxQB; O95486; -.
 PaxDb; O95486; -.
 PeptideAtlas; O95486; -.
 PRIDE; O95486; -.
 ProteomicsDB; 50913; -. [O95486-1]
 ProteomicsDB; 50914; -. [O95486-2]
 Antibodypedia; 45232; 105 antibodies.
 Ensembl; ENST00000322887; ENSP00000321749; ENSG00000113615. [O95486-2]
 Ensembl; ENST00000398844; ENSP00000381823; ENSG00000113615. [O95486-1]
 GeneID; 10802; -.
 KEGG; hsa:10802; -.
 UCSC; uc003kzs.4; human. [O95486-1]
 CTD; 10802; -.
 GeneCards; SEC24A; -.
 HGNC; HGNC:10703; SEC24A.
 HPA; ENSG00000113615; Low tissue specificity.
 MIM; 607183; gene.
 neXtProt; NX_O95486; -.
 OpenTargets; ENSG00000113615; -.
 PharmGKB; PA35626; -.
 VEuPathDB; HostDB:ENSG00000113615.12; -.
 eggNOG; KOG1985; Eukaryota.
 GeneTree; ENSGT00950000182924; -.
 HOGENOM; CLU_004589_2_0_1; -.
 InParanoid; O95486; -.
 OMA; VVQDQVI; -.
 PhylomeDB; O95486; -.
 TreeFam; TF350406; -.
 PathwayCommons; O95486; -.
 Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
 Reactome; R-HSA-204005; COPII-mediated vesicle transport.
 Reactome; R-HSA-2132295; MHC class II antigen presentation.
 Reactome; R-HSA-5694530; Cargo concentration in the ER.
 Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
 BioGRID-ORCS; 10802; 10 hits in 988 CRISPR screens.
 ChiTaRS; SEC24A; human.
 EvolutionaryTrace; O95486; -.
 GenomeRNAi; 10802; -.
 Pharos; O95486; Tbio.
 PRO; PR:O95486; -.
 Proteomes; UP000005640; Chromosome 5.
 RNAct; O95486; protein.
 Bgee; ENSG00000113615; Expressed in jejunal mucosa and 242 other tissues.
 ExpressionAtlas; O95486; baseline and differential.
 Genevisible; O95486; HS.
 GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
 GO; GO:0005829; C:cytosol; TAS:Reactome.
 GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
 GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
 GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
 GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
 GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
 GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
 GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
 GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
 CDD; cd01479; Sec24-like; 1.
 Gene3D; 3.40.20.10; -; 1.
 Gene3D; 3.40.50.410; -; 1.
 InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
 InterPro; IPR007123; Gelsolin-like_dom.
 InterPro; IPR036180; Gelsolin-like_dom_sf.
 InterPro; IPR006900; Sec23/24_helical_dom.
 InterPro; IPR036175; Sec23/24_helical_dom_sf.
 InterPro; IPR006896; Sec23/24_trunk_dom.
 InterPro; IPR012990; Sec23_24_beta_S.
 InterPro; IPR041742; Sec24-like_trunk_dom.
 InterPro; IPR036465; vWFA_dom_sf.
 InterPro; IPR006895; Znf_Sec23_Sec24.
 Pfam; PF00626; Gelsolin; 1.
 Pfam; PF08033; Sec23_BS; 1.
 Pfam; PF04815; Sec23_helical; 1.
 Pfam; PF04811; Sec23_trunk; 1.
 Pfam; PF04810; zf-Sec23_Sec24; 1.
 SUPFAM; SSF53300; SSF53300; 1.
 SUPFAM; SSF81811; SSF81811; 1.
 SUPFAM; SSF82754; SSF82754; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
 Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
 Protein transport; Reference proteome; Transport; Zinc.
 CHAIN           1..1093
                 /note="Protein transport protein Sec24A"
                 /id="PRO_0000205153"
 REPEAT          966..1038
                 /note="Gelsolin-like"
                 /evidence="ECO:0000255"
 REGION          431..455
                 /note="Zinc finger-like"
 COMPBIAS        89..237
                 /note="Pro-rich"
 METAL           431
                 /note="Zinc"
                 /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
 METAL           434
                 /note="Zinc"
                 /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
 METAL           452
                 /note="Zinc"
                 /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
 METAL           455
                 /note="Zinc"
                 /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
 VAR_SEQ         594..613
                 /note="LVQDLLKTLPQMFTKTLETQ -> SVIGVSSEETLITCLEIAMR (in
                 isoform 2)"
                 /evidence="ECO:0000303|PubMed:15489334"
                 /id="VSP_029571"
 VAR_SEQ         614..1093
                 /note="Missing (in isoform 2)"
                 /evidence="ECO:0000303|PubMed:15489334"
                 /id="VSP_029572"
 VARIANT         261
                 /note="S -> G (in dbSNP:rs7718102)"
                 /id="VAR_037253"
 VARIANT         302
                 /note="T -> I (in dbSNP:rs17851746)"
                 /evidence="ECO:0000269|PubMed:15489334"
                 /id="VAR_037254"
 VARIANT         396
                 /note="T -> M (in dbSNP:rs17851745)"
                 /evidence="ECO:0000269|PubMed:15489334"
                 /id="VAR_037255"
 MUTAGEN         541
                 /note="R->A: Decreased ability to interact with and package
                 the SNARE SEC22B cargo into COPII vesicles. Has no effect
                 on other cargos packaging."
                 /evidence="ECO:0000269|PubMed:17499046"
 STRAND          350..352
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           353..356
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           374..377
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            383..385
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          386..396
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           397..403
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          408..411
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            432..434
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          442..451
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            453..455
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          458..460
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           463..465
                 /evidence="ECO:0007744|PDB:5VNJ"
 HELIX           477..479
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           481..484
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          486..491
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           494..496
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          498..500
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          505..511
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           514..519
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           521..532
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            533..535
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          543..557
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          562..564
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          566..570
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           573..575
                 /evidence="ECO:0007744|PDB:5VNI"
 STRAND          581..587
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            588..591
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           592..601
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           602..604
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            605..608
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           616..627
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            628..630
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          632..638
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          657..659
                 /evidence="ECO:0007744|PDB:2NUP"
 HELIX           672..682
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          685..691
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           699..702
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           704..707
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            708..710
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          713..715
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            721..723
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           725..740
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          744..753
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          757..768
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          770..772
                 /evidence="ECO:0007744|PDB:5VNL"
 STRAND          774..779
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          785..793
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          799..810
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          816..828
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           831..836
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           840..857
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           860..879
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          891..893
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           894..896
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           899..908
                 /evidence="ECO:0007744|PDB:2NUT"
 TURN            910..912
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           920..932
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           935..942
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          945..948
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          954..956
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          960..962
                 /evidence="ECO:0007744|PDB:5VNE"
 TURN            975..977
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          982..987
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          989..996
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           1002..1007
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           1014..1016
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           1030..1043
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          1046..1048
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          1051..1053
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          1058..1061
                 /evidence="ECO:0007744|PDB:2NUT"
 HELIX           1066..1068
                 /evidence="ECO:0007744|PDB:2NUT"
 STRAND          1075..1077
                 /evidence="ECO:0007744|PDB:5VNH"
 HELIX           1080..1091
                 /evidence="ECO:0007744|PDB:2NUT"
 SEQUENCE   1093 AA;  119749 MW;  E21F3A1333674A6A CRC64;
 MSQPGIPASG GAPASLQAQN GAALASGSPY TNGPVQNALL SSQESVSQGY NFQLPGSYPH
 PIPAKTLNPV SGQSNYGGSQ GSGQTLNRPP VASNPVTPSL HSGPAPRMPL PASQNPATTP
 MPSSSFLPEA NLPPPLNWQY NYPSTASQTN HCPRASSQPT VSGNTSLTTN HQYVSSGYPS
 LQNSFIKSGP SVPPLVNPPL PTTFQPGAPH GPPPAGGPPP VRALTPLTSS YRDVPQPLFN
 SAVNQEGITS NTNNGSMVVH SSYDEIEGGG LLATPQLTNK NPKMSRSVGY SYPSLPPGYQ
 NTTPPGATGV PPSSLNYPSG PQAFTQTPLG ANHLTTSMSG LSLQPEGLRV VNLLQERNML
 PSTPLKPPVP NLHEDIQKLN CNPELFRCTL TSIPQTQALL NKAKLPLGLL LHPFKDLVQL
 PVVTSSTIVR CRSCRTYINP FVSFLDQRRW KCNLCYRVND VPEEFLYNPL TRVYGEPHRR
 PEVQNATIEF MAPSEYMLRP PQPPVYLFVF DVSHNAVETG YLNSVCQSLL DNLDLLPGNT
 RTKIGFITFD STIHFYGLQE SLSQPQMLIV SDIEDVFIPM PENLLVNLNE SKELVQDLLK
 TLPQMFTKTL ETQSALGPAL QAAFKLMSPT GGRMSVFQTQ LPTLGVGALK PREEPNHRSS
 AKDIHMTPST DFYKKLALDC SGQQVAVDLF LLSGQYSDLA SLGCISRYSA GSVYYYPSYH
 HQHNPVQVQK LQKELQRYLT RKIGFEAVMR IRCTKGLSIH TFHGNFFVRS TDLLSLPNVN
 PDAGYAVQMS VEESLTDTQL VSFQSALLYT SSKGERRIRV HTLCLPVVST LNDVFLGADV
 QAISGLLANM AVDRSMTASL SDARDALVNA VIDSLSAYRS SVLSNQQPGL MVPFSLRLFP
 LFVLALLKQK SFQTGTNARL DERIFAMCQV KNQPLVYLML TTHPSLYRVD NLSDEGALNI
 SDRTIPQPPI LQLSVEKLSR DGAFLMDAGS VLMLWVGKNC TQNFLSQVLG VQNYASIPQP
 MTDLPELDTP ESARIIAFIS WLREQRPFFP ILYVIRDESP MKANFLQNMI EDRTESALSY
 YEFLLHIQQQ VNK

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