SC24A_HUMAN
ID SC24A_HUMAN Reviewed; 1093 AA.
AC O95486; A8MVW3; Q8WUV2; Q96GP7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Protein transport protein Sec24A {ECO:0000305};
DE AltName: Full=SEC24-related protein A;
GN Name=SEC24A {ECO:0000312|HGNC:HGNC:10703};
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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 690-1093 (ISOFORM 1), AND VARIANTS ILE-302 AND
RP MET-396.
RC TISSUE=Brain, and Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-1093 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=10075675; DOI=10.1074/jbc.274.12.7833;
RA Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L., Orci L.,
RA Paccaud J.-P.;
RT "Sec24 proteins and sorting at the endoplasmic reticulum.";
RL J. Biol. Chem. 274:7833-7840(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH TMED2.
RX PubMed=20427317; DOI=10.1242/jcs.062950;
RA Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
RT "Selective export of human GPI-anchored proteins from the endoplasmic
RT reticulum.";
RL J. Cell Sci. 123:1705-1715(2010).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH TMEM39A AND SACM1L.
RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA Miao G., Zhang Y., Chen D., Zhang H.;
RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL Mol. Cell 0:0-0(2019).
RN [8]
RP INTERACTION WITH FAM20C.
RX PubMed=34349020; DOI=10.1073/pnas.2100133118;
RA Chen X., Zhang J., Liu P., Wei Y., Wang X., Xiao J., Wang C.C., Wang L.;
RT "Proteolytic processing of secretory pathway kinase Fam20C by site-1
RT protease promotes biomineralization.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [9] {ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2NUT}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 341-1093 IN COMPLEX WITH ZINC;
RP SEC23A AND SEC22B, FUNCTION, INTERACTION WITH SEC22B, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF ARG-541.
RX PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
RA Mancias J.D., Goldberg J.;
RT "The transport signal on Sec22 for packaging into COPII-coated vesicles is
RT a conformational epitope.";
RL Mol. Cell 26:403-414(2007).
RN [10] {ECO:0007744|PDB:3EGD, ECO:0007744|PDB:3EGX}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 346-1093 IN COMPLEX WITH CARGO
RP PEPTIDES; SEC22B; SEC23A AND ZINC, AND FUNCTION.
RX PubMed=18843296; DOI=10.1038/emboj.2008.208;
RA Mancias J.D., Goldberg J.;
RT "Structural basis of cargo membrane protein discrimination by the human
RT COPII coat machinery.";
RL EMBO J. 27:2918-2928(2008).
RN [11]
RP INTERACTION WITH STING1.
RX PubMed=32690950; DOI=10.1038/s41590-020-0730-5;
RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
RA Thomsen M.K., Paludan S.R.;
RT "STEEP mediates STING ER exit and activation of signaling.";
RL Nat. Immunol. 21:868-879(2020).
RN [12]
RP ERRATUM OF PUBMED:32690950.
RX PubMed=32929276; DOI=10.1038/s41590-020-0803-5;
RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
RA Thomsen M.K., Paludan S.R.;
RL Nat. Immunol. 21:1468-1469(2020).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules for their transport to the Golgi complex
CC (PubMed:20427317, PubMed:17499046, PubMed:18843296). Plays a central
CC role in cargo selection within the COPII complex and together with
CC SEC24B may have a different specificity compared to SEC24C and SEC24D.
CC May package preferentially cargos with cytoplasmic DxE or LxxLE motifs
CC and may also recognize conformational epitopes (PubMed:17499046,
CC PubMed:18843296). {ECO:0000269|PubMed:17499046,
CC ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and Sar1 (PubMed:17499046). Interacts
CC with TMED2 (PubMed:20427317). Interacts (as part of the Sec23/24
CC complex) with SEC22B; recruits SEC22B into COPII-coated vesicles for
CC its transport from the endoplasmic reticulum to the Golgi
CC (PubMed:17499046). Interacts with STING1; promoting STING1
CC translocation to COPII vesicles in a STEEP1-dependent manner
CC (PubMed:32690950). Interacts with TMEM39A (PubMed:31806350). Interacts
CC with SACM1L; this interaction is reduced in the absence of TMEM39A
CC (PubMed:31806350). Interacts with kinase FAM20C; transport of FAM20C
CC from the endoplasmic reticulum to the Golgi is likely to be mediated by
CC COPII vesicles (PubMed:34349020). {ECO:0000269|PubMed:17499046,
CC ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:31806350,
CC ECO:0000269|PubMed:32690950, ECO:0000269|PubMed:34349020}.
CC -!- INTERACTION:
CC O95486; Q01844: EWSR1; NbExp=3; IntAct=EBI-749911, EBI-739737;
CC O95486; Q92734: TFG; NbExp=3; IntAct=EBI-749911, EBI-357061;
CC O95486-2; Q03989: ARID5A; NbExp=3; IntAct=EBI-12320085, EBI-948603;
CC O95486-2; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-12320085, EBI-724639;
CC O95486-2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-12320085, EBI-11975223;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000305|PubMed:17499046}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17499046}; Cytoplasmic side
CC {ECO:0000305|PubMed:17499046}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:17499046}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17499046}; Cytoplasmic side
CC {ECO:0000305|PubMed:17499046}. Cytoplasm, cytosol
CC {ECO:0000305|PubMed:17499046}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95486-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95486-2; Sequence=VSP_029571, VSP_029572;
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA10334.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=COPII entry;
CC URL="https://en.wikipedia.org/wiki/COPII";
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DR EMBL; CH471062; EAW62246.1; -; Genomic_DNA.
DR EMBL; BC009325; AAH09325.2; -; mRNA.
DR EMBL; BC019341; AAH19341.1; -; mRNA.
DR EMBL; AJ131244; CAA10334.1; ALT_FRAME; mRNA.
DR CCDS; CCDS43363.1; -. [O95486-1]
DR CCDS; CCDS58967.1; -. [O95486-2]
DR RefSeq; NP_001239160.1; NM_001252231.1. [O95486-2]
DR RefSeq; NP_068817.1; NM_021982.2. [O95486-1]
DR PDB; 2NUP; X-ray; 2.80 A; B=341-1093.
DR PDB; 2NUT; X-ray; 2.30 A; B=341-1093.
DR PDB; 3EGD; X-ray; 2.70 A; B=346-1093.
DR PDB; 3EGX; X-ray; 3.30 A; B=346-1093.
DR PDB; 5VNE; X-ray; 2.70 A; B=346-1093.
DR PDB; 5VNF; X-ray; 2.41 A; B=346-1093.
DR PDB; 5VNG; X-ray; 2.60 A; B=346-1093.
DR PDB; 5VNH; X-ray; 2.60 A; B=346-1093.
DR PDB; 5VNI; X-ray; 2.79 A; B=346-1093.
DR PDB; 5VNJ; X-ray; 2.81 A; B=346-1093.
DR PDB; 5VNK; X-ray; 2.55 A; B=346-1093.
DR PDB; 5VNL; X-ray; 2.39 A; B=346-1093.
DR PDB; 5VNM; X-ray; 2.77 A; B=346-1093.
DR PDB; 5VNN; X-ray; 2.50 A; B=346-1093.
DR PDB; 5VNO; X-ray; 2.90 A; B=346-1093.
DR PDBsum; 2NUP; -.
DR PDBsum; 2NUT; -.
DR PDBsum; 3EGD; -.
DR PDBsum; 3EGX; -.
DR PDBsum; 5VNE; -.
DR PDBsum; 5VNF; -.
DR PDBsum; 5VNG; -.
DR PDBsum; 5VNH; -.
DR PDBsum; 5VNI; -.
DR PDBsum; 5VNJ; -.
DR PDBsum; 5VNK; -.
DR PDBsum; 5VNL; -.
DR PDBsum; 5VNM; -.
DR PDBsum; 5VNN; -.
DR PDBsum; 5VNO; -.
DR AlphaFoldDB; O95486; -.
DR SMR; O95486; -.
DR BioGRID; 116016; 163.
DR IntAct; O95486; 30.
DR MINT; O95486; -.
DR STRING; 9606.ENSP00000381823; -.
DR GlyGen; O95486; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; O95486; -.
DR MetOSite; O95486; -.
DR PhosphoSitePlus; O95486; -.
DR BioMuta; SEC24A; -.
DR EPD; O95486; -.
DR jPOST; O95486; -.
DR MassIVE; O95486; -.
DR MaxQB; O95486; -.
DR PaxDb; O95486; -.
DR PeptideAtlas; O95486; -.
DR PRIDE; O95486; -.
DR ProteomicsDB; 50913; -. [O95486-1]
DR ProteomicsDB; 50914; -. [O95486-2]
DR Antibodypedia; 45232; 111 antibodies from 24 providers.
DR DNASU; 10802; -.
DR Ensembl; ENST00000322887.8; ENSP00000321749.4; ENSG00000113615.13. [O95486-2]
DR Ensembl; ENST00000398844.7; ENSP00000381823.2; ENSG00000113615.13. [O95486-1]
DR GeneID; 10802; -.
DR KEGG; hsa:10802; -.
DR MANE-Select; ENST00000398844.7; ENSP00000381823.2; NM_021982.3; NP_068817.1.
DR UCSC; uc003kzs.4; human. [O95486-1]
DR CTD; 10802; -.
DR GeneCards; SEC24A; -.
DR HGNC; HGNC:10703; SEC24A.
DR HPA; ENSG00000113615; Low tissue specificity.
DR MIM; 607183; gene.
DR neXtProt; NX_O95486; -.
DR OpenTargets; ENSG00000113615; -.
DR PharmGKB; PA35626; -.
DR VEuPathDB; HostDB:ENSG00000113615; -.
DR eggNOG; KOG1985; Eukaryota.
DR GeneTree; ENSGT00950000182924; -.
DR HOGENOM; CLU_004589_2_0_1; -.
DR InParanoid; O95486; -.
DR OMA; TFPRDQS; -.
DR PhylomeDB; O95486; -.
DR TreeFam; TF350406; -.
DR PathwayCommons; O95486; -.
DR Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SignaLink; O95486; -.
DR SIGNOR; O95486; -.
DR BioGRID-ORCS; 10802; 17 hits in 1070 CRISPR screens.
DR ChiTaRS; SEC24A; human.
DR EvolutionaryTrace; O95486; -.
DR GenomeRNAi; 10802; -.
DR Pharos; O95486; Tbio.
DR PRO; PR:O95486; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O95486; protein.
DR Bgee; ENSG00000113615; Expressed in jejunal mucosa and 205 other tissues.
DR ExpressionAtlas; O95486; baseline and differential.
DR Genevisible; O95486; HS.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0032374; P:regulation of cholesterol transport; IEA:Ensembl.
DR CDD; cd01479; Sec24-like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..1093
FT /note="Protein transport protein Sec24A"
FT /id="PRO_0000205153"
FT REPEAT 966..1038
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..455
FT /note="Zinc finger-like"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..221
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
FT VAR_SEQ 594..613
FT /note="LVQDLLKTLPQMFTKTLETQ -> SVIGVSSEETLITCLEIAMR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029571"
FT VAR_SEQ 614..1093
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029572"
FT VARIANT 261
FT /note="S -> G (in dbSNP:rs7718102)"
FT /id="VAR_037253"
FT VARIANT 302
FT /note="T -> I (in dbSNP:rs17851746)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037254"
FT VARIANT 396
FT /note="T -> M (in dbSNP:rs17851745)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037255"
FT MUTAGEN 541
FT /note="R->A: Decreased ability to interact with and package
FT the SNARE SEC22B cargo into COPII vesicles. Has no effect
FT on other cargos packaging."
FT /evidence="ECO:0000269|PubMed:17499046"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 386..396
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:5VNJ"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 505..511
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 521..532
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 543..557
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:5VNI"
FT STRAND 581..587
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 588..591
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 592..601
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 605..608
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 616..627
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 632..638
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:2NUP"
FT HELIX 672..682
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 685..691
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 704..707
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 708..710
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 725..740
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 744..753
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 757..768
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:5VNL"
FT STRAND 774..779
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 785..793
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 799..810
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 816..828
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 831..836
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 840..857
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 860..879
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 891..893
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 899..908
FT /evidence="ECO:0007829|PDB:2NUT"
FT TURN 910..912
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 920..932
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 935..942
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 945..948
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 954..956
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 960..962
FT /evidence="ECO:0007829|PDB:5VNE"
FT TURN 975..977
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 982..987
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 989..996
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 1002..1007
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 1014..1016
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 1030..1043
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 1046..1048
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 1051..1053
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 1058..1061
FT /evidence="ECO:0007829|PDB:2NUT"
FT HELIX 1066..1068
FT /evidence="ECO:0007829|PDB:2NUT"
FT STRAND 1075..1077
FT /evidence="ECO:0007829|PDB:5VNH"
FT HELIX 1080..1091
FT /evidence="ECO:0007829|PDB:2NUT"
SQ 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
