ID SC24D_HUMAN Reviewed; 1032 AA. AC O94855; Q8IYI7; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=Protein transport protein Sec24D {ECO:0000305}; DE AltName: Full=SEC24-related protein D; GN Name=SEC24D {ECO:0000312|HGNC:HGNC:10706}; GN Synonyms=KIAA0755 {ECO:0000312|EMBL:BAA34475.2}; 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), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Pancreas; RX PubMed=10329445; DOI=10.1006/bbrc.1999.0574; RA Tang B.L., Kausalya J., Low D.Y.H., Lock M.L., Hong W.; RT "A family of mammalian proteins homologous to yeast Sec24p."; RL Biochem. Biophys. Res. Commun. 258:679-684(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [5] RP FUNCTION, AND SUBUNIT. 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 [6] RP FUNCTION, AND INTERACTION WITH TMED2 AND TMED10. 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 [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, 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). RN [9] 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 [10] RP INTERACTION WITH CNIH4. RX PubMed=24405750; DOI=10.1111/tra.12148; RA Sauvageau E., Rochdi M.D., Oueslati M., Hamdan F.F., Percherancier Y., RA Simpson J.C., Pepperkok R., Bouvier M.; RT "CNIH4 interacts with newly synthesized GPCR and controls their export from RT the endoplasmic reticulum."; RL Traffic 15:383-400(2014). RN [11] RP INVOLVEMENT IN CLCRP2, AND VARIANTS CLCRP2 PRO-978 AND PHE-1015. RX PubMed=25683121; DOI=10.1016/j.ajhg.2015.01.002; RA Garbes L., Kim K., Riess A., Hoyer-Kuhn H., Beleggia F., Bevot A., RA Kim M.J., Huh Y.H., Kweon H.S., Savarirayan R., Amor D., Kakadia P.M., RA Lindig T., Kagan K.O., Becker J., Boyadjiev S.A., Wollnik B., Semler O., RA Bohlander S.K., Kim J., Netzer C.; RT "Mutations in SEC24D, encoding a component of the COPII machinery, cause a RT syndromic form of osteogenesis imperfecta."; RL Am. J. Hum. Genet. 96:432-439(2015). 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). RN [13] {ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 266-1032 IN COMPLEX WITH CARGO RP PEPTIDES; SEC23A AND ZINC, FUNCTION, AND INTERACTION WITH GOSR2 AND STX5. 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 [14] {ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYW, ECO:0007744|PDB:5KYX, ECO:0007744|PDB:5KYY} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 266-1032 IN COMPLEX WITH SEC23A RP AND ZINC, AND INTERACTION WITH SEC23A. RX PubMed=27551091; DOI=10.1073/pnas.1605916113; RA Ma W., Goldberg J.; RT "TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large RT COPII coats."; RL Proc. Natl. Acad. Sci. U.S.A. 113:10061-10066(2016). 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:17499046, PubMed:20427317, PubMed:18843296). Plays a central CC role in cargo selection within the COPII complex and together with CC SEC24C may have a different specificity compared to SEC24A and SEC24B CC (PubMed:17499046, PubMed:20427317, PubMed:18843296). May more CC specifically package GPI-anchored proteins through the cargo receptor CC TMED10 (PubMed:20427317). May also be specific for IxM motif-containing CC cargos like the SNAREs GOSR2 and STX5 (PubMed:18843296). CC {ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296, CC 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, CC PubMed:27551091). Interacts with TMED2 and TMED10 (PubMed:20427317). CC Interacts with CNIH4 (PubMed:24405750). Interacts with GOSR2 (via IxM CC motif) and STX5 (via IxM motif); recruits GOSR2 and STX5 into COPII- CC coated vesicles (PubMed:18843296). {ECO:0000269|PubMed:17499046, CC ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317, CC ECO:0000269|PubMed:24405750, ECO:0000269|PubMed:27551091}. CC -!- INTERACTION: CC O94855; Q01844: EWSR1; NbExp=3; IntAct=EBI-748817, EBI-739737; CC O94855; Q15437: SEC23B; NbExp=6; IntAct=EBI-748817, EBI-742673; CC O94855; Q15427: SF3B4; NbExp=3; IntAct=EBI-748817, EBI-348469; CC O94855-2; Q15436: SEC23A; NbExp=3; IntAct=EBI-12081096, EBI-81088; CC O94855-2; Q15437: SEC23B; NbExp=3; IntAct=EBI-12081096, EBI-742673; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle CC membrane {ECO:0000269|PubMed:10329445}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P53992}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P53992}. Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:10329445}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P53992}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P53992}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P53992}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O94855-1; Sequence=Displayed; CC Name=2; CC IsoId=O94855-2; Sequence=VSP_035761; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with higher amounts in CC placenta, pancreas, heart and liver. {ECO:0000269|PubMed:10329445}. CC -!- DISEASE: Cole-Carpenter syndrome 2 (CLCRP2) [MIM:616294]: A form of CC Cole-Carpenter syndrome, a disorder characterized by features of CC osteogenesis imperfecta such as bone deformities and severe bone CC fragility with frequent fractures, in association with CC craniosynostosis, ocular proptosis, hydrocephalus, growth failure and CC distinctive facial features. Craniofacial findings include marked CC frontal bossing, midface hypoplasia, and micrognathia. Despite the CC craniosynostosis and hydrocephalus, intellectual development is normal. CC CLCRP2 inheritance is autosomal recessive. CC {ECO:0000269|PubMed:25683121}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34475.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF130464; AAD28756.2; -; mRNA. DR EMBL; AB018298; BAA34475.2; ALT_INIT; mRNA. DR EMBL; CH471229; EAW73656.1; -; Genomic_DNA. DR EMBL; BC035761; AAH35761.1; -; mRNA. DR CCDS; CCDS3710.1; -. [O94855-1] DR RefSeq; NP_001304995.1; NM_001318066.1. [O94855-2] DR RefSeq; NP_055637.2; NM_014822.3. [O94855-1] DR RefSeq; XP_005263436.1; XM_005263379.2. DR PDB; 3EFO; X-ray; 2.70 A; B=266-1032. DR PDB; 3EG9; X-ray; 3.00 A; B=266-1032. DR PDB; 5KYU; X-ray; 3.51 A; B=266-1032. DR PDB; 5KYW; X-ray; 3.20 A; B=266-1032. DR PDB; 5KYX; X-ray; 3.52 A; B=266-1032. DR PDB; 5KYY; X-ray; 3.40 A; B=266-1032. DR PDBsum; 3EFO; -. DR PDBsum; 3EG9; -. DR PDBsum; 5KYU; -. DR PDBsum; 5KYW; -. DR PDBsum; 5KYX; -. DR PDBsum; 5KYY; -. DR AlphaFoldDB; O94855; -. DR SMR; O94855; -. DR BioGRID; 115204; 56. DR ComplexPortal; CPX-2360; COPII vesicle coat complex. DR IntAct; O94855; 21. DR MINT; O94855; -. DR STRING; 9606.ENSP00000280551; -. DR GlyGen; O94855; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; O94855; -. DR MetOSite; O94855; -. DR PhosphoSitePlus; O94855; -. DR SwissPalm; O94855; -. DR BioMuta; SEC24D; -. DR EPD; O94855; -. DR jPOST; O94855; -. DR MassIVE; O94855; -. DR MaxQB; O94855; -. DR PaxDb; 9606-ENSP00000280551; -. DR PeptideAtlas; O94855; -. DR ProteomicsDB; 50488; -. [O94855-1] DR ProteomicsDB; 50489; -. [O94855-2] DR Pumba; O94855; -. DR Antibodypedia; 26618; 128 antibodies from 25 providers. DR DNASU; 9871; -. DR Ensembl; ENST00000280551.11; ENSP00000280551.6; ENSG00000150961.15. [O94855-1] DR GeneID; 9871; -. DR KEGG; hsa:9871; -. DR MANE-Select; ENST00000280551.11; ENSP00000280551.6; NM_014822.4; NP_055637.2. DR UCSC; uc003ici.5; human. [O94855-1] DR AGR; HGNC:10706; -. DR CTD; 9871; -. DR DisGeNET; 9871; -. DR GeneCards; SEC24D; -. DR HGNC; HGNC:10706; SEC24D. DR HPA; ENSG00000150961; Low tissue specificity. DR MalaCards; SEC24D; -. DR MIM; 607186; gene. DR MIM; 616294; phenotype. DR neXtProt; NX_O94855; -. DR OpenTargets; ENSG00000150961; -. DR Orphanet; 2050; Cole-Carpenter syndrome. DR Orphanet; 216796; Osteogenesis imperfecta type 1. DR PharmGKB; PA35629; -. DR VEuPathDB; HostDB:ENSG00000150961; -. DR eggNOG; KOG1984; Eukaryota. DR GeneTree; ENSGT00950000182924; -. DR HOGENOM; CLU_004589_1_1_1; -. DR InParanoid; O94855; -. DR OMA; QNGAHAS; -. DR OrthoDB; 977017at2759; -. DR PhylomeDB; O94855; -. DR TreeFam; TF300464; -. DR PathwayCommons; O94855; -. 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; O94855; -. DR SIGNOR; O94855; -. DR BioGRID-ORCS; 9871; 6 hits in 1148 CRISPR screens. DR ChiTaRS; SEC24D; human. DR EvolutionaryTrace; O94855; -. DR GeneWiki; SEC24D; -. DR GenomeRNAi; 9871; -. DR Pharos; O94855; Tbio. DR PRO; PR:O94855; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O94855; Protein. DR Bgee; ENSG00000150961; Expressed in stromal cell of endometrium and 176 other cell types or tissues. DR ExpressionAtlas; O94855; baseline and differential. 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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0000149; F:SNARE binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. 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:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR CDD; cd01479; Sec24-like; 1. DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1. DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1. DR Gene3D; 3.40.20.10; Severin; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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 PANTHER; PTHR13803:SF6; PROTEIN TRANSPORT PROTEIN SEC24D; 1. DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1. 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; SSF81995; beta-sandwich domain of Sec23/24; 2. DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1. DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR Genevisible; O94855; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Craniosynostosis; Cytoplasm; KW Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum; KW ER-Golgi transport; Membrane; Metal-binding; Osteogenesis imperfecta; KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc. FT CHAIN 1..1032 FT /note="Protein transport protein Sec24D" FT /id="PRO_0000205157" FT REPEAT 901..974 FT /note="Gelsolin-like" FT /evidence="ECO:0000255" FT REGION 1..260 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 363..388 FT /note="Zinc finger-like" FT COMPBIAS 94..137 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 139..209 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 219..233 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 363 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT BINDING 366 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT BINDING 385 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT BINDING 388 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 224 FT /note="Q -> QA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_035761" FT VARIANT 42 FT /note="M -> T (in dbSNP:rs10029206)" FT /id="VAR_047472" FT VARIANT 193 FT /note="P -> L (in dbSNP:rs6844109)" FT /id="VAR_047473" FT VARIANT 496 FT /note="F -> I (in dbSNP:rs11723368)" FT /id="VAR_047474" FT VARIANT 978 FT /note="Q -> P (in CLCRP2; dbSNP:rs786204846)" FT /evidence="ECO:0000269|PubMed:25683121" FT /id="VAR_073658" FT VARIANT 1015 FT /note="S -> F (in CLCRP2; dbSNP:rs760670617)" FT /evidence="ECO:0000269|PubMed:25683121" FT /id="VAR_073659" FT CONFLICT 559 FT /note="P -> S (in Ref. 1; AAD28756 and 2; BAA34475)" FT /evidence="ECO:0000305" FT HELIX 267..278 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 281..284 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 312..322 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 323..329 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 364..366 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 386..388 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 415..418 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 420..425 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 441..447 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 450..454 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 457..468 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 469..471 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 484..498 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 507..511 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 522..527 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 529..532 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 533..548 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 558..571 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 575..581 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 587..589 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 607..611 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 614..616 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 617..627 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 630..636 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 644..647 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 649..653 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 658..660 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 666..682 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 685..695 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 699..707 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 711..714 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 716..724 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 727..735 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 739..741 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 742..752 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 758..771 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 773..778 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 782..796 FT /evidence="ECO:0007829|PDB:3EFO" FT TURN 797..799 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 802..823 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 832..835 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 837..839 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 842..851 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 853..855 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 858..861 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 863..875 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 878..885 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 888..891 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 897..899 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 910..912 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 918..922 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 924..931 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 937..944 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 945..948 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 949..951 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 966..978 FT /evidence="ECO:0007829|PDB:3EFO" FT STRAND 986..992 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 998..1001 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 1016..1029 FT /evidence="ECO:0007829|PDB:3EFO" SQ SEQUENCE 1032 AA; 113010 MW; B46E566F096F37F0 CRC64; MSQQGYVATP PYSQPQPGIG LSPPHYGHYG DPSHTASPTG MMKPAGPLGA TATRGMLPPG PPPPGPHQFG QNGAHATGHP PQRFPGPPPV NNVASSHAPY QPSAQSSYPG PISTSSVTQL GSQLSAMQIN SYGSGMAPPS QGPPGPLSAT SLQTPPRPPQ PSILQPGSQV LPPPPTTLNG PGASPLPLPM YRPDGLSGPP PPNAQYQPPP LPGQTLGAGY PPQQANSGPQ MAGAQLSYPG GFPGGPAQMA GPPQPQKKLD PDSIPSPIQV IENDRASRGG QVYATNTRGQ IPPLVTTDCM IQDQGNASPR FIRCTTYCFP CTSDMAKQAQ IPLAAVIKPF ATIPSNESPL YLVNHGESGP VRCNRCKAYM CPFMQFIEGG RRYQCGFCNC VNDVPPFYFQ HLDHIGRRLD HYEKPELSLG SYEYVATLDY CRKSKPPNPP AFIFMIDVSY SNIKNGLVKL ICEELKTMLE KIPKEEQEET SAIRVGFITY NKVLHFFNVK SNLAQPQMMV VTDVGEVFVP LLDGFLVNYQ ESQSVIHNLL DQIPDMFADS NENETVFAPV IQAGMEALKA ADCPGKLFIF HSSLPTAEAP GKLKNRDDKK LVNTDKEKIL FQPQTNVYDS LAKDCVAHGC SVTLFLFPSQ YVDVASLGLV PQLTGGTLYK YNNFQMHLDR QQFLNDLRND IEKKIGFDAI MRVRTSTGFR ATDFFGGILM NNTTDVEMAA IDCDKAVTVE FKHDDKLSED SGALIQCAVL YTTISGQRRL RIHNLGLNCS SQLADLYKSC ETDALINFFA KSAFKAVLHQ PLKVIREILV NQTAHMLACY RKNCASPSAA SQLILPDSMK VLPVYMNCLL KNCVLLSRPE ISTDERAYQR QLVMTMGVAD SQLFFYPQLL PIHTLDVKST MLPAAVRCSE SRLSEEGIFL LANGLHMFLW LGVSSPPELI QGIFNVPSFA HINTDMTLLP EVGNPYSQQL RMIMGIIQQK RPYSMKLTIV KQREQPEMVF RQFLVEDKGL YGGSSYVDFL CCVHKEICQL LN //