SC24D_HUMAN
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 03-AUG-2022, entry version 183.
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};
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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. [O94855-2]
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; 49.
DR IntAct; O94855; 20.
DR MINT; O94855; -.
DR STRING; 9606.ENSP00000280551; -.
DR GlyGen; O94855; 1 site, 1 O-linked glycan (1 site).
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; O94855; -.
DR PeptideAtlas; O94855; -.
DR PRIDE; O94855; -.
DR ProteomicsDB; 50488; -. [O94855-1]
DR ProteomicsDB; 50489; -. [O94855-2]
DR Antibodypedia; 26618; 108 antibodies from 24 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 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; NSMMPGP; -.
DR OrthoDB; 330236at2759; -.
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 1070 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 174 other tissues.
DR ExpressionAtlas; O94855; baseline and differential.
DR Genevisible; O94855; 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: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; 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; 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
