ID SMC2_HUMAN Reviewed; 1197 AA.
AC O95347; Q6IEE0; Q9P1P2;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 197.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE Short=SMC protein 2;
DE Short=SMC-2;
DE AltName: Full=Chromosome-associated protein E;
DE Short=hCAP-E;
DE AltName: Full=XCAP-E homolog;
GN Name=SMC2; Synonyms=CAPE, SMC2L1; ORFNames=PRO0324;
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 INTERACTION WITH SMC4.
RC TISSUE=Teratocarcinoma;
RX PubMed=9789013; DOI=10.1073/pnas.95.22.12906;
RA Schmiesing J.A., Ball A.R. Jr., Gregson H.C., Alderton J.M., Zhou S.,
RA Yokomori K.;
RT "Identification of two distinct human SMC protein complexes involved in
RT mitotic chromosome dynamics.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12906-12911(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1197 (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W.,
RA Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 32 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [8]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4 AND CNAP1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10958694; DOI=10.1128/mcb.20.18.6996-7006.2000;
RA Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.;
RT "A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of
RT Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the
RT early stage of mitotic chromosome condensation.";
RL Mol. Cell. Biol. 20:6996-7006(2000).
RN [9]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; BRRN1; CNAP1 AND CAPG, AND
RP FUNCTION OF THE COMPLEX.
RX PubMed=11136719; DOI=10.1074/jbc.c000873200;
RA Kimura K., Cuvier O., Hirano T.;
RT "Chromosome condensation by a human condensin complex in Xenopus egg
RT extracts.";
RL J. Biol. Chem. 276:5417-5420(2001).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-222; LYS-677; LYS-1158
RP AND LYS-1160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
RP INTERACTION WITH BRD4.
RX PubMed=23728299; DOI=10.1038/nature12147;
RA Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C., Cannell I.G.,
RA Bryson B.D., Rameseder J., Lee M.J., Blake E.J., Fydrych A., Ho R.,
RA Greenberger B.A., Chen G.C., Maffa A., Del Rosario A.M., Root D.E.,
RA Carpenter A.E., Hahn W.C., Sabatini D.M., Chen C.C., White F.M.,
RA Bradner J.E., Yaffe M.B.;
RT "The bromodomain protein Brd4 insulates chromatin from DNA damage
RT signalling.";
RL Nature 498:246-250(2013).
RN [13]
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: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.
CC -!- SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three non
CC SMC subunits that probably regulate the complex: BRRN1/CAPH,
CC CNAP1/CAPD2 and CAPG. Interacts with BRD4 (isoform B), leading to
CC insulate chromatin from DNA damage response pathway.
CC {ECO:0000269|PubMed:10958694, ECO:0000269|PubMed:11136719,
CC ECO:0000269|PubMed:23728299, ECO:0000269|PubMed:9789013}.
CC -!- INTERACTION:
CC O95347; Q15003: NCAPH; NbExp=5; IntAct=EBI-355822, EBI-1046410;
CC O95347; Q6IBW4: NCAPH2; NbExp=2; IntAct=EBI-355822, EBI-2548296;
CC O95347; Q9NTJ3: SMC4; NbExp=3; IntAct=EBI-355822, EBI-356173;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}. Cytoplasm
CC {ECO:0000269|PubMed:10958694}. Chromosome
CC {ECO:0000269|PubMed:10958694}. Note=In interphase cells, the majority
CC of the condensin complex is found in the cytoplasm, while a minority of
CC the complex is associated with chromatin. A subpopulation of the
CC complex however remains associated with chromosome foci in interphase
CC cells. During mitosis, most of the condensin complex is associated with
CC the chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDC2, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95347-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95347-2; Sequence=VSP_007243, VSP_007244;
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC4, forming a
CC V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72360.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF29579.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF092563; AAC72360.1; ALT_FRAME; mRNA.
DR EMBL; AL833191; CAI46187.1; -; mRNA.
DR EMBL; AL161791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58973.1; -; Genomic_DNA.
DR EMBL; BC130385; AAI30386.1; -; mRNA.
DR EMBL; AF113673; AAF29579.1; ALT_INIT; mRNA.
DR EMBL; BN000163; CAD89875.1; -; mRNA.
DR CCDS; CCDS35086.1; -. [O95347-1]
DR RefSeq; NP_001036015.1; NM_001042550.1. [O95347-1]
DR RefSeq; NP_001036016.1; NM_001042551.1. [O95347-1]
DR RefSeq; NP_001252531.1; NM_001265602.1. [O95347-1]
DR RefSeq; NP_006435.2; NM_006444.2. [O95347-1]
DR RefSeq; XP_006716996.1; XM_006716933.3. [O95347-1]
DR RefSeq; XP_011516450.1; XM_011518148.2. [O95347-1]
DR RefSeq; XP_011516451.1; XM_011518149.2. [O95347-1]
DR RefSeq; XP_011516455.1; XM_011518153.1. [O95347-2]
DR RefSeq; XP_016869695.1; XM_017014206.1. [O95347-1]
DR RefSeq; XP_016869696.1; XM_017014207.1.
DR RefSeq; XP_016869697.1; XM_017014208.1. [O95347-1]
DR PDB; 4U4P; X-ray; 1.89 A; A=476-707.
DR PDBsum; 4U4P; -.
DR AlphaFoldDB; O95347; -.
DR EMDB; EMD-10827; -.
DR EMDB; EMD-10833; -.
DR SMR; O95347; -.
DR BioGRID; 115841; 297.
DR ComplexPortal; CPX-979; Condensin I complex.
DR ComplexPortal; CPX-985; Condensin II complex.
DR CORUM; O95347; -.
DR DIP; DIP-35422N; -.
DR IntAct; O95347; 91.
DR MINT; O95347; -.
DR STRING; 9606.ENSP00000286398; -.
DR ChEMBL; CHEMBL4105890; -.
DR GlyGen; O95347; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O95347; -.
DR MetOSite; O95347; -.
DR PhosphoSitePlus; O95347; -.
DR SwissPalm; O95347; -.
DR BioMuta; SMC2; -.
DR EPD; O95347; -.
DR jPOST; O95347; -.
DR MassIVE; O95347; -.
DR MaxQB; O95347; -.
DR PaxDb; 9606-ENSP00000286398; -.
DR PeptideAtlas; O95347; -.
DR ProteomicsDB; 50812; -. [O95347-1]
DR ProteomicsDB; 50813; -. [O95347-2]
DR Pumba; O95347; -.
DR Antibodypedia; 14701; 303 antibodies from 33 providers.
DR DNASU; 10592; -.
DR Ensembl; ENST00000286398.11; ENSP00000286398.7; ENSG00000136824.19. [O95347-1]
DR Ensembl; ENST00000374787.7; ENSP00000363919.3; ENSG00000136824.19. [O95347-1]
DR Ensembl; ENST00000374793.8; ENSP00000363925.3; ENSG00000136824.19. [O95347-1]
DR GeneID; 10592; -.
DR KEGG; hsa:10592; -.
DR MANE-Select; ENST00000374793.8; ENSP00000363925.3; NM_006444.3; NP_006435.2.
DR UCSC; uc004bbw.4; human. [O95347-1]
DR AGR; HGNC:14011; -.
DR CTD; 10592; -.
DR DisGeNET; 10592; -.
DR GeneCards; SMC2; -.
DR HGNC; HGNC:14011; SMC2.
DR HPA; ENSG00000136824; Tissue enhanced (lymphoid).
DR MIM; 605576; gene.
DR neXtProt; NX_O95347; -.
DR OpenTargets; ENSG00000136824; -.
DR PharmGKB; PA37833; -.
DR VEuPathDB; HostDB:ENSG00000136824; -.
DR eggNOG; KOG0933; Eukaryota.
DR GeneTree; ENSGT00550000074857; -.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; O95347; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 231904at2759; -.
DR PhylomeDB; O95347; -.
DR TreeFam; TF101157; -.
DR PathwayCommons; O95347; -.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
DR SignaLink; O95347; -.
DR SIGNOR; O95347; -.
DR BioGRID-ORCS; 10592; 789 hits in 1139 CRISPR screens.
DR ChiTaRS; SMC2; human.
DR GeneWiki; SMC2; -.
DR GenomeRNAi; 10592; -.
DR Pharos; O95347; Tchem.
DR PRO; PR:O95347; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O95347; Protein.
DR Bgee; ENSG00000136824; Expressed in ventricular zone and 181 other cell types or tissues.
DR ExpressionAtlas; O95347; baseline and differential.
DR Genevisible; O95347; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:ComplexPortal.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051383; P:kinetochore organization; IEA:Ensembl.
DR GO; GO:0010032; P:meiotic chromosome condensation; IEA:Ensembl.
DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:Ensembl.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; IDA:ComplexPortal.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; ISO:ComplexPortal.
DR GO; GO:1905820; P:positive regulation of chromosome separation; ISO:ComplexPortal.
DR CDD; cd03273; ABC_SMC2_euk; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Chromosome; Coiled coil; Cytoplasm; DNA condensation;
KW Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1197
FT /note="Structural maintenance of chromosomes protein 2"
FT /id="PRO_0000118995"
FT DOMAIN 522..640
FT /note="SMC hinge"
FT COILED 173..507
FT /evidence="ECO:0000255"
FT COILED 672..926
FT /evidence="ECO:0000255"
FT COILED 963..1031
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 677
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1160
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1091..1099
FT /note="SLVALSLIL -> QKQQNHTTG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_007243"
FT VAR_SEQ 1100..1197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_007244"
FT VARIANT 1009
FT /note="E -> K (in dbSNP:rs4562395)"
FT /id="VAR_047489"
FT CONFLICT 294
FT /note="G -> V (in Ref. 1; AAC72360)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="N -> H (in Ref. 1; AAC72360)"
FT /evidence="ECO:0000305"
FT CONFLICT 998
FT /note="Y -> C (in Ref. 1; AAC72360)"
FT /evidence="ECO:0000305"
FT HELIX 476..502
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 538..545
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 557..566
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:4U4P"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 588..598
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 617..624
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 633..640
FT /evidence="ECO:0007829|PDB:4U4P"
FT TURN 643..645
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:4U4P"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 674..704
FT /evidence="ECO:0007829|PDB:4U4P"
SQ SEQUENCE 1197 AA; 135656 MW; 15EBB56B31FC1364 CRC64;
MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS
NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE ITVTRQVVIG GRNKYLINGV
NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA
AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL
LAEDTKVRSA EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE
DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK EVKKITDGLH
ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMMACKNDIS KAQTEAKQAQ
MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA LEAVKRLKEK LEAEMKKLNY EENKEESLLE
KRRQLSRDIG RLKETYEALL ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA
LELVAGERLY NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP
DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV TLGGDVFDPH
GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE ELAGLKNTAE KYRQLKQQWE
MKTEEADLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK NTKEIQRKAE EKYEVLENKM
KNAEAERERE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL
EAVNEAIKSY ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK
EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ PNSAYDFKTN
NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND LMKKKRIVEN DKSKILTTIE
DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE
NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF
IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV
//
