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   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.
DR   Genevisible; O95347; HS.
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
//