ID SMC3_MOUSE Reviewed; 1217 AA. AC Q9CW03; O35667; Q9QUS3; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 25-MAR-2003, sequence version 2. DT 14-OCT-2015, entry version 132. DE RecName: Full=Structural maintenance of chromosomes protein 3; DE Short=SMC protein 3; DE Short=SMC-3; DE AltName: Full=Basement membrane-associated chondroitin proteoglycan; DE Short=Bamacan; DE AltName: Full=Chondroitin sulfate proteoglycan 6; DE AltName: Full=Chromosome segregation protein SmcD; DE AltName: Full=Mad member-interacting protein 1; GN Name=Smc3; Synonyms=Bam, Bmh, Cspg6, Mmip1, Smc3l1, Smcd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10358101; DOI=10.1074/jbc.274.24.17384; RA Ghiselli G., Siracusa L.D., Iozzo R.V.; RT "Complete cDNA cloning, genomic organization, chromosomal assignment, RT functional characterization of the promoter, and expression of the RT murine Bamacan gene."; RL J. Biol. Chem. 274:17384-17393(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN A COHESIN RP COMPLEX WITH SMC1A AND RAD21. RX PubMed=10375619; DOI=10.1016/S0378-1119(99)00160-2; RA Darwiche N., Freeman L.A., Strunnikov A.; RT "Characterization of the components of the putative mammalian sister RT chromatid cohesion complex."; RL Gene 233:39-47(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 478-1217, INTERACTION WITH MXI1; MXD3 RP AND MXD4, AND MUTAGENESIS OF LEU-807. RC TISSUE=Embryo; RX PubMed=9528857; DOI=10.1038/sj.onc.1201634; RA Gupta K., Anand G., Yin X.Y., Prochownik E.V.; RT "Mmip1: a novel leucine zipper protein that reverses the suppressive RT effects of mad family members on C-myc."; RL Oncogene 16:1149-1159(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 887-1217. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP INTERACTION WITH STAG3. RX PubMed=11483963; DOI=10.1038/35087082; RA Prieto I., Suja J.A., Pezzi N., Kremer L., Martinez-A C., Rufas J.S., RA Barbero J.L.; RT "Mammalian STAG3 is a cohesin specific to sister chromatid arms in RT meiosis I."; RL Nat. Cell Biol. 3:761-766(2001). RN [6] RP INTERACTION WITH SMC1B. RX PubMed=11564881; DOI=10.1128/MCB.21.20.6984-6998.2001; RA Revenkova E., Eijpe M., Heyting C., Gross B., Jessberger R.; RT "Novel meiosis-specific isoform of mammalian SMC1."; RL Mol. Cell. Biol. 21:6984-6998(2001). RN [7] RP PHOSPHORYLATION AT SER-1013. RX PubMed=15378723; DOI=10.1002/rcm.1604; RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.; RT "Phosphoproteome analysis of mouse liver using immobilized metal RT affinity purification and linear ion trap mass spectrometry."; RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [10] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-1083. RX PubMed=22346761; DOI=10.1371/journal.pgen.1002485; RA Fukuda T., Pratto F., Schimenti J.C., Turner J.M., RA Camerini-Otero R.D., Hoeoeg C.; RT "Phosphorylation of chromosome core components may serve as axis marks RT for the status of chromosomal events during mammalian meiosis."; RL PLoS Genet. 8:E1002485-E1002485(2012). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-106, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Central component of cohesin, a complex required for CC chromosome cohesion during the cell cycle. The cohesin complex may CC form a large proteinaceous ring within which sister chromatids can CC be trapped. At anaphase, the complex is cleaved and dissociates CC from chromatin, allowing sister chromatids to segregate. Cohesion CC is coupled to DNA replication and is involved in DNA repair. The CC cohesin complex plays also an important role in spindle pole CC assembly during mitosis and in chromosomes movement. CC {ECO:0000269|PubMed:10375619}. CC -!- SUBUNIT: Interacts with NUMA1, and forms a ternary complex with CC KIF3B and KIFAP3, suggesting a function in tethering the CC chromosomes to the spindle pole and a function in chromosome CC movement. Interacts with SYCP2. Found in a complex with SMC1A, CC CDCA5 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Interacts with CC PDS5A and WAPAL; regulated by SMC3 acetylation (By similarity). CC Forms a heterodimer with SMC1A or SMC1B in cohesin complexes. CC Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and CC SMC3 heterodimer attached via their hinge domain, RAD21 which link CC them, and one STAG protein (STAG1, STAG2 or STAG3), which CC interacts with RAD21. Also found in meiosis-specific cohesin CC complexes. Interacts with MXI1, MXD3 and MXD4. Interacts with RPGR CC (By similarity). Interacts (via central hinge region) with CC KIAA1328 (via N- and C-terminal domains) (By similarity). CC {ECO:0000250, ECO:0000250|UniProtKB:Q9UQE7}. CC -!- INTERACTION: CC Q9Z2D6:Mecp2; NbExp=3; IntAct=EBI-2550068, EBI-1188816; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22346761}. CC Chromosome {ECO:0000269|PubMed:22346761}. Chromosome, centromere CC {ECO:0000269|PubMed:22346761}. Note=Associates with chromatin. CC Before prophase it is scattered along chromosome arms. During CC prophase, most of cohesin complexes dissociate from chromatin CC probably because of phosphorylation by PLK, except at centromeres, CC where cohesin complexes remain. At anaphase, the RAD21 subunit of CC the cohesin complex is cleaved, leading to the dissociation of the CC complex from chromosomes, allowing chromosome separation. The CC phosphorylated form at Ser-1083 is preferentially associated with CC unsynapsed chromosomal regions. CC -!- TISSUE SPECIFICITY: Widely expressed, with higher expression in CC testis and brain. CC -!- DOMAIN: The flexible hinge domain, which separates the large CC intramolecular coiled coil regions, allows the heterotypic CC interaction with the corresponding domain of SMC1A or SMC1B, CC forming a V-shaped heterodimer. The two heads of the heterodimer CC are then connected by different ends of the cleavable RAD21 CC protein, forming a ring structure (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated at Ser-1083 in a SPO11-dependent manner. CC {ECO:0000269|PubMed:15378723, ECO:0000269|PubMed:22346761}. CC -!- PTM: Acetylation at Lys-105 and Lys-106 by ESCO1 is important for CC genome stability and S phase sister chromatid cohesion. Regulated CC by DSCC1, it is required for processive DNA synthesis, coupling CC sister chromatid cohesion establishment during S phase to DNA CC replication (By similarity). Deacetylation by HDAC8, regulates CC release of the cohesin complex from chromatin (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. CC {ECO:0000305}. CC -!- CAUTION: Was originally isolated as a proteoglycan protein CC (explaining its name). Although not excluded, such secreted CC function is not clear. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA75400.1; Type=Frameshift; Positions=522, 1018, 1144; 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; AF141294; AAD42073.1; -; mRNA. DR EMBL; AF047601; AAD27754.1; -; mRNA. DR EMBL; Y15128; CAA75400.1; ALT_FRAME; mRNA. DR EMBL; AK005647; BAB24167.1; -; mRNA. DR CCDS; CCDS38025.1; -. DR RefSeq; NP_031816.2; NM_007790.3. DR UniGene; Mm.14910; -. DR PDB; 2WD5; X-ray; 2.70 A; B=484-696. DR PDBsum; 2WD5; -. DR ProteinModelPortal; Q9CW03; -. DR SMR; Q9CW03; 493-686. DR BioGrid; 198951; 12. DR DIP; DIP-57028N; -. DR IntAct; Q9CW03; 17. DR MINT; MINT-4134864; -. DR STRING; 10090.ENSMUSP00000025930; -. DR PhosphoSite; Q9CW03; -. DR MaxQB; Q9CW03; -. DR PaxDb; Q9CW03; -. DR PRIDE; Q9CW03; -. DR GeneID; 13006; -. DR KEGG; mmu:13006; -. DR UCSC; uc008hwy.2; mouse. DR CTD; 9126; -. DR MGI; MGI:1339795; Smc3. DR eggNOG; COG1196; -. DR HOGENOM; HOG000166512; -. DR HOVERGEN; HBG039849; -. DR InParanoid; Q9CW03; -. DR KO; K06669; -. DR OMA; NRLFHHV; -. DR OrthoDB; EOG73803T; -. DR PhylomeDB; Q9CW03; -. DR TreeFam; TF105602; -. DR Reactome; R-MMU-1221632; Meiotic synapsis. DR Reactome; R-MMU-1221633; Meiotic Synapsis. DR Reactome; R-MMU-2467813; Separation of Sister Chromatids. DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion. DR Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin. DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins. DR ChiTaRS; Smc3; mouse. DR EvolutionaryTrace; Q9CW03; -. DR NextBio; 282832; -. DR PRO; PR:Q9CW03; -. DR Proteomes; UP000000589; Unplaced. DR Bgee; Q9CW03; -. DR CleanEx; MM_SMC3; -. DR ExpressionAtlas; Q9CW03; baseline and differential. DR Genevisible; Q9CW03; MM. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0008280; C:cohesin core heterodimer; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0000800; C:lateral element; IDA:MGI. DR GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB. DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0045502; F:dynein binding; ISS:UniProtKB. DR GO; GO:0036033; F:mediator complex binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0007126; P:meiotic nuclear division; ISS:UniProtKB. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:InterPro. DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB. DR GO; GO:0032876; P:negative regulation of DNA endoreduplication; ISO:MGI. DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB. DR GO; GO:0007062; P:sister chromatid cohesion; ISO:MGI. DR GO; GO:0019827; P:stem cell maintenance; IMP:MGI. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR InterPro; IPR024704; SMC. DR InterPro; IPR029685; SMC3. DR InterPro; IPR010935; SMC_hinge. DR PANTHER; PTHR18937:SF164; PTHR18937:SF164; 1. DR Pfam; PF06470; SMC_hinge; 1. DR Pfam; PF02463; SMC_N; 1. DR PIRSF; PIRSF005719; SMC; 1. DR SMART; SM00968; SMC_hinge; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF75553; SSF75553; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; KW Centromere; Chromosome; Coiled coil; Complete proteome; DNA damage; KW DNA repair; Meiosis; Mitosis; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1 1217 Structural maintenance of chromosomes FT protein 3. FT /FTId=PRO_0000119002. FT NP_BIND 32 39 ATP. {ECO:0000255}. FT REGION 505 667 Flexible hinge. FT COILED 179 350 {ECO:0000255}. FT COILED 393 503 {ECO:0000255}. FT COILED 669 916 {ECO:0000255}. FT COILED 958 989 {ECO:0000255}. FT COMPBIAS 1115 1150 Ala/Asp-rich (DA-box). FT MOD_RES 105 105 N6-acetyllysine. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 106 106 N6-acetyllysine. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 140 140 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9UQE7}. FT MOD_RES 783 783 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q9UQE7}. FT MOD_RES 787 787 Phosphoserine. FT {ECO:0000244|PubMed:17525332}. FT MOD_RES 1013 1013 Phosphoserine. FT {ECO:0000269|PubMed:15378723}. FT MOD_RES 1065 1065 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9UQE7}. FT MOD_RES 1067 1067 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 1074 1074 Phosphoserine. FT {ECO:0000250|UniProtKB:P97690}. FT MOD_RES 1083 1083 Phosphoserine. FT {ECO:0000269|PubMed:22346761}. FT MOD_RES 1190 1190 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9UQE7}. FT MUTAGEN 807 807 L->P: Abolishes interaction with MXI1. FT {ECO:0000269|PubMed:9528857}. FT CONFLICT 999 999 K -> R (in Ref. 3; CAA75400). FT {ECO:0000305}. FT CONFLICT 1175 1175 F -> L (in Ref. 3). {ECO:0000305}. FT HELIX 495 498 {ECO:0000244|PDB:2WD5}. FT TURN 499 501 {ECO:0000244|PDB:2WD5}. FT HELIX 502 522 {ECO:0000244|PDB:2WD5}. FT HELIX 526 529 {ECO:0000244|PDB:2WD5}. FT STRAND 532 535 {ECO:0000244|PDB:2WD5}. FT HELIX 536 538 {ECO:0000244|PDB:2WD5}. FT STRAND 539 541 {ECO:0000244|PDB:2WD5}. FT HELIX 544 546 {ECO:0000244|PDB:2WD5}. FT HELIX 547 554 {ECO:0000244|PDB:2WD5}. FT HELIX 557 559 {ECO:0000244|PDB:2WD5}. FT STRAND 561 564 {ECO:0000244|PDB:2WD5}. FT HELIX 566 578 {ECO:0000244|PDB:2WD5}. FT STRAND 585 589 {ECO:0000244|PDB:2WD5}. FT TURN 590 592 {ECO:0000244|PDB:2WD5}. FT STRAND 604 608 {ECO:0000244|PDB:2WD5}. FT HELIX 609 612 {ECO:0000244|PDB:2WD5}. FT HELIX 617 619 {ECO:0000244|PDB:2WD5}. FT HELIX 620 627 {ECO:0000244|PDB:2WD5}. FT STRAND 630 635 {ECO:0000244|PDB:2WD5}. FT HELIX 636 645 {ECO:0000244|PDB:2WD5}. FT STRAND 649 651 {ECO:0000244|PDB:2WD5}. FT STRAND 664 666 {ECO:0000244|PDB:2WD5}. FT HELIX 676 685 {ECO:0000244|PDB:2WD5}. SQ SEQUENCE 1217 AA; 141556 MW; 11FF55165BE6A88E CRC64; MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLEHFR RKGINQHVQN GYHGIVMNNF ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSGESERG SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV ITAEMAKDFV EDDTTHG //