SMC1A_MOUSE
ID SMC1A_MOUSE Reviewed; 1233 AA.
AC Q9CU62; A2AFQ5; Q3V480; Q9CUX9; Q9D959; Q9WTU1;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Structural maintenance of chromosomes protein 1A;
DE Short=SMC protein 1A;
DE Short=SMC-1-alpha;
DE Short=SMC-1A;
DE AltName: Full=Chromosome segregation protein SmcB;
DE AltName: Full=Sb1.8;
GN Name=Smc1a; Synonyms=Sb1.8, Smc1, Smc1l1, Smcb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND IDENTIFICATION IN A
RP COHESIN COMPLEX WITH SMC3 AND RAD21.
RC TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-301 AND 977-1233.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, Pancreas, and Thymus;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 meiosis
RT I.";
RL Nat. Cell Biol. 3:761-766(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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 expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=22977523; DOI=10.3892/etm.2011.232;
RA So E.Y., Ouchi T.;
RT "Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK
RT catalytic subunit.";
RL Exp. Ther. Med. 2:443-447(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1037, AND IDENTIFICATION BY MASS
RP 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., Zhang Y.,
RA 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: Involved in chromosome cohesion during cell cycle and in DNA
CC repair. Involved in DNA repair via its interaction with BRCA1 and its
CC related phosphorylation by ATM, and works as a downstream effector in
CC the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central
CC component of cohesin complex. The cohesin complex is required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the complex is cleaved and
CC dissociates from chromatin, allowing sister chromatids to segregate.
CC The cohesin complex may also play a role in spindle pole assembly
CC during mitosis. Involved in DNA repair via its interaction with BRCA1
CC and its related phosphorylation by ATM, or via its phosphorylation by
CC ATR. Works as a downstream effector both in the ATM/NBS1 branch and in
CC the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC3 in cohesin complexes. Cohesin
CC complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3
CC heterodimer attached via their SMC hinge domain, RAD21 which link them,
CC and one STAG protein (STAG1, STAG2 or STAG3), which interacts with
CC RAD21. In germ cell cohesin complexes, SMC1A is mutually exclusive with
CC SMC1B (PubMed:10375619). Interacts with STAG3 (PubMed:11483963). Found
CC in a complex with CDCA5, SMC3 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN.
CC Found in a complex containing POLE and SMC3. Interacts with BRCA1,
CC SYCP2, NDC80, RPGR and BRAT1. Found in a cohesin complex with SMC3,
CC STAG1 and RAD21. The SMC1A-SMC3 heterodimer interacts with the NIPBL-
CC MAU2 heterodimer (By similarity). {ECO:0000250|UniProtKB:O97593,
CC ECO:0000250|UniProtKB:Q14683, ECO:0000250|UniProtKB:Q9Z1M9,
CC ECO:0000269|PubMed:10375619, ECO:0000269|PubMed:11483963}.
CC -!- INTERACTION:
CC Q9CU62; Q61687: Atrx; NbExp=4; IntAct=EBI-2550016, EBI-2657527;
CC Q9CU62; Q6A078: Cep290; NbExp=2; IntAct=EBI-2550016, EBI-1811999;
CC Q9CU62; Q9Z2D6: Mecp2; NbExp=3; IntAct=EBI-2550016, EBI-1188816;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC Note=Associates with chromatin. The phosphorylated form on Ser-957 and
CC Ser-966 associates with chromatin during G1/S/G2 phases but not during
CC M phase, suggesting that phosphorylation does not regulate cohesin
CC function (By similarity). Before prophase it is scattered along
CC chromosome arms. During prophase, most of cohesin complexes dissociate
CC from chromatin probably because of phosphorylation by PLK, except at
CC centromeres, where cohesin complexes remain. At anaphase, the RAD21
CC subunit of the cohesin complex is cleaved, leading to the dissociation
CC of the complex from chromosomes, allowing chromosome separation. In
CC germ cells, cohesin complex dissociates from chromatin at prophase I,
CC and may be replaced by a meiosis-specific cohesin complex.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level).
CC {ECO:0000269|PubMed:22977523}.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC3, forming a V-shaped heterodimer.
CC The two heads of the heterodimer are then connected by different ends
CC of the cleavable RAD21 protein, forming a ring structure (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated upon ionizing radiation or DNA methylation.
CC Phosphorylation of Ser-957 and Ser-966 activates it and is required for
CC S-phase checkpoint activation (By similarity).
CC {ECO:0000250|UniProtKB:Q14683}.
CC -!- PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its
CC degradation. {ECO:0000250|UniProtKB:Q14683}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily. {ECO:0000305}.
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DR EMBL; AF047600; AAD27753.1; -; mRNA.
DR EMBL; AL672180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131667; AAI31668.1; -; mRNA.
DR EMBL; AK007334; BAE43202.1; -; mRNA.
DR EMBL; AK013648; BAB28937.1; -; mRNA.
DR EMBL; AK017948; BAB31016.3; -; mRNA.
DR EMBL; AK088183; BAC40193.1; -; mRNA.
DR CCDS; CCDS30473.1; -.
DR RefSeq; NP_062684.2; NM_019710.2.
DR PDB; 2WD5; X-ray; 2.70 A; A=461-685.
DR PDB; 7DG5; X-ray; 2.00 A; A/C=471-685.
DR PDBsum; 2WD5; -.
DR PDBsum; 7DG5; -.
DR AlphaFoldDB; Q9CU62; -.
DR SMR; Q9CU62; -.
DR BioGRID; 204874; 47.
DR CORUM; Q9CU62; -.
DR DIP; DIP-57021N; -.
DR IntAct; Q9CU62; 38.
DR MINT; Q9CU62; -.
DR STRING; 10090.ENSMUSP00000044645; -.
DR iPTMnet; Q9CU62; -.
DR PhosphoSitePlus; Q9CU62; -.
DR EPD; Q9CU62; -.
DR MaxQB; Q9CU62; -.
DR PaxDb; Q9CU62; -.
DR PeptideAtlas; Q9CU62; -.
DR PRIDE; Q9CU62; -.
DR ProteomicsDB; 257203; -.
DR Antibodypedia; 491; 1021 antibodies from 43 providers.
DR DNASU; 24061; -.
DR Ensembl; ENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133.
DR GeneID; 24061; -.
DR KEGG; mmu:24061; -.
DR UCSC; uc009upx.2; mouse.
DR CTD; 8243; -.
DR MGI; MGI:1344345; Smc1a.
DR VEuPathDB; HostDB:ENSMUSG00000041133; -.
DR eggNOG; KOG0018; Eukaryota.
DR GeneTree; ENSGT00940000155614; -.
DR HOGENOM; CLU_001042_0_2_1; -.
DR InParanoid; Q9CU62; -.
DR OMA; YIRDHTT; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; Q9CU62; -.
DR TreeFam; TF101156; -.
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 BioGRID-ORCS; 24061; 31 hits in 115 CRISPR screens.
DR ChiTaRS; Smc1a; mouse.
DR EvolutionaryTrace; Q9CU62; -.
DR PRO; PR:Q9CU62; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CU62; protein.
DR Bgee; ENSMUSG00000041133; Expressed in undifferentiated genital tubercle and 263 other tissues.
DR ExpressionAtlas; Q9CU62; baseline and differential.
DR Genevisible; Q9CU62; MM.
DR GO; GO:0008278; C:cohesin complex; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
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; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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:0051321; P:meiotic cell cycle; IPI:MGI.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0072423; P:response to DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISO:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR CDD; cd03275; ABC_SMC1_euk; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR028468; Smc1_ABC.
DR InterPro; IPR029683; SMC1A_metazoan.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF170; PTHR18937:SF170; 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; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Centromere; Chromosome; Coiled coil; DNA damage; DNA repair; Meiosis;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1233
FT /note="Structural maintenance of chromosomes protein 1A"
FT /id="PRO_0000118990"
FT DOMAIN 515..629
FT /note="SMC hinge"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..124
FT /evidence="ECO:0000255"
FT COILED 163..503
FT /evidence="ECO:0000255"
FT COILED 667..935
FT /evidence="ECO:0000255"
FT COILED 988..1068
FT /evidence="ECO:0000255"
FT COMPBIAS 949..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 648
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 713
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 1037
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 321
FT /note="N -> H (in Ref. 1; AAD27753)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="E -> G (in Ref. 1; AAD27753)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="K -> E (in Ref. 1; AAD27753)"
FT /evidence="ECO:0000305"
FT CONFLICT 944
FT /note="K -> E (in Ref. 1; AAD27753)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="A -> G (in Ref. 4; BAE43202)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="Q -> R (in Ref. 1; AAD27753)"
FT /evidence="ECO:0000305"
FT HELIX 495..510
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 531..538
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 539..543
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 550..563
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:7DG5"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 583..587
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 594..597
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 606..613
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 622..630
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 631..634
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 656..662
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 665..672
FT /evidence="ECO:0007829|PDB:7DG5"
SQ SEQUENCE 1233 AA; 143235 MW; E62CEB174854D9A6 CRC64;
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK
IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE
QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ
TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGSSQGE
ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI
AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL
LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ
