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   27-MAR-2024, entry version 192.
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,
RC   Pancreas, 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. The cohesin complex interacts with the
CC       cohesin loading complex subunits NIPBL/Scc2 (via HEAT repeats) and
CC       MAU2/Scc4. NIPBL directly contacts all members of the complex, RAD21,
CC       SMC1A/B, SMC3 and STAG1 (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; 49.
DR   CORUM; Q9CU62; -.
DR   DIP; DIP-57021N; -.
DR   IntAct; Q9CU62; 40.
DR   MINT; Q9CU62; -.
DR   STRING; 10090.ENSMUSP00000044645; -.
DR   GlyGen; Q9CU62; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CU62; -.
DR   PhosphoSitePlus; Q9CU62; -.
DR   SwissPalm; Q9CU62; -.
DR   EPD; Q9CU62; -.
DR   MaxQB; Q9CU62; -.
DR   PaxDb; 10090-ENSMUSP00000044645; -.
DR   PeptideAtlas; Q9CU62; -.
DR   ProteomicsDB; 257203; -.
DR   Pumba; Q9CU62; -.
DR   Antibodypedia; 491; 1147 antibodies from 43 providers.
DR   DNASU; 24061; -.
DR   Ensembl; ENSMUST00000045312.6; ENSMUSP00000044645.6; ENSMUSG00000041133.12.
DR   GeneID; 24061; -.
DR   KEGG; mmu:24061; -.
DR   UCSC; uc009upx.2; mouse.
DR   AGR; MGI:1344345; -.
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; SYIRDHT; -.
DR   OrthoDB; 231904at2759; -.
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 121 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 266 other cell types or tissues.
DR   ExpressionAtlas; Q9CU62; baseline and differential.
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:0000800; C:lateral element; ISO:MGI.
DR   GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
DR   GO; GO:0030892; C:mitotic cohesin complex; ISO:MGI.
DR   GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR   GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:CAFA.
DR   GO; GO:0000795; C:synaptonemal complex; ISO:MGI.
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: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; 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; IPR028468; Smc1_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF170; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 1A; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
DR   Genevisible; Q9CU62; MM.
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
//