RAD21_MOUSE
ID RAD21_MOUSE Reviewed; 635 AA.
AC Q61550; P70219; Q3TQ09; Q810A8; Q91VB9; Q9DBU4;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Double-strand-break repair protein rad21 homolog;
DE Short=mHR21 {ECO:0000303|PubMed:8812457};
DE AltName: Full=Pokeweed agglutinin-binding protein 29;
DE Short=PW29 {ECO:0000303|PubMed:8521526};
DE AltName: Full=SCC1 homolog;
DE Contains:
DE RecName: Full=64-kDa C-terminal product;
DE AltName: Full=64-kDa carboxy-terminal product {ECO:0000250|UniProtKB:O60216};
GN Name=Rad21;
GN Synonyms=Hr21 {ECO:0000303|PubMed:8812457},
GN Scc1 {ECO:0000250|UniProtKB:O60216};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Teratocarcinoma;
RX PubMed=8521526; DOI=10.1247/csf.20.263;
RA Yu S., Ozawa M., Naved A.F., Miyauchi T., Muramatsu H., Muramatsu T.;
RT "cDNA cloning and sequence analysis of a novel calcium binding protein with
RT oligoproline motif.";
RL Cell Struct. Funct. 20:263-268(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8812457; DOI=10.1006/geno.1996.0466;
RA McKay M.J., Troelstra C., van der Spek P., Kanaar R., Smit B.,
RA Hagemeijer A., Bootsma D., Hoeijmakers J.H.J.;
RT "Sequence conservation of the rad21 Schizosaccharomyces pombe DNA double-
RT strand break repair gene in human and mouse.";
RL Genomics 36:305-315(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 IDENTIFICATION IN THE COHESIN COMPLEX, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP FUNCTION, AND INTERACTION WITH SMC1; SMC3 AND STAG1.
RX PubMed=18237772; DOI=10.1016/j.cell.2008.01.011;
RA Parelho V., Hadjur S., Spivakov M., Leleu M., Sauer S., Gregson H.C.,
RA Jarmuz A., Canzonetta C., Webster Z., Nesterova T., Cobb B.S., Yokomori K.,
RA Dillon N., Aragon L., Fisher A.G., Merkenschlager M.;
RT "Cohesins functionally associate with CTCF on mammalian chromosome arms.";
RL Cell 132:422-433(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-175, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, 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).
CC -!- FUNCTION: [Double-strand-break repair protein rad21 homolog]: As a
CC member of the cohesin complex, involved in sister chromatid cohesion
CC from the time of DNA replication in S phase to their segregation in
CC mitosis, a function that is essential for proper chromosome
CC segregation, post-replicative DNA repair, and the prevention of
CC inappropriate recombination between repetitive regions. The cohesin
CC complex may also play a role in spindle pole assembly during mitosis
CC (By similarity). In interphase, cohesins may function in the control of
CC gene expression by binding to numerous sites within the genome
CC (PubMed:18237772). May control RUNX1 gene expression. Binds to and
CC represses APOB gene promoter (By similarity). May play a role in
CC embryonic gut development, possibly through the regulation of enteric
CC neuron development (By similarity). {ECO:0000250|UniProtKB:O60216,
CC ECO:0000250|UniProtKB:Q6TEL1, ECO:0000269|PubMed:18237772}.
CC -!- FUNCTION: [64-kDa C-terminal product]: May promote apoptosis.
CC {ECO:0000250|UniProtKB:O60216}.
CC -!- SUBUNIT: Component of the cohesin complex, which consists of an SMC1A/B
CC and SMC3 heterodimer core and 2 non-Smc subunits RAD21 and STAG1/SA1,
CC STAG2/SA2 or STAG3/SA3 (PubMed:10375619, PubMed:18237772). Interacts
CC (via N-terminus) with SMC1A; the interaction is direct (By similarity).
CC The cohesin complex interacts with NUMA1. The cohesin complex also
CC interacts with CDCA5, PDS5A and PDS5B; this interaction might regulate
CC the ability of the cohesin complex to mediate sister chromatid
CC cohesion. The interaction with PDS5B is direct and is stimulated by
CC STAG1/SA1. The cohesin complex interacts with the cohesin loading
CC complex subunits NIPBL/Scc2 (via HEAT repeats) and MAU2/Scc4. The
CC cohesin complex interacts with DDX11/ChIR1. Directly interacts with
CC WAPL; this interaction is stimulated by STAG1/SA1 (By similarity).
CC Interacts with the ISWI chromatin remodeling complex component SMARCA5;
CC the interaction is direct (By similarity). Interacts with the NuRD
CC complex component CHD4; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:O60216, ECO:0000269|PubMed:10375619,
CC ECO:0000269|PubMed:18237772}.
CC -!- SUBCELLULAR LOCATION: [Double-strand-break repair protein rad21
CC homolog]: Nucleus {ECO:0000269|PubMed:10375619}. Chromosome
CC {ECO:0000269|PubMed:10375619}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O60216}. Note=Associates with chromatin. Before
CC prophase, scattered along chromosome arms. During prophase and
CC prometaphase, most cohesins dissociate from the arms of condensing
CC chromosome, possibly through PLK1-mediated phosphorylation (By
CC similarity). A small amount of cohesin remains in centromeric regions
CC and is removed from chromosomes only at the onset of anaphase. At
CC anaphase, cleavage by separase/ESPL1 leads to the dissociation of
CC cohesin from chromosomes and chromosome separation (By similarity).
CC {ECO:0000250|UniProtKB:O60216, ECO:0000250|UniProtKB:O93310}.
CC -!- SUBCELLULAR LOCATION: [64-kDa C-terminal product]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O60216}. Nucleus {ECO:0000250|UniProtKB:O60216}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis,
CC brain, kidney, heart and thymus. Lowest levels in skeletal muscle.
CC {ECO:0000269|PubMed:8521526, ECO:0000269|PubMed:8812457}.
CC -!- DEVELOPMENTAL STAGE: Not regulated during the cell cycle (at protein
CC level). {ECO:0000269|PubMed:10375619}.
CC -!- DOMAIN: The C-terminal part associates with the head of SMC1A, while
CC the N-terminal part binds to the head of SMC3. {ECO:0000250}.
CC -!- PTM: Cleaved by separase/ESPL1 at the onset of anaphase; this cleavage
CC is required for sister chromatid separation and cytokinesis. Cleaved by
CC caspase-3/CASP3 or caspase-7/CASP7 at the beginning of apoptosis.
CC {ECO:0000250|UniProtKB:O60216}.
CC -!- PTM: Phosphorylated; becomes hyperphosphorylated in M phase of cell
CC cycle. The large dissociation of cohesin from chromosome arms during
CC prophase may be partly due to its phosphorylation by PLK1.
CC {ECO:0000250|UniProtKB:O60216}.
CC -!- MISCELLANEOUS: Seems to bind calcium.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR EMBL; D49429; BAA08408.1; -; mRNA.
DR EMBL; X98293; CAA66939.1; -; mRNA.
DR EMBL; AF332086; AAK56114.1; -; mRNA.
DR EMBL; AF332085; AAK56113.1; -; mRNA.
DR EMBL; AK004746; BAB23527.1; -; mRNA.
DR EMBL; AK163992; BAE37576.1; -; mRNA.
DR EMBL; BC043032; AAH43032.2; -; mRNA.
DR CCDS; CCDS27463.1; -.
DR PIR; JC4248; JC4248.
DR RefSeq; NP_033035.3; NM_009009.4.
DR RefSeq; XP_006520707.1; XM_006520644.1.
DR RefSeq; XP_006520708.1; XM_006520645.1.
DR AlphaFoldDB; Q61550; -.
DR SMR; Q61550; -.
DR BioGRID; 202560; 25.
DR CORUM; Q61550; -.
DR DIP; DIP-56655N; -.
DR IntAct; Q61550; 19.
DR MINT; Q61550; -.
DR STRING; 10090.ENSMUSP00000022927; -.
DR iPTMnet; Q61550; -.
DR PhosphoSitePlus; Q61550; -.
DR EPD; Q61550; -.
DR jPOST; Q61550; -.
DR MaxQB; Q61550; -.
DR PaxDb; Q61550; -.
DR PeptideAtlas; Q61550; -.
DR PRIDE; Q61550; -.
DR ProteomicsDB; 300304; -.
DR Antibodypedia; 13592; 328 antibodies from 35 providers.
DR DNASU; 19357; -.
DR Ensembl; ENSMUST00000022927; ENSMUSP00000022927; ENSMUSG00000022314.
DR GeneID; 19357; -.
DR KEGG; mmu:19357; -.
DR UCSC; uc007vrd.2; mouse.
DR CTD; 5885; -.
DR MGI; MGI:108016; Rad21.
DR VEuPathDB; HostDB:ENSMUSG00000022314; -.
DR eggNOG; KOG1213; Eukaryota.
DR GeneTree; ENSGT00940000154655; -.
DR HOGENOM; CLU_015775_1_1_1; -.
DR InParanoid; Q61550; -.
DR OMA; LKQEEPY; -.
DR OrthoDB; 1253899at2759; -.
DR PhylomeDB; Q61550; -.
DR TreeFam; TF101215; -.
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; 19357; 29 hits in 114 CRISPR screens.
DR ChiTaRS; Rad21; mouse.
DR PRO; PR:Q61550; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61550; protein.
DR Bgee; ENSMUSG00000022314; Expressed in gonadal ridge and 263 other tissues.
DR ExpressionAtlas; Q61550; baseline and differential.
DR Genevisible; Q61550; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0008278; C:cohesin complex; IDA:CAFA.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; 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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:CAFA.
DR GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IMP:CAFA.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; ISO:MGI.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR Gene3D; 1.10.10.580; -; 1.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006909; Rad21/Rec8_C_eu.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR InterPro; IPR023093; ScpA-like_C.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04824; Rad21_Rec8; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Developmental protein; DNA damage;
KW DNA repair; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..635
FT /note="Double-strand-break repair protein rad21 homolog"
FT /id="PRO_0000097873"
FT CHAIN 280..635
FT /note="64-kDa C-terminal product"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT /id="PRO_0000446318"
FT REGION 1..126
FT /note="Required for interaction with SMCA1"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT REGION 126..282
FT /note="Required for interaction with SMARCA5"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT REGION 258..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..403
FT /note="Interaction with WAPL and PDS5B"
FT /evidence="ECO:0000250"
FT REGION 362..403
FT /note="Interaction with STAG1"
FT /evidence="ECO:0000250"
FT REGION 423..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 172..173
FT /note="Cleavage; by ESPL1"
FT /evidence="ECO:0000250"
FT SITE 279..280
FT /note="Cleavage; by caspase-3 or caspase-7"
FT /evidence="ECO:0000250"
FT SITE 454..455
FT /note="Cleavage; by ESPL1"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MOD_RES 627
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT CONFLICT 147
FT /note="E -> G (in Ref. 4; BAB23527)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="K -> E (in Ref. 4; BAB23527)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="F -> S (in Ref. 1; BAA08408 and 3; AAK56113/
FT AAK56114)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="Missing (in Ref. 1; BAA08408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 72083 MW; 2EC1AC08E358E9CE CRC64;
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL
LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP
LPDLDDIDVA QQFSLNQSRV EEITMREEVG NISILQENDF GDFGMDDREI MREGSAFEDD
DMLVSTSASN LLLEPEQSTS NLNEKMNHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG
IFDDPPALSE AGVMLPEQPA HDDMDEDDNG SLGGPDSPDS VDPVEPMPTM TDQTTLVPNE
EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT LDLAPPTKKL
MMWKETGGVE KLFFLPAQPL WNNRLLKLFT RCLTPLVPED LRKRRKGGEA DNLDEFLKEF
ENPEVPREEQ QPQQQQPQPQ RDVIDEPIIE EPSRLQDSVM EASRTTIEES AMPPPPPQGV
KRKAGQIDPE PSIPPQQVEQ MEIPPVELPP EEPPNICQLI PELELLPEKE KEKEKEKEEE
EEEEDEDASG GDQDQEERRW NKRTQQMLHG LQRALAKTGA ESISLLELCR NTNRKQAAAK
FYSFLVLKKQ QAIELTQEEP YSDIIATPGP RFHII
