SEPT6_MOUSE
ID SEPT6_MOUSE Reviewed; 434 AA.
AC Q9R1T4; A2A3V9; A2A3W0; Q3TRH9; Q3TUA2; Q542H3; Q6A0C4; Q8C2L2; Q8C848;
AC Q91XH2; Q9CZ94;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Septin-6;
GN Name=Septin6 {ECO:0000303|Ref.1};
GN Synonyms=Kiaa0128 {ECO:0000303|PubMed:15368895},
GN Sept6 {ECO:0000312|MGI:MGI:1888939};
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] (ISOFORM V).
RC STRAIN=NIH Swiss; TISSUE=Heart;
RA Kinoshita M.;
RT "Identification of mouse Septin6 gene and its product.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS II AND V).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Head, 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC TISSUE=Salivary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427.
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6]
RP PROTEIN SEQUENCE OF 16-111; 164-171; 177-185; 255-273; 281-287; 294-299;
RP 310-337; 388-397 AND 400-420, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11064363;
RX DOI=10.1002/1096-9861(20001211)428:2<223::aid-cne3>3.0.co;2-m;
RA Kinoshita A., Noda M., Kinoshita M.;
RT "Differential localization of septins in the mouse brain.";
RL J. Comp. Neurol. 428:223-239(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=20181826; DOI=10.1091/mbc.e09-10-0869;
RA Shinoda T., Ito H., Sudo K., Iwamoto I., Morishita R., Nagata K.;
RT "Septin 14 is involved in cortical neuronal migration via interaction with
RT Septin 4.";
RL Mol. Biol. Cell 21:1324-1334(2010).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal
CC organization of the actin cytoskeleton. Involved in cytokinesis. Forms
CC a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably
CC SEPTIN4 at the sperm annulus which is required for the structural
CC integrity and motility of the sperm tail during postmeiotic
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q14141}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation. Filaments are assembled from asymmetrical heterotrimers,
CC composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to
CC form a hexameric unit. Within the trimer, directly interacts with
CC SEPTIN2 and SEPTIN7. Also interacts with SEPTIN9 and SEPTIN12.
CC Interaction with SEPTIN12 alters filament structure. Component of a
CC septin core octomeric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6
CC and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-
CC 7-12 and located in the sperm annulus. Interacts with SOCS7. Interacts
CC with HNRNPA1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q14141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Cleavage furrow
CC {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium,
CC flagellum {ECO:0000250|UniProtKB:Q14141}. Note=In metaphase cells,
CC localized within the microtubule spindle. At the metaphase plate, in
CC close apposition to the kinetochores of the congressed chromosomes. In
CC cells undergoing cytokinesis, localized to the midbody, the ingressing
CC cleavage furrow, and the central spindle. Found in the sperm annulus
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q14141}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=II;
CC IsoId=Q9R1T4-1; Sequence=Displayed;
CC Name=I; Synonyms=III;
CC IsoId=Q9R1T4-2; Sequence=VSP_006055;
CC Name=V;
CC IsoId=Q9R1T4-3; Sequence=VSP_006056;
CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex (at protein level)
CC (PubMed:20181826). Associated with synaptic vesicles in various brain
CC regions, including glomeruli of the olfactory bulb (at protein level)
CC (PubMed:11064363). {ECO:0000269|PubMed:11064363,
CC ECO:0000269|PubMed:20181826}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPT2 and SEPT7.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM19782.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB023622; BAA82838.1; -; mRNA.
DR EMBL; AK012858; BAB28516.1; -; mRNA.
DR EMBL; AK048455; BAC33342.1; -; mRNA.
DR EMBL; AK088406; BAC40335.1; -; mRNA.
DR EMBL; AK088614; BAC40453.1; -; mRNA.
DR EMBL; AK160884; BAE36069.1; -; mRNA.
DR EMBL; AK162755; BAE37050.1; -; mRNA.
DR EMBL; AL450399; CAM19780.1; -; Genomic_DNA.
DR EMBL; AL450399; CAM19781.1; -; Genomic_DNA.
DR EMBL; AL450399; CAM19782.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC010489; AAH10489.1; -; mRNA.
DR EMBL; AK172894; BAD32172.1; ALT_INIT; mRNA.
DR CCDS; CCDS30066.1; -. [Q9R1T4-3]
DR CCDS; CCDS53051.1; -. [Q9R1T4-1]
DR CCDS; CCDS57749.1; -. [Q9R1T4-2]
DR RefSeq; NP_001170794.1; NM_001177323.2.
DR RefSeq; NP_001170795.1; NM_001177324.1. [Q9R1T4-1]
DR RefSeq; NP_001240635.1; NM_001253706.1. [Q9R1T4-2]
DR RefSeq; NP_064326.2; NM_019942.5. [Q9R1T4-3]
DR RefSeq; XP_006541452.1; XM_006541389.3.
DR RefSeq; XP_006541453.1; XM_006541390.2. [Q9R1T4-2]
DR AlphaFoldDB; Q9R1T4; -.
DR SMR; Q9R1T4; -.
DR BioGRID; 208037; 37.
DR IntAct; Q9R1T4; 27.
DR STRING; 10090.ENSMUSP00000110894; -.
DR iPTMnet; Q9R1T4; -.
DR PhosphoSitePlus; Q9R1T4; -.
DR SwissPalm; Q9R1T4; -.
DR EPD; Q9R1T4; -.
DR jPOST; Q9R1T4; -.
DR MaxQB; Q9R1T4; -.
DR PaxDb; Q9R1T4; -.
DR PeptideAtlas; Q9R1T4; -.
DR PRIDE; Q9R1T4; -.
DR ProteomicsDB; 261156; -. [Q9R1T4-1]
DR ProteomicsDB; 261157; -. [Q9R1T4-2]
DR ProteomicsDB; 261158; -. [Q9R1T4-3]
DR Antibodypedia; 465; 289 antibodies from 35 providers.
DR DNASU; 56526; -.
DR Ensembl; ENSMUST00000053456; ENSMUSP00000054034; ENSMUSG00000050379. [Q9R1T4-2]
DR Ensembl; ENSMUST00000060474; ENSMUSP00000062014; ENSMUSG00000050379. [Q9R1T4-3]
DR Ensembl; ENSMUST00000115239; ENSMUSP00000110894; ENSMUSG00000050379. [Q9R1T4-1]
DR GeneID; 56526; -.
DR KEGG; mmu:56526; -.
DR UCSC; uc009sxx.2; mouse. [Q9R1T4-3]
DR UCSC; uc009sxz.2; mouse. [Q9R1T4-1]
DR CTD; 23157; -.
DR MGI; MGI:1888939; Septin6.
DR VEuPathDB; HostDB:ENSMUSG00000050379; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000158026; -.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; Q9R1T4; -.
DR OMA; NNGIHIY; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9R1T4; -.
DR TreeFam; TF101080; -.
DR BioGRID-ORCS; 56526; 1 hit in 49 CRISPR screens.
DR ChiTaRS; Sept6; mouse.
DR PRO; PR:Q9R1T4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R1T4; protein.
DR Bgee; ENSMUSG00000050379; Expressed in barrel cortex and 239 other tissues.
DR ExpressionAtlas; Q9R1T4; baseline and differential.
DR Genevisible; Q9R1T4; MM.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0032173; C:septin collar; IDA:MGI.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IDA:MGI.
DR GO; GO:0097227; C:sperm annulus; ISO:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030644; SEPT6.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF55; PTHR18884:SF55; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell projection; Centromere; Chromosome; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Direct protein sequencing; Flagellum;
KW GTP-binding; Kinetochore; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT CHAIN 2..434
FT /note="Septin-6"
FT /id="PRO_0000173526"
FT DOMAIN 39..305
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 49..56
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 184..187
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 403..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..407
FT /evidence="ECO:0000255"
FT COMPBIAS 418..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 185..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14141"
FT VAR_SEQ 428..434
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006055"
FT VAR_SEQ 428..434
FT /note="NPWLCIE -> FF (in isoform V)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_006056"
FT CONFLICT 10
FT /note="V -> L (in Ref. 2; BAB28516)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="Missing (in Ref. 2; BAC33342)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="L -> P (in Ref. 2; BAC40335)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="H -> Y (in Ref. 1; BAA82838)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="M -> I (in Ref. 2; BAE36069)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..239
FT /note="VG -> C (in Ref. 2; BAB28516)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="V -> A (in Ref. 2; BAC40335)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="A -> R (in Ref. 1; BAA82838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 49620 MW; 33DCD4F44607168A CRC64;
MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD
TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYKPIVE
FIDAQFEAYL QEELKIRRVL HSYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII
PVIAKSDAIS KSELAKFKIK ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS
TEEVKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA
EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK AAAELLQSQG SQAGGSQTLK
RDKEKKNNPW LCIE
