ID SEPT9_MOUSE Reviewed; 583 AA. AC Q80UG5; A2A6U2; A2A6U4; A2A6U6; Q3URP2; Q80TM7; Q9QYX9; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 163. DE RecName: Full=Septin-9; DE AltName: Full=SL3-3 integration site 1 protein; GN Name=Septin9 {ECO:0000312|MGI:MGI:1858222}; GN Synonyms=Kiaa0991 {ECO:0000303|PubMed:12693553}, Sept9 GN {ECO:0000312|MGI:MGI:1858222}, Sint1 {ECO:0000303|PubMed:10666245}; 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 2), AND TISSUE SPECIFICITY. RX PubMed=10666245; DOI=10.1128/jvi.74.5.2161-2168.2000; RA Soerensen A.B., Lund A.H., Ethelberg S., Copeland N.G., Jenkins N.A., RA Pedersen F.S.; RT "Sint1, a common integration site in SL3-3-induced T-cell lymphomas, RT harbors a putative proto-oncogene with homology to the septin gene RT family."; RL J. Virol. 74:2161-2168(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=12039034; DOI=10.1016/s0378-1119(02)00406-7; RA Soerensen A.B., Warming S., Fuechtbauer E.-M., Pedersen F.S.; RT "Alternative splicing, expression, and gene structure of the septin-like RT putative proto-oncogene Sint1."; RL Gene 285:79-89(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Embryonic tail; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II. RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [4] RP SEQUENCE REVISION. RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Head; 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=129; TISSUE=Mammary 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 [8] RP PROTEIN SEQUENCE OF 548-559, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [9] RP SUBCELLULAR LOCATION. RX PubMed=17546647; DOI=10.1002/humu.20554; RA Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.; RT "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are RT associated with altered interactions with SEPT4/SEPT11 and resistance to RT Rho/Rhotekin-signaling."; RL Hum. Mutat. 28:1005-1013(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-49 AND THR-143, AND RP IDENTIFICATION 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 expression."; RL Cell 143:1174-1189(2010). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, 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: Filament-forming cytoskeletal GTPase (By similarity). May CC play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}. 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. Interacts with SEPTIN2, SEPTIN6, SEPTIN7, SEPTIN11 and CC SEPTIN14. Interacts with RTKN and ARHGEF18 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:17546647}. Note=In an epithelial cell line, CC concentrates at cell-cell contact areas. After TGF-beta1 treatment and CC induction of epithelial to mesenchymal transition, colocalizes with CC actin stress fibers. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q80UG5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80UG5-2; Sequence=VSP_012341; CC Name=3; CC IsoId=Q80UG5-3; Sequence=VSP_012342; CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined except muscle. CC Isoforms are differentially expressed in testes, kidney, liver, heart, CC spleen and brain. {ECO:0000269|PubMed:10666245, CC ECO:0000269|PubMed:12039034}. CC -!- DEVELOPMENTAL STAGE: At 8 dpc mainly expressed in the lateral plate CC mesoderm and the somites. Beginning at 9 dpc the lateral plate CC expression is clearly focused in the developing fore- and hindlimb CC buds. In the cephalic region, expressed in the first and second CC branchial arch, in the nasal process and around the otic pit. At 9.5 CC dpc strongest expression is observed in the mesenchyme of the branchial CC arches, the limbs, and the developing dorsal root ganglia. Weak to CC intermediate expression is found in the neural epithelium. Expression CC is seen in the newly formed somites in the tail bud of older embryos. CC During formation of the digits, expression seems to outline the CC surviving tissue bordering it towards the apoptotic webbing. Expression CC is seen in the developing outer ear and in several areas known to be CC regulated by intensive epithelial mesenchymal interactions, like the CC viscera follicles and the developing mammary glands. CC {ECO:0000269|PubMed:12039034}. CC -!- DISEASE: Note=Putative proto-oncogene involved in T-cell CC lymphomagenesis. May play a role in leukemogenesis. CC -!- MISCELLANEOUS: Targeted by proviral insertion in T-cell lymphomas CC induced by the murine retrovirus SL3-3 MuLV. 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=BAC65697.2; Type=Erroneous initiation; 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; AJ250723; CAB59833.1; -; mRNA. DR EMBL; AF450142; AAL50685.1; -; Genomic_DNA. DR EMBL; AF450141; AAL50685.1; JOINED; Genomic_DNA. DR EMBL; AK031757; BAC27538.1; -; mRNA. DR EMBL; AK122415; BAC65697.2; ALT_INIT; mRNA. DR EMBL; AK141312; BAE24646.1; -; mRNA. DR EMBL; AL603868; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL611935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645975; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC046524; AAH46524.1; -; mRNA. DR CCDS; CCDS25684.1; -. [Q80UG5-2] DR CCDS; CCDS48990.1; -. [Q80UG5-1] DR CCDS; CCDS48991.1; -. [Q80UG5-3] DR RefSeq; NP_001106958.1; NM_001113486.1. [Q80UG5-1] DR RefSeq; NP_001106959.1; NM_001113487.1. [Q80UG5-3] DR RefSeq; NP_001106960.1; NM_001113488.1. [Q80UG5-2] DR RefSeq; NP_059076.1; NM_017380.2. [Q80UG5-2] DR RefSeq; XP_006533808.2; XM_006533745.3. [Q80UG5-2] DR RefSeq; XP_006533809.1; XM_006533746.3. [Q80UG5-2] DR AlphaFoldDB; Q80UG5; -. DR SMR; Q80UG5; -. DR BioGRID; 207494; 57. DR IntAct; Q80UG5; 41. DR MINT; Q80UG5; -. DR STRING; 10090.ENSMUSP00000091435; -. DR GlyGen; Q80UG5; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q80UG5; -. DR PhosphoSitePlus; Q80UG5; -. DR SwissPalm; Q80UG5; -. DR EPD; Q80UG5; -. DR jPOST; Q80UG5; -. DR MaxQB; Q80UG5; -. DR PaxDb; 10090-ENSMUSP00000091435; -. DR PeptideAtlas; Q80UG5; -. DR ProteomicsDB; 257120; -. [Q80UG5-1] DR ProteomicsDB; 257121; -. [Q80UG5-2] DR ProteomicsDB; 257122; -. [Q80UG5-3] DR Pumba; Q80UG5; -. DR Antibodypedia; 32488; 281 antibodies from 31 providers. DR DNASU; 53860; -. DR Ensembl; ENSMUST00000019038.15; ENSMUSP00000019038.9; ENSMUSG00000059248.14. [Q80UG5-3] DR Ensembl; ENSMUST00000093907.11; ENSMUSP00000091435.5; ENSMUSG00000059248.14. [Q80UG5-1] DR Ensembl; ENSMUST00000100193.8; ENSMUSP00000097767.2; ENSMUSG00000059248.14. [Q80UG5-2] DR Ensembl; ENSMUST00000106349.2; ENSMUSP00000101956.2; ENSMUSG00000059248.14. [Q80UG5-2] DR GeneID; 53860; -. DR KEGG; mmu:53860; -. DR UCSC; uc007mnd.2; mouse. [Q80UG5-1] DR UCSC; uc007mne.2; mouse. [Q80UG5-3] DR AGR; MGI:1858222; -. DR CTD; 10801; -. DR MGI; MGI:1858222; Septin9. DR VEuPathDB; HostDB:ENSMUSG00000059248; -. DR eggNOG; KOG1547; Eukaryota. DR GeneTree; ENSGT00940000157195; -. DR HOGENOM; CLU_017718_7_1_1; -. DR InParanoid; Q80UG5; -. DR OrthoDB; 5396944at2759; -. DR PhylomeDB; Q80UG5; -. DR TreeFam; TF101078; -. DR BioGRID-ORCS; 53860; 2 hits in 49 CRISPR screens. DR ChiTaRS; Sept9; mouse. DR PRO; PR:Q80UG5; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q80UG5; Protein. DR Bgee; ENSMUSG00000059248; Expressed in ectoplacental cone and 236 other cell types or tissues. DR ExpressionAtlas; Q80UG5; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI. DR GO; GO:0005930; C:axoneme; ISO:MGI. DR GO; GO:0032153; C:cell division site; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; ISO:MGI. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0097730; C:non-motile cilium; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0031105; C:septin complex; IDA:UniProtKB. DR GO; GO:0005940; C:septin ring; IBA:GO_Central. DR GO; GO:0001725; C:stress fiber; ISO: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:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central. DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISO:MGI. DR CDD; cd01850; CDC_Septin; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR030379; G_SEPTIN_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016491; Septin. DR PANTHER; PTHR18884; SEPTIN; 1. DR PANTHER; PTHR18884:SF47; SEPTIN-9; 1. DR Pfam; PF00735; Septin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51719; G_SEPTIN; 1. DR Genevisible; Q80UG5; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; GTP-binding; Nucleotide-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1..583 FT /note="Septin-9" FT /id="PRO_0000173536" FT DOMAIN 293..565 FT /note="Septin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 79..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 166..252 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 303..310 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 360..363 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 442..445 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT COMPBIAS 204..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 303..310 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 337 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 363 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 443..451 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 499 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 514 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 42 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT MOD_RES 49 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 62 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT MOD_RES 143 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 276 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UHD8" FT VAR_SEQ 1..249 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10666245, FT ECO:0000303|PubMed:16141072" FT /id="VSP_012341" FT VAR_SEQ 1..25 FT /note="MKKSYSGVTRTSSGRLRRLADPTGP -> MSDPAVNAQLDGIISDFE (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:12693553" FT /id="VSP_012342" SQ SEQUENCE 583 AA; 65575 MW; 174D2F1E8EA382FC CRC64; MKKSYSGVTR TSSGRLRRLA DPTGPALKRS FEVEEIEPPN STPPRRVQTP LLRATVASSS QKFQDLGVKN SEPAARLVDS LSQRSPKPSL RRVELAGAKA PEPMSRRTEI SIDISSKQVE STASAAGPSR FGLKRAEVLG HKTPEPVPRR TEITIVKPQE SVLRRVETPA SKIPEGSAVP ATDAAPKRVE IQVPKPAEAP NCPLPSQTLE NSEAPMSQLQ SRLEPRPSVA EVPYRNQEDS EVTPSCVGDM ADNPRDAMLK QAPASRNEKA PMEFGYVGID SILEQMRRKA MKQGFEFNIM VVGQSGLGKS TLINTLFKSK ISRKSVQPTS EERIPKTIEI KSITHDIEEK GVRMKLTVID TPGFGDHINN ENCWQPIMKF INDQYEKYLQ EEVNINRKKR IPDTRVHCCL YFIPATGHSL RPLDIEFMKR LSKVVNIVPV IAKADTLTLE ERVYFKQRIT ADLLSNGIDV YPQKEFDEDA EDRLVNEKFR EMIPFAVVGS DHEYQVNGKR ILGRKTKWGT IEVENTTHCE FAYLRDLLIR THMQNIKDIT SNIHFEAYRV KRLNEGNSAM ANGIEKEPEA QEM //