ID MTUS1_MOUSE Reviewed; 1210 AA. AC Q5HZI1; Q3UP60; Q6ITD2; Q6ZPU5; Q80YG5; Q80YV9; Q80ZZ2; Q8BH23; Q8BMM8; AC Q8C0C8; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 24-JAN-2024, entry version 105. DE RecName: Full=Microtubule-associated tumor suppressor 1 homolog; DE AltName: Full=AT2 receptor-binding protein; DE AltName: Full=Angiotensin-II type 2 receptor-interacting protein; DE AltName: Full=Coiled-coiled tumor suppressor gene 1 protein; DE AltName: Full=Mitochondrial tumor suppressor 1 homolog; GN Name=Mtus1; Synonyms=Atbp, Atip, Cctsg1, Kiaa1288, Mtsg1; 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), INTERACTION WITH AGTR2, AND RP FUNCTION. RX PubMed=15123706; DOI=10.1074/jbc.m403880200; RA Nouet S., Amzallag N., Li J.-M., Louis S., Seitz I., Cui T.-X., RA Alleaume A.-M., Di Benedetto M., Boden C., Masson M., Strosberg A.D., RA Horiuchi M., Couraud P.-O., Nahmias C.; RT "Trans-inactivation of receptor tyrosine kinases by novel angiotensin II RT AT2 receptor-interacting protein, ATIP."; RL J. Biol. Chem. 279:28989-28997(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), SUBUNIT, INTERACTION WITH RP AGTR2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION. RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo; RX PubMed=15539617; DOI=10.1161/01.atv.0000150662.51436.14; RA Wruck C.J., Funke-Kaiser H., Pufe T., Kusserow H., Menk M., Schefe J.H., RA Kruse M.L., Stoll M., Unger T.; RT "Regulation of transport of the angiotensin AT2 receptor by a novel RT membrane-associated Golgi protein."; RL Arterioscler. Thromb. Vasc. Biol. 25:57-64(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=C57BL/6N; RA Seibold S., Wanner C., Galle J.; RT "Cloning and characterization of MTSG1."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III. 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. 10:167-180(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-759 (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Pituitary, Spleen, and Testis; 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 MRNA] (ISOFORMS 1 AND 4). RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Eye, and Kidney; 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 [7] RP SUBCELLULAR LOCATION, INTERACTION WITH PTPN6, AND FUNCTION. RX PubMed=17068200; DOI=10.1210/me.2006-0005; RA Li J.-M., Mogi M., Tsukuda K., Tomochika H., Iwanami J., Min L.-J., RA Nahmias C., Iwai M., Horiuchi M.; RT "Angiotensin II-induced neural differentiation via angiotensin II type 2 RT (AT2) receptor-MMS2 cascade involving interaction between AT2 receptor- RT interacting protein and Src homology 2 domain-containing protein-tyrosine RT phosphatase 1."; RL Mol. Endocrinol. 21:499-511(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-380; SER-1195; RP SER-1203 AND SER-1208, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-380; SER-1164; RP SER-1185; SER-1201 AND SER-1208, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Pancreas; 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: Cooperates with AGTR2 to inhibit ERK2 activation and cell CC proliferation. May be required for AGTR2 cell surface expression. CC Together with PTPN6, induces UBE2V2 expression upon angiotensin-II CC stimulation. {ECO:0000269|PubMed:15123706, ECO:0000269|PubMed:15539617, CC ECO:0000269|PubMed:17068200}. CC -!- SUBUNIT: Homodimer. Interacts with AGTR2. Interacts with PTPN6. CC {ECO:0000269|PubMed:15123706, ECO:0000269|PubMed:15539617, CC ECO:0000269|PubMed:17068200}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Golgi apparatus. CC Cell membrane. Nucleus. Note=In neurons, translocates into the nucleus CC after treatment with angiotensin-II. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=ATBP135; CC IsoId=Q5HZI1-1; Sequence=Displayed; CC Name=2; Synonyms=ATBP50; CC IsoId=Q5HZI1-2; Sequence=VSP_028279, VSP_028282; CC Name=3; CC IsoId=Q5HZI1-3; Sequence=VSP_028279, VSP_028282, VSP_028283; CC Name=4; Synonyms=ATBP60; CC IsoId=Q5HZI1-4; Sequence=VSP_028280, VSP_028281; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in CC uterus and adrenal gland. {ECO:0000269|PubMed:15539617}. CC -!- SIMILARITY: Belongs to the MTUS1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH41777.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH42206.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC98134.1; 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; AF173380; AAD49746.1; -; mRNA. DR EMBL; AY626781; AAT45892.1; -; mRNA. DR EMBL; AY626782; AAT45893.1; -; mRNA. DR EMBL; AY626783; AAT45894.1; -; mRNA. DR EMBL; AY246699; AAO88908.1; -; mRNA. DR EMBL; AF493235; AAQ06609.1; -; mRNA. DR EMBL; AK129324; BAC98134.1; ALT_INIT; mRNA. DR EMBL; AK030510; BAC26996.1; -; mRNA. DR EMBL; AK031693; BAC27517.1; -; mRNA. DR EMBL; AK143781; BAE25537.1; -; mRNA. DR EMBL; BC041777; AAH41777.1; ALT_INIT; mRNA. DR EMBL; BC042206; AAH42206.1; ALT_INIT; mRNA. DR EMBL; BC043321; AAH43321.1; -; mRNA. DR EMBL; BC089009; AAH89009.1; -; mRNA. DR CCDS; CCDS40328.1; -. [Q5HZI1-1] DR CCDS; CCDS40329.1; -. [Q5HZI1-4] DR CCDS; CCDS40330.1; -. [Q5HZI1-2] DR RefSeq; NP_001005863.1; NM_001005863.2. DR RefSeq; NP_001005864.1; NM_001005864.3. DR RefSeq; NP_001005865.2; NM_001005865.3. DR RefSeq; NP_001273342.1; NM_001286413.1. DR AlphaFoldDB; Q5HZI1; -. DR SMR; Q5HZI1; -. DR STRING; 10090.ENSMUSP00000059503; -. DR GlyGen; Q5HZI1; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q5HZI1; -. DR PhosphoSitePlus; Q5HZI1; -. DR jPOST; Q5HZI1; -. DR MaxQB; Q5HZI1; -. DR PaxDb; 10090-ENSMUSP00000091252; -. DR PeptideAtlas; Q5HZI1; -. DR ProteomicsDB; 290116; -. [Q5HZI1-1] DR ProteomicsDB; 290117; -. [Q5HZI1-2] DR ProteomicsDB; 290118; -. [Q5HZI1-3] DR ProteomicsDB; 290119; -. [Q5HZI1-4] DR Pumba; Q5HZI1; -. DR DNASU; 102103; -. DR GeneID; 102103; -. DR KEGG; mmu:102103; -. DR UCSC; uc009lnk.2; mouse. [Q5HZI1-2] DR UCSC; uc009lnl.2; mouse. [Q5HZI1-4] DR UCSC; uc009lnm.1; mouse. [Q5HZI1-1] DR AGR; MGI:2142572; -. DR CTD; 57509; -. DR MGI; MGI:2142572; Mtus1. DR eggNOG; ENOG502QPVG; Eukaryota. DR InParanoid; Q5HZI1; -. DR OrthoDB; 4226649at2759; -. DR PhylomeDB; Q5HZI1; -. DR TreeFam; TF333416; -. DR BioGRID-ORCS; 102103; 2 hits in 74 CRISPR screens. DR ChiTaRS; Mtus1; mouse. DR PRO; PR:Q5HZI1; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q5HZI1; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0010758; P:regulation of macrophage chemotaxis; IDA:MGI. DR PANTHER; PTHR24200:SF7; MICROTUBULE-ASSOCIATED TUMOR SUPPRESSOR 1; 1. DR PANTHER; PTHR24200; TOUCAN, ISOFORM A; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell membrane; Coiled coil; KW Golgi apparatus; Membrane; Mitochondrion; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..1210 FT /note="Microtubule-associated tumor suppressor 1 homolog" FT /id="PRO_0000305198" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 370..404 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 446..482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 513..545 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 585..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 683..771 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1177..1210 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 876..1171 FT /evidence="ECO:0000255" FT COMPBIAS 1..17 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 513..540 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 585..617 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 683..704 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1181..1210 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ULD2" FT MOD_RES 621 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ULD2" FT MOD_RES 1143 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6IMY1" FT MOD_RES 1164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1185 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1195 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 1199 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6IMY1" FT MOD_RES 1201 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 1204 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ULD2" FT MOD_RES 1208 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT VAR_SEQ 1..767 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14621295, FT ECO:0000303|PubMed:15123706, ECO:0000303|PubMed:15539617, FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3" FT /id="VSP_028279" FT VAR_SEQ 1..690 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15539617" FT /id="VSP_028280" FT VAR_SEQ 691..754 FT /note="APKTSTTPGRSSSKPDSRSLRKTPGLKAKVGPTAACLRRKSESRTLGSDRAL FT SPQRIRRVSGSG -> MTIPGGFRSCTETDISSTIFINSTLTPPAGSERQYDATLLALL FT VVGSYSLCIIPLLATLTRKKS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15539617" FT /id="VSP_028281" FT VAR_SEQ 768..810 FT /note="KQAFQNGSGPLYLKPLVPRAHSHLLKTSPKGPSRKSLFTAFNS -> MLLSP FT KFSLSTIHVRLTAKGLLRNLRLPSGLRKNTVIFHT (in isoform 2 and FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14621295, FT ECO:0000303|PubMed:15123706, ECO:0000303|PubMed:15539617, FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3" FT /id="VSP_028282" FT VAR_SEQ 977..1011 FT /note="FDNLNAAHETTKLEIEASHSEKVELLKKTYETSLS -> LP (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14621295" FT /id="VSP_028283" FT CONFLICT 401 FT /note="P -> S (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 426 FT /note="E -> K (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 455 FT /note="R -> S (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 519 FT /note="I -> V (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 525 FT /note="S -> N (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="H -> Q (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 553 FT /note="F -> L (in Ref. 6; AAH89009)" FT /evidence="ECO:0000305" FT CONFLICT 556 FT /note="S -> G (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 600 FT /note="T -> A (in Ref. 6; AAH41777/AAH42206)" FT /evidence="ECO:0000305" FT CONFLICT 646 FT /note="T -> A (in Ref. 5; BAE25537)" FT /evidence="ECO:0000305" FT CONFLICT 867 FT /note="T -> N (in Ref. 1; AAD49746 and 2; AAT45892)" FT /evidence="ECO:0000305" FT CONFLICT 919 FT /note="A -> T (in Ref. 2; AAT45893/AAT45894, 5; FT BAC26996/BAC27517 and 6; AAH43321/AAH89009)" FT /evidence="ECO:0000305" FT CONFLICT Q5HZI1-2:22 FT /note="Missing (in Ref. 5; BAC27517)" FT /evidence="ECO:0000305" FT CONFLICT Q5HZI1-2:29 FT /note="S -> P (in Ref. 5; BAC27517)" FT /evidence="ECO:0000305" SQ SEQUENCE 1210 AA; 134379 MW; 42642BCAE0759B25 CRC64; MNDDNSDRTE DGSRYVFIRD KNSNPSEYYQ TSLSAQCPSV SHGDWNSDNP DAMVVDYEMD PAVDSSESVS LSHQCVEELA YPEPSSDFMG KHEFTMYSEL TCQSPALVNT GKPQDLHSNC DSLEAIQDEK FDPLKPCECR SDDDYACGDS PEVLELKQTY GMKVDTANYT FIARHDIEQG QPLHAPGGLQ TTVRDRNALS SCGRTPPHSS KMYVRGVNYN RENFENLQAT PSKTLNTTFT VISDVLMQTD SPDVGVQGQN SLGNVTKEYT DGTRRGLIGE KEIQAVTLVS DGMEVPNGSA SQEFYCVSED DPNSETHSHG PYAQQEMGQN LRGTLPNCHV DGECPVLVPA FEKSKTRVLG SECKVTVTED PHIDSHDNDS DIQSSTEELT LRSVSGQRGS PYEMGWGENG GAICTDKAGC MSTPVEQPPN LSFRLEPAEV KKYNNVENGP RDAKRAPNLK GEPTNMPKPN LGKSATKTNT TVGSKVRKTE IISYPTPNFK NIKAKVISRS VLQPKDTSIM KDTPSPQVTG GSSPSPGPSK HLTMMNKAPR SDFKASKKAE IPINKTHKQQ FNKLITSQAA QVTTHSKNAS LGVPRTTSAT KSNQENVDKT GSPHAGSETG SVAAFFQKIK GILPVKMKSS ECLEVTYVSH IDQISPEKGE QDGEAPMEKQ ELGKQATNEI FESKSLLVGS APKTSTTPGR SSSKPDSRSL RKTPGLKAKV GPTAACLRRK SESRTLGSDR ALSPQRIRRV SGSGGHAAIN KYEEKPPKQA FQNGSGPLYL KPLVPRAHSH LLKTSPKGPS RKSLFTAFNS VEKGRQKNPR SLCIQTQTAP DVLSSERTLE LAQYKTKCES QSGFILHLRQ LLSRGNTKFE ALTVVIQHLL SEREEALKQH KTLSQELVSL RGELVAASSA CEKLEKARAD LQTAYQEFVQ KLNQQHQTDR TELENRLKDL YTAECEKLQS IYIEEAEKYK TQLQEQFDNL NAAHETTKLE IEASHSEKVE LLKKTYETSL SEIKKSHEME KKSLEDLLNE KQESLEKQIN DLKSENDALN ERLKSEEQKQ LSREKANSKN PQVMYLEQEL ESLKAVLEIK NEKLHQQDMK LMKMEKLVDN NTALVDKLKR FQQENEELKA RMDKHMAISR QLSTEQAALQ ESLEKESKVN KRLSMENEEL LWKLHNGDLC SPKRSPTSSA IPFQSPRNSG SFSSPSISPR //