MTUS1_MOUSE
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 25-MAY-2022, entry version 99.
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};
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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.ENSMUSP00000091252; -.
DR iPTMnet; Q5HZI1; -.
DR PhosphoSitePlus; Q5HZI1; -.
DR jPOST; Q5HZI1; -.
DR MaxQB; Q5HZI1; -.
DR PaxDb; Q5HZI1; -.
DR PeptideAtlas; Q5HZI1; -.
DR PRIDE; Q5HZI1; -.
DR ProteomicsDB; 290116; -. [Q5HZI1-1]
DR ProteomicsDB; 290117; -. [Q5HZI1-2]
DR ProteomicsDB; 290118; -. [Q5HZI1-3]
DR ProteomicsDB; 290119; -. [Q5HZI1-4]
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 CTD; 57509; -.
DR MGI; MGI:2142572; Mtus1.
DR eggNOG; ENOG502QPVG; Eukaryota.
DR InParanoid; Q5HZI1; -.
DR OrthoDB; 91479at2759; -.
DR PhylomeDB; Q5HZI1; -.
DR TreeFam; TF333416; -.
DR BioGRID-ORCS; 102103; 2 hits in 69 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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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 InterPro; IPR029786; MTUS1.
DR PANTHER; PTHR24200:SF7; PTHR24200:SF7; 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; BAC26996/
FT 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
