SMCR8_MOUSE
ID SMCR8_MOUSE Reviewed; 935 AA.
AC Q3UMB5; Q5U4H2; Q8BNG6; Q8C704;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Guanine nucleotide exchange protein SMCR8 {ECO:0000305};
DE AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 8 protein homolog;
GN Name=Smcr8;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Mammary gland;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=11997338; DOI=10.1101/gr.73702;
RA Bi W., Yan J., Stankiewicz P., Park S.-S., Walz K., Boerkoel C.F.,
RA Potocki L., Shaffer L.G., Devriendt K., Nowaczyk M.J.M., Inoue K.,
RA Lupski J.R.;
RT "Genes in a refined Smith-Magenis syndrome critical deletion interval on
RT chromosome 17p11.2 and the syntenic region of the mouse.";
RL Genome Res. 12:713-728(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-488; SER-491;
RP SER-497 AND SER-788, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [7]
RP INTERACTION WITH C9ORF72.
RX PubMed=27875531; DOI=10.1371/journal.pgen.1006443;
RA Ugolino J., Ji Y.J., Conchina K., Chu J., Nirujogi R.S., Pandey A.,
RA Brady N.R., Hamacher-Brady A., Wang J.;
RT "Loss of C9orf72 enhances autophagic activity via deregulated mTOR and TFEB
RT signaling.";
RL PLoS Genet. 12:E1006443-E1006443(2016).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27617292; DOI=10.1126/sciadv.1601167;
RA Yang M., Liang C., Swaminathan K., Herrlinger S., Lai F., Shiekhattar R.,
RA Chen J.F.;
RT "A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in
RT autophagy.";
RL Sci. Adv. 2:E1601167-E1601167(2016).
RN [9]
RP INTERACTION WITH DLG4, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31651360; DOI=10.1186/s40478-019-0812-5;
RA Xiao S., McKeever P.M., Lau A., Robertson J.;
RT "Synaptic localization of C9orf72 regulates post-synaptic glutamate
RT receptor 1 levels.";
RL Acta Neuropathol. Commun. 7:161-161(2019).
CC -!- FUNCTION: Component of the C9orf72-SMCR8 complex, a complex that has
CC guanine nucleotide exchange factor (GEF) activity and regulates
CC autophagy (PubMed:27617292). In the complex, C9orf72 and SMCR8 probably
CC constitute the catalytic subunits that promote the exchange of GDP to
CC GTP, converting inactive GDP-bound RAB8A and RAB39B into their active
CC GTP-bound form, thereby promoting autophagosome maturation (By
CC similarity). The C9orf72-SMCR8 complex also acts as a negative
CC regulator of autophagy initiation by interacting with the ULK1/ATG1
CC kinase complex and inhibiting its protein kinase activity
CC (PubMed:27617292). As part of the C9orf72-SMCR8 complex, stimulates
CC RAB8A and RAB11A GTPase activity in vitro (By similarity). Acts as a
CC regulator of mTORC1 signaling by promoting phosphorylation of mTORC1
CC substrates (By similarity). In addition to its activity in the
CC cytoplasm within the C9orf72-SMCR8 complex, SMCR8 also localizes in the
CC nucleus, where it associates with chromatin and negatively regulates
CC expression of suppresses ULK1 and WIPI2 genes (By similarity).
CC {ECO:0000250|UniProtKB:Q8TEV9, ECO:0000269|PubMed:27617292}.
CC -!- SUBUNIT: Component of the C9orf72-SMCR8 complex, at least composed of
CC C9orf72, SMCR8 and WDR41 (Probable). The complex is formed of two
CC protomers, each individually consisting of one molecule each of
CC C9orf72, SMCR8 and WDR41 (By similarity). The protomers homodimerize
CC via an interaction between C9orf72 (via C-terminus) and SMCR8 (via N-
CC terminus) (By similarity). Within each protomer SMCR8 (via DENN domain)
CC acts as a bridging protein between WDR41 (via C-terminus and N-
CC terminus) and C9orf72 (via C-terminus) (By similarity). The C9orf72-
CC SMCR8 complex associates with the ULK1/ATG1 kinase complex (By
CC similarity). Interacts with C9orf72; the interaction is direct
CC (PubMed:27875531). Interacts with DLG4/PSD-95 (PubMed:31651360).
CC {ECO:0000250|UniProtKB:Q8TEV9, ECO:0000269|PubMed:27875531,
CC ECO:0000269|PubMed:31651360}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27617292}. Nucleus
CC {ECO:0000250|UniProtKB:Q8TEV9}. Presynapse
CC {ECO:0000269|PubMed:31651360}. Postsynapse
CC {ECO:0000269|PubMed:31651360}. Note=Localizes mainly in the cytoplasm.
CC {ECO:0000250|UniProtKB:Q8TEV9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UMB5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UMB5-2; Sequence=VSP_025488;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11997338). Expressed in
CC the forebrain and hippocampus (at protein level) (PubMed:31651360).
CC {ECO:0000269|PubMed:11997338, ECO:0000269|PubMed:31651360}.
CC -!- PTM: Phosphorylation by TBK1 is required to promote autophagosome
CC maturation. Phosphorylated by ULK1. {ECO:0000250|UniProtKB:Q8TEV9}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking display impaired autophagy
CC induction. {ECO:0000269|PubMed:27617292}.
CC -!- SIMILARITY: Belongs to the SMCR8 family. {ECO:0000305}.
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DR EMBL; AK052754; BAC35133.1; -; mRNA.
DR EMBL; AK083739; BAC39010.1; -; mRNA.
DR EMBL; AK145010; BAE26183.1; -; mRNA.
DR EMBL; AL596215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC085095; AAH85095.1; -; mRNA.
DR CCDS; CCDS24798.1; -. [Q3UMB5-2]
DR CCDS; CCDS48814.1; -. [Q3UMB5-1]
DR RefSeq; NP_001078909.1; NM_001085440.1. [Q3UMB5-1]
DR RefSeq; NP_780700.1; NM_175491.4. [Q3UMB5-2]
DR AlphaFoldDB; Q3UMB5; -.
DR SMR; Q3UMB5; -.
DR BioGRID; 231908; 5.
DR ComplexPortal; CPX-3962; C9orf72-SMCR8 complex.
DR IntAct; Q3UMB5; 5.
DR MINT; Q3UMB5; -.
DR STRING; 10090.ENSMUSP00000099728; -.
DR iPTMnet; Q3UMB5; -.
DR PhosphoSitePlus; Q3UMB5; -.
DR EPD; Q3UMB5; -.
DR jPOST; Q3UMB5; -.
DR MaxQB; Q3UMB5; -.
DR PaxDb; Q3UMB5; -.
DR PeptideAtlas; Q3UMB5; -.
DR PRIDE; Q3UMB5; -.
DR ProteomicsDB; 257267; -. [Q3UMB5-1]
DR ProteomicsDB; 257268; -. [Q3UMB5-2]
DR Antibodypedia; 13526; 40 antibodies from 14 providers.
DR DNASU; 237782; -.
DR Ensembl; ENSMUST00000056907; ENSMUSP00000055926; ENSMUSG00000049323. [Q3UMB5-1]
DR Ensembl; ENSMUST00000102667; ENSMUSP00000099728; ENSMUSG00000049323. [Q3UMB5-2]
DR GeneID; 237782; -.
DR KEGG; mmu:237782; -.
DR UCSC; uc007jgn.1; mouse. [Q3UMB5-1]
DR CTD; 140775; -.
DR MGI; MGI:2444720; Smcr8.
DR VEuPathDB; HostDB:ENSMUSG00000049323; -.
DR eggNOG; ENOG502QSW2; Eukaryota.
DR GeneTree; ENSGT00390000010052; -.
DR HOGENOM; CLU_013891_0_0_1; -.
DR InParanoid; Q3UMB5; -.
DR OMA; KPVKHWV; -.
DR OrthoDB; 692565at2759; -.
DR PhylomeDB; Q3UMB5; -.
DR TreeFam; TF330880; -.
DR BioGRID-ORCS; 237782; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Smcr8; mouse.
DR PRO; PR:Q3UMB5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UMB5; protein.
DR Bgee; ENSMUSG00000049323; Expressed in embryonic post-anal tail and 221 other tissues.
DR Genevisible; Q3UMB5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; ISO:MGI.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0045920; P:negative regulation of exocytosis; IC:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0050777; P:negative regulation of immune response; IC:ComplexPortal.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR GO; GO:1903432; P:regulation of TORC1 signaling; ISS:UniProtKB.
DR InterPro; IPR037521; FLCN/SMCR8_DENN.
DR InterPro; IPR037520; Folliculin/SMCR8_longin.
DR Pfam; PF11704; Folliculin; 1.
DR PROSITE; PS51834; DENN_FLCN_SMCR8; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell projection; Cytoplasm;
KW Guanine-nucleotide releasing factor; Nucleus; Phosphoprotein;
KW Reference proteome; Synapse; Transcription; Transcription regulation.
FT CHAIN 1..935
FT /note="Guanine nucleotide exchange protein SMCR8"
FT /id="PRO_0000287470"
FT DOMAIN 48..220
FT /note="uDENN FLCN/SMCR8-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01178"
FT DOMAIN 318..833
FT /note="cDENN FLCN/SMCR8-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01178"
FT DOMAIN 842..908
FT /note="dDENN FLCN/SMCR8-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01178"
FT REGION 1..349
FT /note="Required for the homodimerization of the C9orf72-
FT SMCR8 complex"
FT /evidence="ECO:0000250|UniProtKB:Q8TEV9"
FT REGION 257..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..912
FT /note="Interacts with WDR41 within the C9orf72-SMCR8
FT complex"
FT /evidence="ECO:0000250|UniProtKB:Q8TEV9"
FT COMPBIAS 268..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEV9"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEV9"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 794
FT /note="Phosphothreonine; by TBK1"
FT /evidence="ECO:0000250|UniProtKB:Q8TEV9"
FT VAR_SEQ 786..935
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025488"
FT CONFLICT 7
FT /note="V -> A (in Ref. 3; AAH85095)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="A -> T (in Ref. 1; BAE26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="V -> A (in Ref. 1; BAE26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="V -> I (in Ref. 1; BAE26183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 935 AA; 104957 MW; 6950CE4A0C50D8EE CRC64;
MISAPDVVAF TKEDEYEEEP YNEPALPEEY SVPLFPYASQ GANPWSKLSG AKFSRDFILI
SEFSEQVGPQ PLLTIPNDTK VFGTFDLNYF SLRIMSVDYQ ASFVGHPPGS AYPKLNFVED
SKVVLGDSKE GAFAYVHHLT LYDLEARGFV RPFCMAYISA DQHKIMQQFQ ELSAEFSKAS
ECLKMGNRKA FAGELEKKLK DLDYTRTVLH TETEIQKKAN DKGFYSSQAI EKANELANVE
KSIIEHQDLL RQIRSYPRQK TKIPDLQPGD TEHTQDQADQ VSTTSNPEES ANADLYTCRP
AYTPKLIKAK STKCFDKKLK TLEELCDTEY FTQTLAQLSH IEHMFRGDLC YLLTSQIDRV
LRKQQPITNF LFEDFVEVDD RMEKQENVPS QPSQDRLPPK PVEECPIPKV LISVGSYKSS
VESVLIKMEQ ELGDEEYTGV EATEARSFDP QENLDYLDMD MKGSISSGES IEVLGTEKSA
SVLSKSDSQA SLTVPLSPHV VRSKAVSHRT ISEDSIEVLS TCPSEALIPD DFKASYPSAI
NEEEAYADNE GAIHFQASAG SPEPDETQEG NLENIPSQID SSCCIGKESE GHLVPLPTPA
YTLSDEDSVV SIPPQRYIQK DQGLHVDFGV ENTDPSPRDN SCEMFPAYEL DPSCLLASRD
VSKMSLDNYS DTTSYMGSAA STSSDRIPSA PPAGLSSERH KKRAGQNALK FIRQYPFAHP
AIYSLLSGRT LVVLGEDETI VRKLVTALSI FVPNYGCYAK PVKHWISSPL HIMDFQKWKL
IGLQRVASPA NVGTLHTLSR YSRYTSILDL DSKTLRCPLY RGTLVPRLAD HRTQIKRGST
YYLHVQSMLT QLCSKAFLYT FCHHLHLPAH SEETQEAVAS RQTSFLKLNL GLVNEDIRVV
QYLAELLKLH YMQESPGTTH PLLRFDYVPS FLYKI
