STOM_MOUSE
ID STOM_MOUSE Reviewed; 284 AA.
AC P54116; O88988; Q3UP81; Q60744; Q62455;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Stomatin {ECO:0000312|MGI:MGI:95403};
DE AltName: Full=Erythrocyte band 7 integral membrane protein {ECO:0000303|PubMed:8921901};
DE AltName: Full=Erythrocyte membrane protein band 7.2 {ECO:0000250|UniProtKB:P27105};
DE AltName: Full=Protein 7.2b {ECO:0000303|PubMed:7540886};
GN Name=Stom {ECO:0000312|MGI:MGI:95403};
GN Synonyms=Epb7.2 {ECO:0000312|MGI:MGI:95403},
GN Epb72 {ECO:0000312|MGI:MGI:95403};
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], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=7540886;
RA Gallagher P.G., Romana M., Lieman J.H., Ward D.C.;
RT "cDNA structure, tissue-specific expression, and chromosomal localization
RT of the murine band 7.2b gene.";
RL Blood 86:359-365(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Bone marrow;
RX PubMed=8921901; DOI=10.1016/0378-1119(96)00347-2;
RA Schlegel W., Unfried I., Prohaska R.;
RT "Cloning and analysis of a cDNA encoding the BALB/c murine erythrocyte band
RT 7 integral membrane protein.";
RL Gene 178:115-118(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8786142; DOI=10.1006/geno.1996.0304;
RA Gallagher P.G., Turetsky T., Mentzer W.C.;
RT "Genomic organization and 5'-flanking DNA sequence of the murine stomatin
RT gene (Epb72).";
RL Genomics 34:410-412(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Neuron;
RX PubMed=10383825; DOI=10.1006/mcne.1999.0761;
RA Mannsfeldt A.G., Carroll P., Stucky C.L., Lewin G.R.;
RT "Stomatin, a MEC-2 like protein, is expressed by mammalian sensory
RT neurons.";
RL Mol. Cell. Neurosci. 13:391-404(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Cerebellum, Spleen, and Sympathetic ganglion;
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 FUNCTION, AND INTERACTION WITH ASIC1; ASIC2 AND ASIC3.
RX PubMed=15471860; DOI=10.1074/jbc.m407708200;
RA Price M.P., Thompson R.J., Eshcol J.O., Wemmie J.A., Benson C.J.;
RT "Stomatin modulates gating of acid-sensing ion channels.";
RL J. Biol. Chem. 279:53886-53891(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, 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 X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 86-213, FUNCTION, SUBUNIT,
RP INTERACTION WITH ASIC3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-97;
RP LEU-109; LEU-145; THR-182 AND VAL-197.
RX PubMed=22850675; DOI=10.1038/emboj.2012.203;
RA Brand J., Smith E.S., Schwefel D., Lapatsina L., Poole K., Omerbasic D.,
RA Kozlenkov A., Behlke J., Lewin G.R., Daumke O.;
RT "A stomatin dimer modulates the activity of acid-sensing ion channels.";
RL EMBO J. 31:3635-3646(2012).
CC -!- FUNCTION: Regulates ion channel activity and transmembrane ion
CC transport. Regulates ASIC2 and ASIC3 channel activity.
CC {ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:22850675}.
CC -!- SUBUNIT: Interacts with LANCL1. Interacts with SLC2A1 and SLC4A1.
CC Identified in large complexes with SLC40A1, SLC14A1, SLC29A1 and AQP1
CC (By similarity). Homodimer and higher order homooligomers. The
CC homodimer is banana-shaped. Interacts with ASIC1, ASIC2 and ASIC3.
CC Interacts with STOML1; may redistribute STOM from the plasma membrane
CC to late endosomes. {ECO:0000250, ECO:0000250|UniProtKB:P27105,
CC ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:22850675}.
CC -!- INTERACTION:
CC P54116; P54116: Stom; NbExp=5; IntAct=EBI-8004826, EBI-8004826;
CC P54116; O35240: Asic3; Xeno; NbExp=3; IntAct=EBI-8004826, EBI-982374;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P27105};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P27105}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P27105}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P27105}. Cell membrane
CC {ECO:0000250|UniProtKB:P27105}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P27105}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P27105}. Membrane raft
CC {ECO:0000250|UniProtKB:P27105}. Melanosome
CC {ECO:0000250|UniProtKB:P27105}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:10383825}. Note=Localizes to juxtanuclear structure
CC probably derived from the Golgi apparatus. Colocalizes with cortical
CC actin microfilaments at small plasma membrane protrusions. Associates
CC with alpha-granular lipid rafts. Translocates from the alpha-granular
CC lipid rafts to the cell membrane on thrombin activation and selectively
CC enriched in released microvesicles. Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC {ECO:0000250|UniProtKB:P27105}.
CC -!- TISSUE SPECIFICITY: Expressed in all sensory neurons of the dorsal root
CC ganglia. In the CNS, expressed in many neurons of the spinal cord,
CC medulla and pons. Expressed only in scattered neurons in the cortex,
CC hippocampus, thalamus and basal ganglia. In the cerebellum, expressed
CC in all Purkinje cells (at protein level). Widely expressed with high
CC levels in heart, liver, skeletal muscle and testis and low levels in
CC lung, brain and spleen. {ECO:0000269|PubMed:10383825,
CC ECO:0000269|PubMed:7540886}.
CC -!- DEVELOPMENTAL STAGE: First expressed in the developing embryo at 11.5
CC dpc when target innervation is complete. Expression continues into
CC adulthood. {ECO:0000269|PubMed:10383825}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18857.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U17297; AAA75024.1; -; mRNA.
DR EMBL; X91043; CAA62503.1; -; mRNA.
DR EMBL; U50999; AAB18857.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U50993; AAB18857.1; JOINED; Genomic_DNA.
DR EMBL; U50994; AAB18857.1; JOINED; Genomic_DNA.
DR EMBL; U50995; AAB18857.1; JOINED; Genomic_DNA.
DR EMBL; U50996; AAB18857.1; JOINED; Genomic_DNA.
DR EMBL; U50997; AAB18857.1; JOINED; Genomic_DNA.
DR EMBL; U50998; AAB18857.1; JOINED; Genomic_DNA.
DR EMBL; AF093620; AAC64173.1; -; mRNA.
DR EMBL; AK139242; BAE23930.1; -; mRNA.
DR EMBL; AK143724; BAE25516.1; -; mRNA.
DR EMBL; AK148975; BAE28708.1; -; mRNA.
DR EMBL; AK149689; BAE29028.1; -; mRNA.
DR EMBL; AK149821; BAE29103.1; -; mRNA.
DR EMBL; AK149991; BAE29219.1; -; mRNA.
DR EMBL; AK151129; BAE30137.1; -; mRNA.
DR CCDS; CCDS15961.1; -.
DR PIR; JC5221; JC5221.
DR RefSeq; NP_038543.1; NM_013515.2.
DR PDB; 4FVF; X-ray; 2.46 A; A/B=86-213.
DR PDB; 4FVG; X-ray; 1.80 A; A=86-213.
DR PDB; 4FVJ; X-ray; 2.69 A; A/B/C/D/E/F/G/H=86-213.
DR PDBsum; 4FVF; -.
DR PDBsum; 4FVG; -.
DR PDBsum; 4FVJ; -.
DR AlphaFoldDB; P54116; -.
DR SMR; P54116; -.
DR BioGRID; 199465; 7.
DR IntAct; P54116; 5.
DR MINT; P54116; -.
DR STRING; 10090.ENSMUSP00000028241; -.
DR iPTMnet; P54116; -.
DR PhosphoSitePlus; P54116; -.
DR SwissPalm; P54116; -.
DR jPOST; P54116; -.
DR MaxQB; P54116; -.
DR PaxDb; P54116; -.
DR PeptideAtlas; P54116; -.
DR PRIDE; P54116; -.
DR ProteomicsDB; 257458; -.
DR Antibodypedia; 2509; 271 antibodies from 34 providers.
DR DNASU; 13830; -.
DR Ensembl; ENSMUST00000028241; ENSMUSP00000028241; ENSMUSG00000026880.
DR GeneID; 13830; -.
DR KEGG; mmu:13830; -.
DR UCSC; uc008jkh.1; mouse.
DR CTD; 2040; -.
DR MGI; MGI:95403; Stom.
DR VEuPathDB; HostDB:ENSMUSG00000026880; -.
DR eggNOG; KOG2621; Eukaryota.
DR GeneTree; ENSGT01030000234614; -.
DR HOGENOM; CLU_024949_3_0_1; -.
DR InParanoid; P54116; -.
DR OMA; MVISPNE; -.
DR OrthoDB; 1062075at2759; -.
DR PhylomeDB; P54116; -.
DR TreeFam; TF105750; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 13830; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Stom; mouse.
DR PRO; PR:P54116; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P54116; protein.
DR Bgee; ENSMUSG00000026880; Expressed in olfactory epithelium and 255 other tissues.
DR Genevisible; P54116; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:AgBase.
DR GO; GO:0048524; P:positive regulation of viral process; IMP:AgBase.
DR GO; GO:1901585; P:regulation of acid-sensing ion channel activity; IDA:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IDA:UniProtKB.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR043202; Band-7_stomatin-like.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
DR InterPro; IPR028515; Stomatin.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR PANTHER; PTHR10264:SF115; PTHR10264:SF115; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR PROSITE; PS01270; BAND_7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Stomatin"
FT /id="PRO_0000094028"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 32..52
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 265..273
FT /note="Required for homooligomerization"
FT /evidence="ECO:0000250"
FT REGION 267..269
FT /note="Required for lipid raft association"
FT /evidence="ECO:0000250"
FT REGION 273..284
FT /note="Interaction with LANCL1"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27105"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT LIPID 30
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 87
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 97
FT /note="R->D: Does not abolish interaction with ASIC3, but
FT abolishes regulation of ASIC3 channel activity; when
FT associated with D-109 and D-145."
FT /evidence="ECO:0000269|PubMed:22850675"
FT MUTAGEN 109
FT /note="L->D: Does not abolish interaction with ASIC3, but
FT abolishes regulation of ASIC3 channel activity; when
FT associated with D-97 and D-145."
FT /evidence="ECO:0000269|PubMed:22850675"
FT MUTAGEN 145
FT /note="L->D: Does not abolish interaction with ASIC3, but
FT abolishes regulation of ASIC3 channel activity; when
FT associated with D-97 and D-109."
FT /evidence="ECO:0000269|PubMed:22850675"
FT MUTAGEN 182
FT /note="T->W: Does not abolish interaction with ASIC3, but
FT abolishes regulation of ASIC2 and ASIC3 channel activity."
FT /evidence="ECO:0000269|PubMed:22850675"
FT MUTAGEN 197
FT /note="V->P: Abolishes homodimerization and
FT oligomerization. Abolishes regulation of ASIC2 and ASIC3
FT channel activity."
FT /evidence="ECO:0000269|PubMed:22850675"
FT CONFLICT 3
FT /note="D -> V (in Ref. 4; AAC64173)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="A -> V (in Ref. 2; CAA62503)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="F -> I (in Ref. 2; CAA62503)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="I -> L (in Ref. 2; CAA62503)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="L -> F (in Ref. 2; CAA62503)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="V -> I (in Ref. 2; CAA62503)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="N -> H (in Ref. 2; CAA62503)"
FT /evidence="ECO:0000305"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:4FVG"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:4FVG"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:4FVG"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4FVG"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:4FVG"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:4FVG"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:4FVG"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4FVG"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:4FVG"
SQ SEQUENCE 284 AA; 31375 MW; AB7CC0E5FF2DF4A9 CRC64;
MSDKRQSSHV QSQRIPESFR ENSKTELGAC GWILVAASFF FVIITFPISI WICIKIVKEY
ERVIIFRLGR ILQGGAKGPG LFFILPCTDS LIKVDMRTIS FDIPPQEVLT KDSVTISVDG
VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNALGTKNL SQILSDREEI AHHMQSTLDD
ATDDWGIKVE RVEIKDVKLP VQLQRAMAAE AEAAREARAK VIAAEGEMNA SRALKEASMV
ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPVDMLQGIM GSNH
