K22E_MOUSE
ID K22E_MOUSE Reviewed; 707 AA.
AC Q3TTY5; Q0VBW1; Q61869;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Keratin, type II cytoskeletal 2 epidermal;
DE AltName: Full=Cytokeratin-2e;
DE Short=CK-2e;
DE AltName: Full=Epithelial keratin-2e;
DE AltName: Full=Keratin-2 epidermis;
DE AltName: Full=Keratin-2e;
DE Short=K2e;
DE AltName: Full=Type-II keratin Kb2;
GN Name=Krt2 {ECO:0000312|EMBL:AAI20486.1};
GN Synonyms=K2e, Krt2-17 {ECO:0000312|MGI:MGI:96699},
GN Krt2a {ECO:0000250|UniProtKB:P35908};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=NMRI {ECO:0000269|PubMed:2448177};
RC TISSUE=Foot sole tissue {ECO:0000269|PubMed:2448177};
RX PubMed=2448177; DOI=10.1111/j.1432-0436.1987.tb00066.x;
RA Rentrop M., Nischt R., Knapp B., Schweizer J., Winter H.;
RT "An unusual type-II 70-kilodalton keratin protein of mouse epidermis
RT exhibiting postnatal body-site specificity and sensitivity to
RT hyperproliferation.";
RL Differentiation 34:189-200(1987).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA52788.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=NMRI {ECO:0000312|EMBL:CAA52788.1};
RX PubMed=7508961; DOI=10.1111/1523-1747.ep12371757;
RA Herzog F., Winter H., Schweizer J.;
RT "The large type II 70-kDa keratin of mouse epidermis is the ortholog of
RT human keratin K2e.";
RL J. Invest. Dermatol. 102:165-170(1994).
RN [3] {ECO:0000312|EMBL:BAE21186.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE36187.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAE36187.1};
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 [4] {ECO:0000312|EMBL:AAI20486.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI20486.1};
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 [5]
RP PROTEIN SEQUENCE OF 23-36; 210-216; 288-296 AND 483-491, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6] {ECO:0000305}
RP INTERACTION WITH KRT10.
RX PubMed=9378767; DOI=10.1242/jcs.110.18.2175;
RA Reichelt J., Bauer C., Porter R., Lane E., Magin V.;
RT "Out of balance: consequences of a partial keratin 10 knockout.";
RL J. Cell Sci. 110:2175-2186(1997).
RN [7] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15118396; DOI=10.1159/000077033;
RA Mahler B., Gocken T., Brojan M., Childress S., Spandau D.F., Foley J.;
RT "Keratin 2e: a marker for murine nipple epidermis.";
RL Cells Tissues Organs 176:169-177(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24751727; DOI=10.1038/jid.2014.197;
RA Fischer H., Langbein L., Reichelt J., Praetzel-Wunder S., Buchberger M.,
RA Ghannadan M., Tschachler E., Eckhart L.;
RT "Loss of keratin K2 expression causes aberrant aggregation of K10,
RT hyperkeratosis, and inflammation.";
RL J. Invest. Dermatol. 134:2579-2588(2014).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22; ARG-52; ARG-555 AND ARG-593,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26603179; DOI=10.1016/j.jdermsci.2015.10.008;
RA Fischer H., Langbein L., Reichelt J., Buchberger M., Tschachler E.,
RA Eckhart L.;
RT "Keratins K2 and K10 are essential for the epidermal integrity of plantar
RT skin.";
RL J. Dermatol. Sci. 81:10-16(2016).
RN [12] {ECO:0000305}
RP VARIANT IBS PRO-500.
RX PubMed=12533510; DOI=10.1101/gad.1023703;
RA Fitch K.R., McGowan K.A., van Raamsdonk C.D., Fuchs H., Lee D., Puech A.,
RA Herault Y., Threadgill D.W., Hrabe de Angelis M., Barsh G.S.;
RT "Genetics of dark skin in mice.";
RL Genes Dev. 17:214-228(2003).
CC -!- FUNCTION: Probably contributes to terminal cornification (By
CC similarity). Associated with keratinocyte activation, proliferation and
CC keratinization (By similarity). Required for maintenance of corneocytes
CC and keratin filaments in suprabasal keratinocytes in the epidermis of
CC the ear, potentially via moderation of expression and localization of
CC keratins and their partner proteins (PubMed:24751727). Plays a role in
CC the establishment of the epidermal barrier on plantar skin
CC (PubMed:26603179). {ECO:0000250|UniProtKB:P35908,
CC ECO:0000269|PubMed:24751727, ECO:0000269|PubMed:26603179}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Associates with KRT10. {ECO:0000269|PubMed:9378767, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24751727}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the suprabasal layers of
CC the plantar epidermis outside of the footpads (at protein level)
CC (PubMed:26603179). Expressed in the suprabasal layers of the
CC interfollicular epidermis of the ear, in the interscale regions distant
CC from the hair follicles in the tail, and in the soles of the footpads
CC (at protein level) (PubMed:24751727). Expressed mainly in the middle
CC spinous and granular cells of the epidermis of adult tail, nipple and
CC footsole skin. Also found in ear. {ECO:0000269|PubMed:15118396,
CC ECO:0000269|PubMed:2448177, ECO:0000269|PubMed:24751727,
CC ECO:0000269|PubMed:26603179, ECO:0000269|PubMed:7508961}.
CC -!- DEVELOPMENTAL STAGE: Induction occurs during the first 2 weeks after
CC birth, being first observed in the epidermis of tail then the footpad
CC and later in the ear. {ECO:0000269|PubMed:2448177}.
CC -!- DISEASE: Note=Defects in Krt2 are a cause of ichthyosis bullosa of
CC siemens (IBS). IBS is a rare autosomal dominant disorder displaying a
CC type of epidermolytic hyperkeratosis characterized by extensive
CC blistering from birth. Hyperkeratoses and shedding of the outer layers
CC of the epidermis (molting) are observed in later weeks.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and display no differences in
CC size and body weight (PubMed:24751727, PubMed:26603179). Scaly skin and
CC increased pigmentation on ears and hyperkeratotic calluses on the soles
CC and toe pads within 6 weeks of birth (PubMed:24751727,
CC PubMed:26603179). Prominent acanthosis, orthokeratotic hyperkeratosis
CC in the epidermis of the ear and to a lesser extent in the epidermis of
CC the tail and the palm skin caused by an increase in cell proliferation
CC and thicker granular layer (PubMed:24751727). Keratinocyte
CC differentiation is disorganized, large coalescent granules are
CC accumulated, and cytolysis is evidence in the ear skin
CC (PubMed:24751727). Increase in defective corneocytes and an increase in
CC transepidermal water loss in ear skin (PubMed:24751727). Suprabasal
CC keratinocytes contain distinct spongy clumps of Krt10 filaments
CC (PubMed:24751727). Increase in Tslp and Il18 expression, and abundance
CC of T-cells and mast cells in ear skin (PubMed:24751727). Increase in
CC expression of Krt1, Krt10, Krt16, Flg and Loricrin in the ear epidermis
CC (PubMed:24751727). Krt1, Krt5, Krt10, Krt16, Flg and Loricrin all show
CC disordered localization within the ear epidermis (PubMed:24751727).
CC Krt10 specifically show aggregation within the cytoplasm in epidermal
CC cells of the ear (PubMed:24751727). Show no epidermal aberrations of
CC the footpads (PubMed:26603179). Double knockout mice of KRT2 and KRT10
CC are viable and display no differences in size and body weight
CC (PubMed:26603179). Show a more severe plantar epidermis phenotype as in
CC single KRT2 knockout mice (PubMed:26603179).
CC {ECO:0000269|PubMed:24751727, ECO:0000269|PubMed:26603179}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X74784; CAA52788.1; -; mRNA.
DR EMBL; AK132476; BAE21186.1; -; mRNA.
DR EMBL; AK161078; BAE36187.1; -; mRNA.
DR EMBL; AK161098; BAE36194.1; -; mRNA.
DR EMBL; BC120485; AAI20486.1; -; mRNA.
DR CCDS; CCDS37220.1; -.
DR RefSeq; NP_034798.2; NM_010668.2.
DR AlphaFoldDB; Q3TTY5; -.
DR SMR; Q3TTY5; -.
DR BioGRID; 201033; 13.
DR IntAct; Q3TTY5; 2.
DR STRING; 10090.ENSMUSP00000023712; -.
DR iPTMnet; Q3TTY5; -.
DR PhosphoSitePlus; Q3TTY5; -.
DR CPTAC; non-CPTAC-3922; -.
DR jPOST; Q3TTY5; -.
DR PaxDb; Q3TTY5; -.
DR PRIDE; Q3TTY5; -.
DR ProteomicsDB; 269145; -.
DR Antibodypedia; 1398; 291 antibodies from 30 providers.
DR DNASU; 16681; -.
DR Ensembl; ENSMUST00000023712; ENSMUSP00000023712; ENSMUSG00000064201.
DR GeneID; 16681; -.
DR KEGG; mmu:16681; -.
DR UCSC; uc007xub.1; mouse.
DR CTD; 3849; -.
DR MGI; MGI:96699; Krt2.
DR VEuPathDB; HostDB:ENSMUSG00000064201; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000162573; -.
DR HOGENOM; CLU_012560_6_0_1; -.
DR InParanoid; Q3TTY5; -.
DR OMA; YERHVWE; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q3TTY5; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16681; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q3TTY5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3TTY5; protein.
DR Bgee; ENSMUSG00000064201; Expressed in tail skin and 40 other tissues.
DR Genevisible; Q3TTY5; MM.
DR GO; GO:0001533; C:cornified envelope; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IDA:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IMP:MGI.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
DR GO; GO:0031424; P:keratinization; ISO:MGI.
DR GO; GO:0032980; P:keratinocyte activation; ISO:MGI.
DR GO; GO:0003334; P:keratinocyte development; IMP:MGI.
DR GO; GO:0051546; P:keratinocyte migration; ISO:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; ISO:MGI.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR GO; GO:0045684; P:positive regulation of epidermis development; IMP:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Disease variant;
KW Ichthyosis; Intermediate filament; Keratin; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..707
FT /note="Keratin, type II cytoskeletal 2 epidermal"
FT /id="PRO_0000283763"
FT DOMAIN 199..512
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..198
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..234
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 235..253
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 254..345
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 346..369
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 370..508
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 509..707
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 531..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 450
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 22
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 52
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35908"
FT MOD_RES 555
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 593
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 607
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 675
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT VARIANT 500
FT /note="T -> P (in IBS)"
FT /evidence="ECO:0000269|PubMed:12533510"
FT CONFLICT 238..246
FT /note="DVGSRTTNL -> ACRQPHHKP (in Ref. 2; CAA52788)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="N -> T (in Ref. 2; CAA52788)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="K -> I (in Ref. 2; CAA52788)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="R -> H (in Ref. 2; CAA52788)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="V -> M (in Ref. 2; CAA52788)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="Missing (in Ref. 4; AAI20486)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="T -> S (in Ref. 2; CAA52788)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="G -> GG (in Ref. 4; AAI20486)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="V -> A (in Ref. 2; CAA52788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 70923 MW; 464D375DCBA90EF4 CRC64;
MSCQISCRSR RGGGGGGGGG FRGFSSGSAV VSGGSRRSNT SFSCISRHGG GRGGSGGGGF
GSQSLVGLGG YKSISSSVAG NSGGYGGSSF GGSSGFGGGR GFGGGQGFGG SGGFGGGSGF
GGGQGFGGGS RFGGGSGFGG GGFGGGSFGG GRFGGGPGGF GGPGGFPGGG IHEVSVNQSL
LQPLDVKVDP EIQNVKSQER EQIKTLNNKF ASFIDKVRFL EQQNQVLRTK WELLQQLDVG
SRTTNLDPIF QAYIGMLKKQ VDRLSAERTS QESELNNMQD LVEDFKKKYE DEINKRTSAE
NDFVTIKKDV DSCYMDKTEL QARLDILAQE VNFLRTLYDA ELSQLQQDVT DTNVILSMDN
NRNLDLDSII AEVQNQYEMI AHKSKAESEE LYHSKYEELQ VTAVKHGDSL KEIKMEISEL
NRTIQRLQGE ISHVKKQCKG VQDSIADAEQ RGEHAIKDAR GKLTDLEEAL QQCREDLARL
LRDYQELMNT KLSLDVEIAT YRKLLEGEEC RMSGDFSDNV SVSITSSTIS SSVASKTGFG
SGGQSSGGRG SYGGRGGGGG GGSTYGSGGR SSGSRGSGSG SGGGGYSSGG GSRGGSGGGY
GSGGGSRGGS GGGYGSGGGS GSGGGYSSGG GSRGGSGGGG VSSGGGSRGG SSSGGGSRGG
SSSGGGGYSS GGGSRGGSSS GGAGSSSEKG GSGSGEGCGS GVTFSFR
