K1C10_MOUSE
ID K1C10_MOUSE Reviewed; 570 AA.
AC P02535; P08731; Q8BUX3; Q8BV09; Q8BVU3; Q9CXH6; Q9JKB4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Keratin, type I cytoskeletal 10;
DE AltName: Full=56 kDa cytokeratin;
DE AltName: Full=Cytokeratin-10;
DE Short=CK-10;
DE AltName: Full=Keratin, type I cytoskeletal 59 kDa;
DE AltName: Full=Keratin-10;
DE Short=K10;
GN Name=Krt10; Synonyms=Krt1-10;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=2581944; DOI=10.1016/s0021-9258(18)88905-0;
RA Krieg T.M., Schafer M.P., Cheng C.K., Filpula D., Flaherty P.,
RA Steinert P.M., Roop D.R.;
RT "Organization of a type I keratin gene. Evidence for evolution of
RT intermediate filaments from a common ancestral gene.";
RL J. Biol. Chem. 260:5867-5870(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=6188955; DOI=10.1038/302794a0;
RA Steinert P.M., Rice R.H., Roop D.R., Trus B.L., Steven A.C.;
RT "Complete amino acid sequence of a mouse epidermal keratin subunit and
RT implications for the structure of intermediate filaments.";
RL Nature 302:794-800(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Head;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-341 (ISOFORMS 2/3).
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Reichelt J., Magin T.M.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=11408584; DOI=10.1091/mbc.12.6.1775;
RA Peters B., Kirfel J., Bussow H., Vidal M., Magin T.M.;
RT "Complete cytolysis and neonatal lethality in keratin 5 knockout mice
RT reveal its fundamental role in skin integrity and in epidermolysis bullosa
RT simplex.";
RL Mol. Biol. Cell 12:1775-1789(2001).
RN [6]
RP PROTEIN SEQUENCE OF 146-154; 164-175; 227-233; 244-254; 361-367; 385-397
RP AND 440-448, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STAPHYLOCOCCUS AUREUS
RP CLFB (MICROBIAL INFECTION).
RX PubMed=15385531; DOI=10.1074/jbc.m408713200;
RA Walsh E.J., O'Brien L.M., Liang X., Hoeoek M., Foster T.J.;
RT "Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface
RT components recognizing adhesive matrix molecules) adhesin of Staphylococcus
RT aureus, also binds to the tail region of type I cytokeratin 10.";
RL J. Biol. Chem. 279:50691-50699(2004).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH S.PNEUMONIAE PSRP
RP (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19627498; DOI=10.1111/j.1365-2958.2009.06796.x;
RA Shivshankar P., Sanchez C., Rose L.F., Orihuela C.J.;
RT "The Streptococcus pneumoniae adhesin PsrP binds to keratin 10 on lung
RT cells.";
RL Mol. Microbiol. 73:663-679(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-48, AND
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 [10]
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 [11]
RP IDENTIFICATION IN A COMPLEX WITH KRT1, AND INTERACTION WITH KRT1 AND PLEC.
RX PubMed=24940650; DOI=10.1038/jid.2014.255;
RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.;
RT "Interaction of plectin with keratins 5 and 14: dependence on several
RT plectin domains and keratin quaternary structure.";
RL J. Invest. Dermatol. 134:2776-2783(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-32, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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 [13]
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).
CC -!- FUNCTION: Plays a role in the establishment of the epidermal barrier on
CC plantar skin (PubMed:26603179). Involved in the maintenance of cell
CC layer development and keratin filament bundles in suprabasal cells of
CC the epithelium (PubMed:24751727). {ECO:0000269|PubMed:24751727,
CC ECO:0000269|PubMed:26603179}.
CC -!- FUNCTION: (Microbial infection) Acts as a mediator of S.aureus
CC adherence to desquamated nasal epithelial cells via clfB, and hence may
CC play a role in nasal colonization. {ECO:0000269|PubMed:15385531}.
CC -!- FUNCTION: (Microbial infection) Binds S.pneumoniae PsrP, mediating
CC adherence of the bacteria to lung cell lines.
CC {ECO:0000269|PubMed:19627498}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminal tail domain)
CC with the S.aureus clumping factor, clfB; this interaction probably
CC mediates S.aureus attachment to the highly keratinized squamous
CC epithelial cells from the nasal cavity. {ECO:0000269|PubMed:15385531}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Heterodimer with KRT1 (PubMed:24940650). Two heterodimers of KRT1 and
CC KRT10 form a heterotetramer (By similarity). The KRT10 subunit in the
CC heterotetramer is probably disulfide-linked (By similarity). Interacts
CC with PLEC isoform 1C, when in a heterodimer with KRT1
CC (PubMed:24940650). {ECO:0000250|UniProtKB:P13645,
CC ECO:0000269|PubMed:24940650}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via the C-terminal tail
CC domain) with S.pneumoniae serine-rich repeat protein PsrP; this
CC interaction probably mediates S.pneumoniae adherence to lung tissue and
CC subsequent pathogenesis. {ECO:0000269|PubMed:19627498}.
CC -!- INTERACTION:
CC P02535; Q60680-1: Chuk; NbExp=6; IntAct=EBI-646288, EBI-646260;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P13645}. Cell surface
CC {ECO:0000269|PubMed:19627498}. Cytoplasm {ECO:0000269|PubMed:24751727}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P02535-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P02535-2; Sequence=VSP_021100, VSP_021101;
CC Name=3;
CC IsoId=P02535-3; Sequence=VSP_021100, VSP_021101, VSP_021102,
CC VSP_021103;
CC -!- TISSUE SPECIFICITY: Expressed in the suprabasal layers of the epidermis
CC throughout the entire sole (at protein level) (PubMed:24751727,
CC PubMed:26603179). Expressed in the infundibular regions of the ear, the
CC interscale regions of the tail, and the interfollicular epidermis of
CC the back (PubMed:24751727). Expressed in lung tissue from young mice
CC (at protein level) (PubMed:19627498). {ECO:0000269|PubMed:19627498,
CC ECO:0000269|PubMed:24751727, ECO:0000269|PubMed:26603179}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the skin at birth.
CC {ECO:0000269|PubMed:11408584}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and display no differences in
CC size and body weight (PubMed:26603179). Show acanthosis, hyperkeratosis
CC and scaling of the stratum corneum in plantar skin (PubMed:26603179).
CC Increase in the number of epidermal cell layers and a decrease in the
CC abundance of cytoplasmic keratin filament bundles in suprabasal cells
CC (PubMed:24751727). Large keratohyalin granules of various shapes are
CC evident in the upper suprabasal cells (PubMed:24751727). KRT2
CC aggregates form in the cytoplasm of keratinocytes (PubMed:24751727).
CC Show no epidermal aberrations of the footpads (PubMed:26603179). Double
CC knockout mice of KRT10 and KRT2 are viable and display no differences
CC in size and body weight (PubMed:26603179). Show a more severe epidermis
CC phenotype as in single KRT10 knockout mice (PubMed:24751727,
CC PubMed:26603179). {ECO:0000269|PubMed:24751727,
CC 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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29296.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L00193; AAA39391.1; -; Genomic_DNA.
DR EMBL; M10081; AAA39391.1; JOINED; Genomic_DNA.
DR EMBL; V00830; CAA24214.1; -; mRNA.
DR EMBL; AK014360; BAB29296.1; ALT_FRAME; mRNA.
DR EMBL; AK076508; BAC36371.1; -; mRNA.
DR EMBL; AK081402; BAC38210.1; -; mRNA.
DR EMBL; AK081914; BAC38369.1; -; mRNA.
DR EMBL; AF245658; AAF65456.1; -; Genomic_DNA.
DR CCDS; CCDS25380.1; -. [P02535-2]
DR PIR; A02940; KRMSE1.
DR PIR; S07330; S07330.
DR RefSeq; NP_034790.2; NM_010660.2.
DR AlphaFoldDB; P02535; -.
DR SMR; P02535; -.
DR BioGRID; 201017; 14.
DR ComplexPortal; CPX-5871; Keratin-1 - Keratin-10 dimer complex.
DR IntAct; P02535; 1.
DR STRING; 10090.ENSMUSP00000099420; -.
DR iPTMnet; P02535; -.
DR PhosphoSitePlus; P02535; -.
DR CPTAC; non-CPTAC-3987; -.
DR jPOST; P02535; -.
DR PRIDE; P02535; -.
DR ProteomicsDB; 268932; -. [P02535-1]
DR ProteomicsDB; 268933; -. [P02535-2]
DR ProteomicsDB; 268934; -. [P02535-3]
DR DNASU; 16661; -.
DR GeneID; 16661; -.
DR KEGG; mmu:16661; -.
DR CTD; 3858; -.
DR MGI; MGI:96685; Krt10.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; P02535; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; P02535; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16661; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Krt10; mouse.
DR PRO; PR:P02535; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P02535; protein.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; IDA:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IGI:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR GO; GO:0008544; P:epidermis development; IGI:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IGI:MGI.
DR GO; GO:0003334; P:keratinocyte development; IGI:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; IDA:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR GO; GO:0045684; P:positive regulation of epidermis development; IMP:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; IDA:MGI.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
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 Alternative splicing; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Intermediate filament; Keratin; Methylation;
KW Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..570
FT /note="Keratin, type I cytoskeletal 10"
FT /id="PRO_0000063643"
FT DOMAIN 144..458
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..143
FT /note="Head"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..179
FT /note="Coil 1A"
FT REGION 180..200
FT /note="Linker 1"
FT REGION 201..292
FT /note="Coil 1B"
FT REGION 293..315
FT /note="Linker 12"
FT REGION 316..454
FT /note="Coil 2"
FT REGION 451..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..570
FT /note="Tail"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 396
FT /note="Stutter"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 32
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 32
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT DISULFID 399
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT VAR_SEQ 97..106
FT /note="YGGSSFGGAG -> S (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021100"
FT VAR_SEQ 144..145
FT /note="GR -> EK (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021101"
FT VAR_SEQ 465..471
FT /note="RGGSGGG -> PRRQPRR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021102"
FT VAR_SEQ 472..570
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021103"
FT CONFLICT 4
FT /note="L -> R (in Ref. 4; AAF65456)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="S -> C (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="G -> GGG (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="S -> F (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="S -> F (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="Y -> L (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="G -> E (in Ref. 1; AAA39391)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="G -> R (in Ref. 3; BAB29296)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="G -> V (in Ref. 3; BAB29296)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..106
FT /note="AG -> GS (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..123
FT /note="SY -> GC (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> G (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="Q -> R (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..188
FT /note="WYEKHGNSSQ -> VVREARQLKP (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..269
FT /note="KSDLEM -> QSVLEL (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="E -> G (in Ref. 3; BAC38210)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="H -> L (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="E -> A (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..400
FT /note="EGRYCV -> VESLLR (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> G (in Ref. 3; BAB29296/BAC36371/BAC38210)"
FT /evidence="ECO:0000305"
FT CONFLICT 466..467
FT /note="GG -> AD (in Ref. 3; BAB29296)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="G -> H (in Ref. 3; BAB29296/BAC36371/BAC38210)"
FT /evidence="ECO:0000305"
FT CONFLICT 509..515
FT /note="GGSHGGS -> CGGRGGG (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> G (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="H -> R (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="S -> G (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="S -> G (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 548..549
FT /note="GQ -> RR (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 556..557
FT /note="KS -> SGT (in Ref. 2; CAA24214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 57770 MW; EE60EA87DE7770E0 CRC64;
MSVLYSSSSK QFSSSRSGGG GGGGSVRVSS TRGSLGGGYS SGGFSGGSFS RGSSGGGCFG
GSSGGYGGFG GGGSFGGGYG GSSFGGGYGG SSFGGGYGGS SFGGAGFGGG GSFGGGSFGG
GSYGGGFGGG GFGGDGGSLL SGNGRVTMQN LNDRLASYMD KVRALEESNY ELEGKIKEWY
EKHGNSSQRE PRDYSKYYKT IEDLKGQILT LTTDNANVLL QIDNARLAAD DFRLKYENEV
TLRQSVEADI NGLRRVLDEL TLSKSDLEMQ IESLNEELAY LKKNHEEEMR DLQNVSTGDV
NVEMNAAPGV DLTQLLNNMR NQYEQLAEKN RKDAEEWFNQ KSKELTTEID SNIEQMSSHK
SEITELRRTV QGLEIELQSQ LALKQSLEAS LAETEGRYCV QLSQIQSQIS ALEEQLQQIR
AETECQNAEY QQLLDIKTRL ENEIQTYRSL LEGEGSSSGG GGGRRGGSGG GSYGGSSGGG
SYGGSSGGGG SYGGSSGGGG SYGGGSSGGG SHGGSSGGGY GGGSSSGGAG GHGGSSGGGY
GGGSSSGGQG GSGGFKSSGG GDQSSKGPRY
