KTN1_MOUSE
ID KTN1_MOUSE Reviewed; 1327 AA.
AC Q61595; Q8BG49; Q8BHF4; Q8BHM8; Q8C9Y5; Q8CG51; Q8CG52; Q8CG53; Q8CG54;
AC Q8CG55; Q8CG56; Q8CG57; Q8CG58; Q8CG59; Q8CG60; Q8CG61; Q8CG62; Q8CG63;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Kinectin;
GN Name=Ktn1 {ECO:0000312|MGI:MGI:109153};
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, ECO:0000312|EMBL:AAB65839.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=8912005; DOI=10.1038/icb.1996.72;
RA Leung E., Print C.G., Parry D.A.D., Closey D.N., Lockhart P.J.,
RA Skinner S.J.M., Batchelor D.C., Krissansen G.W.;
RT "Cloning of novel kinectin splice variants with alternative C-termini:
RT structure, distribution and evolution of mouse kinectin.";
RL Immunol. Cell Biol. 74:421-433(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC30538.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-527.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC30538.1};
RC TISSUE=Thymus {ECO:0000312|EMBL:BAC30538.1};
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 [3] {ECO:0000312|EMBL:CAD56924.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 803-1327 (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9;
RP 10; 11; 12; 13; 14; 15 AND 16), SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Swiss Webster {ECO:0000269|PubMed:15316074};
RC TISSUE=Astrocyte {ECO:0000269|PubMed:15316074}, and
RC Hippocampus {ECO:0000269|PubMed:15316074};
RX PubMed=15316074; DOI=10.1242/jcs.01326;
RA Santama N., Er C.P.N., Ong L.-L., Yu H.;
RT "Distribution and functions of kinectin isoforms.";
RL J. Cell Sci. 117:4537-4549(2004).
RN [4]
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).
CC -!- FUNCTION: Receptor for kinesin thus involved in kinesin-driven vesicle
CC motility. Accumulates in integrin-based adhesion complexes (IAC) upon
CC integrin aggregation by fibronectin (By similarity).
CC {ECO:0000250|UniProtKB:Q86UP2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15316074}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15316074}. Note=Vesicle membrane protein anchored
CC to the endoplasmic reticulum (By similarity). Some isoforms containing
CC the inserts at residues 1007-1035 and 1154-1177 are detected in neurite
CC processes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=16;
CC Name=1 {ECO:0000269|PubMed:8912005};
CC IsoId=Q61595-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15316074}; Synonyms=KNT1
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-2; Sequence=VSP_052042, VSP_052043, VSP_052044,
CC VSP_052045, VSP_052046;
CC Name=3 {ECO:0000269|PubMed:15316074}; Synonyms=KNT2
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-3; Sequence=VSP_052042, VSP_052043, VSP_052044,
CC VSP_052046;
CC Name=4 {ECO:0000269|PubMed:15316074}; Synonyms=KNT3
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-4; Sequence=VSP_052042, VSP_052043, VSP_052045;
CC Name=5 {ECO:0000269|PubMed:15316074}; Synonyms=KNT4
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-5; Sequence=VSP_052043, VSP_052046;
CC Name=6 {ECO:0000269|PubMed:15316074}; Synonyms=KNT5
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-6; Sequence=VSP_052043, VSP_052045, VSP_052046;
CC Name=7 {ECO:0000269|PubMed:15316074}; Synonyms=KNT6
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-7; Sequence=VSP_052042, VSP_052044;
CC Name=8 {ECO:0000269|PubMed:15316074}; Synonyms=KNT7
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-8; Sequence=VSP_052042, VSP_052044, VSP_052045;
CC Name=9 {ECO:0000269|PubMed:15316074}; Synonyms=KNT8
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-9; Sequence=VSP_052044, VSP_052045, VSP_052046;
CC Name=10 {ECO:0000269|PubMed:15316074}; Synonyms=KNT9
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-10; Sequence=VSP_052042, VSP_052043;
CC Name=11 {ECO:0000269|PubMed:15316074}; Synonyms=KNT10
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-11; Sequence=VSP_052042;
CC Name=12 {ECO:0000269|PubMed:15316074}; Synonyms=KNT11
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-12; Sequence=VSP_052042, VSP_052043, VSP_052044,
CC VSP_052045;
CC Name=13 {ECO:0000269|PubMed:15316074}; Synonyms=KNT12
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-13; Sequence=VSP_052042, VSP_052045, VSP_052046;
CC Name=14 {ECO:0000269|PubMed:15316074}; Synonyms=KNT13
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-14; Sequence=VSP_052042, VSP_052044, VSP_052045,
CC VSP_052046;
CC Name=15 {ECO:0000269|PubMed:15316074}; Synonyms=KNT14
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-15; Sequence=VSP_052044, VSP_052045;
CC Name=16 {ECO:0000269|PubMed:15316074}; Synonyms=KNT15
CC {ECO:0000269|PubMed:15316074};
CC IsoId=Q61595-16; Sequence=VSP_052042, VSP_052043, VSP_052045,
CC VSP_052046;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including 12-day
CC embryo, adult heart, brain, ovary, kidney, lung, small intestine,
CC spleen, thymus and pancreas. {ECO:0000269|PubMed:8912005}.
CC -!- DEVELOPMENTAL STAGE: Isoform 6, isoform 7 and isoform 8 are detected in
CC embryonic hippocampus but not in later developmental stages. Isoform
CC 14, isoform 15 and isoform 16 are adult-specific.
CC {ECO:0000269|PubMed:15316074}.
CC -!- SIMILARITY: Belongs to the kinectin family. {ECO:0000255}.
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DR EMBL; L43326; AAB65839.1; -; mRNA.
DR EMBL; AK040200; BAC30538.1; -; mRNA.
DR EMBL; AJ517365; CAD56924.1; -; mRNA.
DR EMBL; AJ517366; CAD56925.1; -; mRNA.
DR EMBL; AJ517367; CAD56926.1; -; mRNA.
DR EMBL; AJ517368; CAD56927.1; -; mRNA.
DR EMBL; AJ517369; CAD56928.1; -; mRNA.
DR EMBL; AJ517370; CAD56929.1; -; mRNA.
DR EMBL; AJ517371; CAD56930.1; -; mRNA.
DR EMBL; AJ517372; CAD56931.1; -; mRNA.
DR EMBL; AJ517373; CAD56932.1; -; mRNA.
DR EMBL; AJ517374; CAD56933.1; -; mRNA.
DR EMBL; AJ517375; CAD56934.1; -; mRNA.
DR EMBL; AJ517376; CAD56935.1; -; mRNA.
DR EMBL; AJ517377; CAD56936.1; -; mRNA.
DR EMBL; AJ517378; CAD56937.1; -; mRNA.
DR EMBL; AJ517379; CAD56938.1; -; mRNA.
DR EMBL; AJ517380; CAD56939.1; -; mRNA.
DR EMBL; AJ517381; CAD56940.1; -; mRNA.
DR EMBL; AJ517382; CAD56941.1; -; mRNA.
DR EMBL; AJ517383; CAD56942.1; -; mRNA.
DR EMBL; AJ517384; CAD56943.1; -; mRNA.
DR CCDS; CCDS36900.1; -. [Q61595-1]
DR CCDS; CCDS84123.1; -. [Q61595-9]
DR CCDS; CCDS84124.1; -. [Q61595-5]
DR CCDS; CCDS84125.1; -. [Q61595-6]
DR CCDS; CCDS84126.1; -. [Q61595-11]
DR CCDS; CCDS84127.1; -. [Q61595-13]
DR CCDS; CCDS84130.1; -. [Q61595-14]
DR CCDS; CCDS84132.1; -. [Q61595-4]
DR CCDS; CCDS84133.1; -. [Q61595-16]
DR CCDS; CCDS84135.1; -. [Q61595-12]
DR CCDS; CCDS84136.1; -. [Q61595-2]
DR RefSeq; NP_001280564.1; NM_001293635.1.
DR RefSeq; NP_001280565.1; NM_001293636.1.
DR RefSeq; NP_001334448.1; NM_001347519.1.
DR RefSeq; NP_001334449.1; NM_001347520.1.
DR RefSeq; NP_001334450.1; NM_001347521.1.
DR RefSeq; NP_001334452.1; NM_001347523.1.
DR RefSeq; NP_001334453.1; NM_001347524.1.
DR RefSeq; NP_001334454.1; NM_001347525.1.
DR RefSeq; NP_001334455.1; NM_001347526.1.
DR RefSeq; NP_001334456.1; NM_001347527.1.
DR RefSeq; NP_001334457.1; NM_001347528.1.
DR RefSeq; NP_032503.2; NM_008477.2.
DR AlphaFoldDB; Q61595; -.
DR SMR; Q61595; -.
DR BioGRID; 201049; 84.
DR IntAct; Q61595; 6.
DR MINT; Q61595; -.
DR STRING; 10090.ENSMUSP00000140324; -.
DR GlyGen; Q61595; 3 sites.
DR iPTMnet; Q61595; -.
DR PhosphoSitePlus; Q61595; -.
DR SwissPalm; Q61595; -.
DR EPD; Q61595; -.
DR jPOST; Q61595; -.
DR MaxQB; Q61595; -.
DR PaxDb; Q61595; -.
DR PeptideAtlas; Q61595; -.
DR PRIDE; Q61595; -.
DR ProteomicsDB; 264882; -. [Q61595-1]
DR ProteomicsDB; 264883; -. [Q61595-2]
DR ProteomicsDB; 264884; -. [Q61595-3]
DR ProteomicsDB; 264885; -. [Q61595-4]
DR ProteomicsDB; 264886; -. [Q61595-5]
DR ProteomicsDB; 264887; -. [Q61595-6]
DR ProteomicsDB; 264888; -. [Q61595-7]
DR ProteomicsDB; 264889; -. [Q61595-8]
DR ProteomicsDB; 264890; -. [Q61595-9]
DR ProteomicsDB; 264891; -. [Q61595-10]
DR ProteomicsDB; 264892; -. [Q61595-11]
DR ProteomicsDB; 264893; -. [Q61595-12]
DR ProteomicsDB; 264894; -. [Q61595-13]
DR ProteomicsDB; 264895; -. [Q61595-14]
DR ProteomicsDB; 264896; -. [Q61595-15]
DR ProteomicsDB; 264897; -. [Q61595-16]
DR DNASU; 16709; -.
DR GeneID; 16709; -.
DR KEGG; mmu:16709; -.
DR CTD; 3895; -.
DR MGI; MGI:109153; Ktn1.
DR eggNOG; ENOG502QSIW; Eukaryota.
DR InParanoid; Q61595; -.
DR OrthoDB; 327650at2759; -.
DR PhylomeDB; Q61595; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 16709; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Ktn1; mouse.
DR PRO; PR:Q61595; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61595; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0019894; F:kinesin binding; TAS:MGI.
DR GO; GO:0007018; P:microtubule-based movement; TAS:MGI.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR InterPro; IPR024854; Kinectin.
DR InterPro; IPR007794; Rib_rcpt_KP.
DR PANTHER; PTHR18864; PTHR18864; 1.
DR Pfam; PF05104; Rib_recp_KP_reg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1327
FT /note="Kinectin"
FT /id="PRO_0000238620"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..1327
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 49..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 329..1327
FT /evidence="ECO:0000255"
FT COMPBIAS 63..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP2"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 836..858
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 7, isoform 8, isoform 10, isoform 11, isoform 12, isoform
FT 13, isoform 14 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:15316074"
FT /id="VSP_052042"
FT VAR_SEQ 1007..1035
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6, isoform 10, isoform 12 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:15316074"
FT /id="VSP_052043"
FT VAR_SEQ 1154..1177
FT /note="Missing (in isoform 2, isoform 3, isoform 7, isoform
FT 8, isoform 9, isoform 12, isoform 14 and isoform 15)"
FT /evidence="ECO:0000303|PubMed:15316074"
FT /id="VSP_052044"
FT VAR_SEQ 1208..1235
FT /note="Missing (in isoform 2, isoform 4, isoform 6, isoform
FT 8, isoform 9, isoform 12, isoform 13, isoform 14, isoform
FT 15 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:15316074"
FT /id="VSP_052045"
FT VAR_SEQ 1294..1327
FT /note="ESPEKETMSVSLNQTVTQLQQLLQEVNQQLTKET -> SEVIGKLLVRS
FT (in isoform 2, isoform 3, isoform 5, isoform 6, isoform 9,
FT isoform 13, isoform 14 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:15316074"
FT /id="VSP_052046"
FT CONFLICT 10
FT /note="I -> V (in Ref. 2; BAC30538)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Q -> K (in Ref. 2; BAC30538)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="M -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="R -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="V -> VS (in Ref. 3; CAD56927)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183
FT /note="E -> G (in Ref. 3; CAD56935)"
FT /evidence="ECO:0000305"
FT CONFLICT 1238
FT /note="L -> F (in Ref. 3; CAD56936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1327 AA; 152592 MW; 2B79EB332D2470E5 CRC64;
MELYESTYFI VLIPSVVITV IFLFFWLFMK ETLYDEVLAK QKREQKLIST KTDKKKAEKK
KNKKKEIQNG TLRESDSEHV PRDFKLSDAS PAEDEQFVPA PLNVAETSSS VRERQKKEKK
QKPSLEEQVI KESDASKIPG KKVEPVLVTK QPAPPPPLEA AALKKKAGQK KSKNGSEEQD
KKVEMLMAPS KEQDVLLSHQ DTKQEGGLGK KKGLSKKQKS ENVAVLVDEP LIHATTYMPL
DNANSNLMMD KREIIDMIKP DHVEGIQKSG TKKLKIETDK ENAEVKFKDF LLSLKTMMFS
EDEALCVVDL LKEKSGVIKE ALKKSNKGEL SGLLHQLQEK ERLLSAMKED AAASKERCKR
LTQEMMTEKE RSSVVIARMK DRIGTLEKEH NIFQNKMHAS YQETQQMQMK FQQVQEQMEA
EIAHLKQENG ILRDAVSNTT NQLESKQSAE LNKLRQDCGR LVSELNEKTG KLQQEGVQKK
NAEQAATQLK VQLQEAERRW EEVQSYIRKR TAEHEAAQQD LQSKFVAKEN EVQSLHSKLT
DTLVSKQQLE QRLMQLMESE QKRASKEESL QIQVQDILEQ NEALKAQIQQ FHSQIAAQTS
ASVLAEELHK VIAEKDKQLK QTEDSLANEQ DHLASKEEEL KDVQNMNFLL KAEVQKWQAL
ANEQAATAHE VEKMQKSIHV KEDEIRLLEE QLQHEVASKM EELKILSEQN KALQSEVRKL
QTAVSQQPNK DVVEQMEKCI QEKDEKLRTV EELLETGLIQ VATREEELSA IRTENSTLTR
EVQELKAKQS DQVSFVSLIE DLKRVIHEKD GQIKSVEELL EVELLKVANK EKTVQALKQE
IEVLKEEIGN AQLEKAHQLS VTSQVQELQN LLRGKEEQVN SMKAALEDRD RGLTGRGTCA
QVCSTPQFEE LESVLKEKDN EIKRIEVKLK DTESDVSKMS ELLKEVQEEN KFLKCQLSHQ
KHQQASFPSQ EELQTVISEK EKEITDLCNE LESLKNAVEH QRKKNNDLRE KNWEAMEALA
STEKMLQDRV NKTSKERRQH VEAIELESKD LLKRLFPTVS VPSNLNYSEW LRGFEKKAKA
CVAGTSDAEA VKVLEHRLKE ASEMHTLLQL ECEKYKSVLA ETEGILQKLQ RSVEQEESKW
KIKADESQRM IKQMQSSFTA SERELERLRQ ENKDMENLRR EREHLEMELE KAEMERSTYV
MEVRELKDLL TELQKKLDDS YSEAVRQNEE LNLLKTQLNE THSKLQNEQT ERKKVADDLH
KAQQSLNSIH SKISLKAAGD TVVIENSDIS PEMESPEKET MSVSLNQTVT QLQQLLQEVN
QQLTKET
