KI21A_MOUSE
ID KI21A_MOUSE Reviewed; 1672 AA.
AC Q9QXL2; Q6P5H1; Q6ZPJ8; Q8BWZ9; Q8BXF1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Kinesin-like protein KIF21A;
GN Name=Kif21a; Synonyms=Kiaa1708;
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] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10225949; DOI=10.1083/jcb.145.3.469;
RA Marszalek J.R., Weiner J.A., Farlow S.J., Chun J., Goldstein L.S.;
RT "Novel dendritic kinesin sorting identified by different process targeting
RT of two related kinesins: KIF21A and KIF21B.";
RL J. Cell Biol. 145:469-479(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-551, AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1129-1672 (ISOFORM 4).
RC STRAIN=C57BL/6J;
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 [LARGE SCALE MRNA] OF 382-1672 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1660 AND SER-1671, AND
RP IDENTIFICATION BY 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-258; SER-1660 AND SER-1671,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1101; SER-1102 AND SER-1207
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Microtubule-binding motor protein probably involved in
CC neuronal axonal transport. In vitro, has a plus-end directed motor
CC activity. {ECO:0000269|PubMed:10225949}.
CC -!- SUBUNIT: Interacts (via residues 1148-1169) with KANK1 (via ankyrin
CC repeats 1-5) and KANK2 (via ankyrin repeats 1-5).
CC {ECO:0000250|UniProtKB:Q7Z4S6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10225949}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10225949}. Cell projection, axon
CC {ECO:0000269|PubMed:10225949}. Note=In neurons, localized to axons and
CC dendrites. {ECO:0000269|PubMed:10225949}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9QXL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QXL2-2; Sequence=VSP_010873, VSP_010874, VSP_010875;
CC Name=3;
CC IsoId=Q9QXL2-3; Sequence=VSP_010873, VSP_010876;
CC Name=4;
CC IsoId=Q9QXL2-4; Sequence=VSP_010877;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.
CC {ECO:0000269|PubMed:10225949}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AF202892; AAF17083.1; -; mRNA.
DR EMBL; BC060698; AAH60698.1; -; mRNA.
DR EMBL; BC062896; AAH62896.1; -; mRNA.
DR EMBL; AK129426; BAC98236.1; -; mRNA.
DR EMBL; AK049303; BAC33669.1; -; mRNA.
DR EMBL; AK047350; BAC33031.1; -; mRNA.
DR CCDS; CCDS37179.1; -. [Q9QXL2-2]
DR CCDS; CCDS49706.1; -. [Q9QXL2-3]
DR CCDS; CCDS49708.1; -. [Q9QXL2-1]
DR RefSeq; NP_001102510.1; NM_001109040.2. [Q9QXL2-1]
DR RefSeq; NP_001102511.1; NM_001109041.2.
DR RefSeq; NP_001102512.1; NM_001109042.2. [Q9QXL2-3]
DR RefSeq; NP_057914.2; NM_016705.4. [Q9QXL2-2]
DR PDB; 5YAY; X-ray; 1.55 A; B=1142-1169.
DR PDB; 5YBE; X-ray; 2.11 A; B=1151-1169.
DR PDBsum; 5YAY; -.
DR PDBsum; 5YBE; -.
DR AlphaFoldDB; Q9QXL2; -.
DR SMR; Q9QXL2; -.
DR BioGRID; 200939; 8.
DR IntAct; Q9QXL2; 7.
DR MINT; Q9QXL2; -.
DR STRING; 10090.ENSMUSP00000085985; -.
DR iPTMnet; Q9QXL2; -.
DR PhosphoSitePlus; Q9QXL2; -.
DR MaxQB; Q9QXL2; -.
DR PaxDb; Q9QXL2; -.
DR PeptideAtlas; Q9QXL2; -.
DR PRIDE; Q9QXL2; -.
DR ProteomicsDB; 264749; -. [Q9QXL2-1]
DR ProteomicsDB; 264750; -. [Q9QXL2-2]
DR ProteomicsDB; 264751; -. [Q9QXL2-3]
DR ProteomicsDB; 264752; -. [Q9QXL2-4]
DR Antibodypedia; 13055; 58 antibodies from 20 providers.
DR DNASU; 16564; -.
DR Ensembl; ENSMUST00000088614; ENSMUSP00000085985; ENSMUSG00000022629. [Q9QXL2-1]
DR Ensembl; ENSMUST00000109287; ENSMUSP00000104910; ENSMUSG00000022629. [Q9QXL2-3]
DR Ensembl; ENSMUST00000109288; ENSMUSP00000104911; ENSMUSG00000022629. [Q9QXL2-2]
DR GeneID; 16564; -.
DR KEGG; mmu:16564; -.
DR UCSC; uc007xhs.3; mouse. [Q9QXL2-1]
DR UCSC; uc007xht.3; mouse. [Q9QXL2-2]
DR UCSC; uc007xhv.3; mouse. [Q9QXL2-3]
DR CTD; 55605; -.
DR MGI; MGI:109188; Kif21a.
DR VEuPathDB; HostDB:ENSMUSG00000022629; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000155323; -.
DR HOGENOM; CLU_001485_4_5_1; -.
DR InParanoid; Q9QXL2; -.
DR OrthoDB; 390391at2759; -.
DR PhylomeDB; Q9QXL2; -.
DR TreeFam; TF105224; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16564; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Kif21a; mouse.
DR PRO; PR:Q9QXL2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9QXL2; protein.
DR Bgee; ENSMUSG00000022629; Expressed in habenula and 243 other tissues.
DR ExpressionAtlas; Q9QXL2; baseline and differential.
DR Genevisible; Q9QXL2; MM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0071532; F:ankyrin repeat binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..1672
FT /note="Kinesin-like protein KIF21A"
FT /id="PRO_0000125463"
FT DOMAIN 9..371
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 1343..1380
FT /note="WD 1"
FT REPEAT 1383..1421
FT /note="WD 2"
FT REPEAT 1447..1485
FT /note="WD 3"
FT REPEAT 1488..1530
FT /note="WD 4"
FT REPEAT 1539..1576
FT /note="WD 5"
FT REPEAT 1580..1619
FT /note="WD 6"
FT REPEAT 1622..1659
FT /note="WD 7"
FT REGION 556..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1169
FT /note="Interaction with KANK1 and KANK2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT REGION 1172..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..840
FT /evidence="ECO:0000255"
FT COILED 933..1021
FT /evidence="ECO:0000255"
FT COILED 1055..1085
FT /evidence="ECO:0000255"
FT COMPBIAS 558..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..637
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT MOD_RES 1227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT MOD_RES 1660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1662
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4S6"
FT MOD_RES 1671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 558..570
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10225949,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010873"
FT VAR_SEQ 1109..1115
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10225949"
FT /id="VSP_010874"
FT VAR_SEQ 1226..1305
FT /note="ISRQSSLSEKKVPEPSPVTRRKAYEKADKPKAKEHKHSDSGASETSLSPPSS
FT PPSRPRNELNVFNRLTVPQGTPSVQQDK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10225949"
FT /id="VSP_010875"
FT VAR_SEQ 1227..1318
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010876"
FT VAR_SEQ 1262..1318
FT /note="HSDSGASETSLSPPSSPPSRPRNELNVFNRLTVPQGTPSVQQDKSDESDSSL
FT SEVHR -> Q (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010877"
FT CONFLICT 1127
FT /note="P -> A (in Ref. 1; AAF17083)"
FT /evidence="ECO:0000305"
FT CONFLICT 1311
FT /note="S -> F (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1321
FT /note="I -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 1155..1157
FT /evidence="ECO:0007829|PDB:5YAY"
FT HELIX 1162..1166
FT /evidence="ECO:0007829|PDB:5YAY"
FT MOD_RES Q9QXL2-2:1101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QXL2-2:1102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QXL2-2:1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1672 AA; 186536 MW; 1B2480E5129105AB CRC64;
MLGAADESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
QEQIYTQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIMEEE QGIISRAVRH
LFKSIDEKKT SAIKNGLPPP EFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIRIHED
STGGIYTVGV TTRTVNTEPE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC
PQTDAENATD NKLISESSPM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
MFHENAMLQT ENNNLRVRIK AMQETVDALR ARITQLVSEQ ANQVLARAGE GNEEISNMIH
SYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARSPYFSAS SAFSPTILSS DKETIEIIDL
AKKDLEKLKR KEKKKKKRLQ KLEESGREER SVAGKDDNAD TDQEKKEEKG VSEKENNELD
VEENQEVSDH EDEEEEEEDE EEEDDIEGEE SSDESDSESD EKANYQADLA NITCEIAIKQ
KLIDELENSQ KRLQTLKKQY EEKLMMLQHK IRDTQLERDQ VLQNLGSVES YSEEKAKKVK
CEYEKKLHAM NKELQRLQTA QKEHARLLKN QSQYEKQLKK LQQDVMEMKK TKVRLMKQMK
EEQEKARLTE SRRNREIAQL KKDQRKRDHQ LRLLEAQKRN QEVVLRRKTE EVTALRRQVR
PMSDKVAGKV TRKLSSSESP APDTGSSAAS GEADTSRPGT QQKMRIPVAR VQALPTPTTN
GTRKKYQRKG FTGRVFTSKT ARMKWQLLER RVTDIIMQKM TISNMEADMN RLLRQREELT
KRREKLSKRR EKIVKESGEG DKSVANIIEE MESLTANIDY INDSIADCQA NIMQMEEAKE
EGETLDVTAV INACTLTEAR YLLDHFLSMG INKGLQAAQK EAQIKVLEGR LKQTEITSAT
QNQLLFHMLK EKAELNPELD ALLGHALQDL DGAPPENEED SSEEDGPLHS PGSEGSTLSS
DLMKLCGEVK PKNKARRRTT TQMELLYADS SEVASDTSAG DASLSGPLAP VAEGQEIGMN
TETSGTSARD KELLAPSGLP SKIGSISRQS SLSEKKVPEP SPVTRRKAYE KADKPKAKEH
KHSDSGASET SLSPPSSPPS RPRNELNVFN RLTVPQGTPS VQQDKSDESD SSLSEVHRGI
INPFPACKGV RASPLQCVHI AEGHTKAVLC VDSTDDLLFT GSKDRTCKVW NLVTGQEIMS
LGVHPNNVVS VKYCNYTSLV FTVSTSYIKV WDIRESAKCI RTLTSSGQVT LGEACSASTS
RTVAIPSGES QINQIALNPT GTFLYAASGN AVRMWDLKRF QSTGKLTGHL GPVMCLTVDQ
ISNGQDLIIT GSKDHYIKMF DVTEGALGTV SPTHNFEPPH YDGIEALAIQ GDNLFSGSRD
NGIKKWDLAQ KGLLQQVPNA HKDWVCALGL VPGHPVLLSG CRGGILKLWN VDTFVPVGEM
RGHDSPINAI CVNSTHVFTA ADDRTVRIWK AHNLQDGQLS DTGDLGEDIA SN
