CKAP5_MOUSE
ID CKAP5_MOUSE Reviewed; 2032 AA.
AC A2AGT5; A0PJ77; A2AGT6; B2RRC4; Q0VGR0; Q3TML9; Q3UDY6; Q4VAE7; Q9CUN0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytoskeleton-associated protein 5;
GN Name=Ckap5 {ECO:0000312|MGI:MGI:1923036};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH89032.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH89032.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAH89032.1}, and
RC Retina {ECO:0000312|EMBL:AAH17140.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAB29779.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-980 (ISOFORMS 1/2/3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB29779.1};
RC TISSUE=Bone marrow macrophage {ECO:0000312|EMBL:BAE29125.1},
RC Lung {ECO:0000312|EMBL:BAE38422.1}, and
RC Testis {ECO:0000312|EMBL:BAB29779.1};
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861, AND IDENTIFICATION BY
RP 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 [5]
RP INTERACTION WITH SLAIN1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M.,
RA Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O.,
RA Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC microtubule dynamics and microtubule organization. Acts as processive
CC microtubule polymerase. Promotes cytoplasmic microtubule nucleation and
CC elongation. Plays a major role in organizing spindle poles. In spindle
CC formation protects kinetochore microtubules from depolymerization by
CC KIF2C and has an essential role in centrosomal microtubule assembly
CC independently of KIF2C activity. Contributes to centrosome integrity.
CC Acts as component of the TACC3/ch-TOG/clathrin complex proposed to
CC contribute to stabilization of kinetochore fibers of the mitotic
CC spindle by acting as inter-microtubule bridge. The TACC3/ch-
CC TOG/clathrin complex is required for the maintenance of kinetochore
CC fiber tension. Enhances the strength of NDC80 complex-mediated
CC kinetochore-tip microtubule attachments.
CC {ECO:0000250|UniProtKB:Q14008}.
CC -!- SUBUNIT: Interacts with TACC1. Interacts with HNRNPA2B1. Interacts with
CC TACC3 independently of clathrin. Interacts with TACC3 and clathrin
CC forming the TACC3/ch-TOG/clathrin complex located at spindle inter-
CC microtubules bridges. Interacts with NDC80; indicative for an
CC association with the NDC80 complex. Interacts with SLAIN2 (By
CC similarity). Interacts with SLAIN1 (PubMed:21646404).
CC {ECO:0000250|UniProtKB:Q14008, ECO:0000269|PubMed:21646404}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q14008}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q14008}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14008}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q14008}. Note=Detected
CC on centrosomes and kinetochores during interphase and mitosis
CC independently from TACC3 and clathrin. Located to spindle poles and
CC microtubules during mitosis. In complex with TACC3 localized to
CC microtubule plus-ends in mitosis and interphase. In complex with TACC3
CC and clathrin localized to inter-microtubule bridges in mitotic
CC spindles. Accumulation sites at microtubule plus ends protruded
CC approximately 100 nm from MAPRE1/EB1 sites in interphase cells.
CC {ECO:0000250|UniProtKB:Q14008}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=A2AGT5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AGT5-2; Sequence=VSP_053003;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=A2AGT5-3; Sequence=VSP_053004;
CC -!- DOMAIN: The TOG (tumor overexpressed gene) domains are arranged in a N-
CC terminal pentameric array with each domain composed of six (for the
CC most part non-canonical) HEAT repeats forming a oblong paddle-like
CC structure. Intra-HEAT loops are positioned along a face of the TOG
CC domain and bind to a single alpha/beta-tubulin heterodimer. The TOG
CC domains in the array seem to be structurally and functionally
CC polarized. Differential functions may range from microtubule (MT)
CC lattice binding and/or free tubulin heterodimer binding to potentiating
CC stable incorporation of tubulin into the MT lattice.
CC {ECO:0000250|UniProtKB:Q14008}.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17140.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AL691489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017140; AAH17140.1; ALT_SEQ; mRNA.
DR EMBL; BC089032; AAH89032.1; -; mRNA.
DR EMBL; BC096422; AAH96422.1; -; mRNA.
DR EMBL; BC138334; AAI38335.1; -; mRNA.
DR EMBL; AK015282; BAB29779.1; -; mRNA.
DR EMBL; AK149854; BAE29125.1; -; mRNA.
DR EMBL; AK165862; BAE38422.1; -; mRNA.
DR CCDS; CCDS16433.1; -. [A2AGT5-3]
DR CCDS; CCDS50640.1; -. [A2AGT5-1]
DR RefSeq; NP_083713.2; NM_029437.2.
DR AlphaFoldDB; A2AGT5; -.
DR BioGRID; 217741; 56.
DR IntAct; A2AGT5; 33.
DR MINT; A2AGT5; -.
DR STRING; 10090.ENSMUSP00000106970; -.
DR iPTMnet; A2AGT5; -.
DR PhosphoSitePlus; A2AGT5; -.
DR SwissPalm; A2AGT5; -.
DR EPD; A2AGT5; -.
DR jPOST; A2AGT5; -.
DR MaxQB; A2AGT5; -.
DR PaxDb; A2AGT5; -.
DR PeptideAtlas; A2AGT5; -.
DR PRIDE; A2AGT5; -.
DR ProteomicsDB; 283624; -. [A2AGT5-1]
DR ProteomicsDB; 283625; -. [A2AGT5-2]
DR ProteomicsDB; 283626; -. [A2AGT5-3]
DR DNASU; 75786; -.
DR GeneID; 75786; -.
DR KEGG; mmu:75786; -.
DR UCSC; uc008kwd.1; mouse. [A2AGT5-3]
DR CTD; 9793; -.
DR MGI; MGI:1923036; Ckap5.
DR eggNOG; KOG1820; Eukaryota.
DR InParanoid; A2AGT5; -.
DR OrthoDB; 33681at2759; -.
DR PhylomeDB; A2AGT5; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 75786; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Ckap5; mouse.
DR PRO; PR:A2AGT5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A2AGT5; protein.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0035371; C:microtubule plus-end; ISO:MGI.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0061863; F:microtubule plus end polymerase; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032289; P:central nervous system myelin formation; IMP:MGI.
DR GO; GO:0007098; P:centrosome cycle; ISO:MGI.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:MGI.
DR GO; GO:0097062; P:dendritic spine maintenance; IMP:MGI.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; ISO:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0046959; P:habituation; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; IMP:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:MGI.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; ISO:MGI.
DR GO; GO:0022618; P:ribonucleoprotein complex assembly; IDA:MGI.
DR GO; GO:0050658; P:RNA transport; ISS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; ISO:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR PANTHER; PTHR12609; PTHR12609; 1.
DR Pfam; PF12348; CLASP_N; 3.
DR SMART; SM01349; TOG; 5.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2032
FT /note="Cytoskeleton-associated protein 5"
FT /id="PRO_0000364005"
FT REPEAT 159..197
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 356..394
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 434..472
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 750..788
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 855..893
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 936..974
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1013..1051
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1284..1322
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 1324..1357
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1361..1399
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REGION 1..223
FT /note="TOG 1"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT REGION 268..502
FT /note="TOG 2"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT REGION 501..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..817
FT /note="TOG 3"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT REGION 811..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..1081
FT /note="TOG 4"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT REGION 1078..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1428
FT /note="TOG 5"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT REGION 1420..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..1957
FT /note="Interaction with TACC3"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT REGION 1948..2032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1897..1926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..1997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1998..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14008"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1564..1623
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053003"
FT VAR_SEQ 1903..1923
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053004"
FT CONFLICT 5
FT /note="S -> C (in Ref. 3; BAE38422)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="K -> N (in Ref. 3; BAB29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="E -> K (in Ref. 3; BAB29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="E -> G (in Ref. 3; BAE38422)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="K -> R (in Ref. 3; BAB29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="A -> T (in Ref. 3; BAB29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="E -> Q (in Ref. 3; BAB29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="S -> F (in Ref. 3; BAB29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="A -> G (in Ref. 3; BAB29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="E -> V (in Ref. 3; BAE29125)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="E -> A (in Ref. 2; AAH89032)"
FT /evidence="ECO:0000305"
FT CONFLICT 1028
FT /note="K -> E (in Ref. 2; AAH89032/AAH96422/AAI38335)"
FT /evidence="ECO:0000305"
FT CONFLICT 1717
FT /note="V -> F (in Ref. 2; AAH96422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2032 AA; 225635 MW; 28FD8628C6F678CB CRC64;
MGDDSEWLKL PVDQKCEHKL WKARLSGYEE ALKIFQKIKD EKSPEWSKYL GLIKKFVTDS
NAVVQLKGLE AALVYVENAH VAGKTTGEVV SGVVSKVFNQ PKAKAKELGI EICLMYVEIE
KGESVQEELL KGLDNKNPKI IVACIETLRK ALSEFGSKII SLKPIIKVLP KLFESRDKAV
RDEAKLFAIE IYRWNRDAVK HTLQNINSVQ LKELEEEWVK LPTGAPKPSR FLRSQQELEA
KLEQQQSAGG DAEGGGDDGD EVPQVDAYEL LDAVEILSKL PKDFYDKIEA KKWQERKEAL
EAVEVLVKNP KLEAGDYADL VKALKKVVGK DTNVMLVALA AKCLTGLAVG LRKKFGQYAG
HVVPTILEKF KEKKPQVVQA LQEAIDAIFL TTTLQNISED VLAVMDNKNP TIKQQTSLFI
ARSFRHCTSS TLPKSLLKPF CAALLKHIND SAPEVRDAAF EALGTALKVV GEKSVNPFLA
DVDKLKLDRI KECSEKVELV HGKKSGLATE KKESKPLPGR AAASGAAGDK DTKDVSGPKP
GPLKKTPTAK AGGPSKKGKT TAPGGSASAG TKNKKGLETK EIVEPELSIE VCEEKASAVL
PPTCIQLLDS SNWKERLACM EEFQKAVELM ERTEMPCQAL VKMLAKKPGW KETNFQVMQM
KLHIVALIAQ KGNFSKTSAQ IVLDGLVDKI GDVKCGNNAK EAMTAIAEAC MLPWTAEQVM
SMAFSQKNPK NQSETLNWLS NAIKEFGFSE LNVKAFISNV KTALAATNPA VRTSAITLLG
VMYLYVGPSL RMIFEDEKPA LLSQIDAEFQ KMQGQSPPAP TRGIAKHSTS ATDEGEDGEE
PGEGGNDVVD LLPRIEISDK ITSELVSKIG DKNWKIRKEG LDEVAGIINE AKFIQPNIGE
LPTALKGRLN DSNKILVQQT LNILQQLAVA MGANIRQHVK NLGIPVITVL GDSKNNVRAA
ALATVNAWAE QTGMKEWLEG EDLSEELKKE NPFLRQELLG WLAEKLPTLR STPTDLILCV
PHLYSCLKDR NGDVRKKAQD ALPFFMMHLG YEKMAKATGK LKPTSKDQVL AMLEKAKANM
PSKPAAPAKA MSKPMGGSAP AKTQPIPAPV EDSVSSTIEA KPDLKKAKAP GVSSKAKSVQ
GKKVPSKTTL KEDDDKSGPI FIVVPNGKEQ RMRDEKGLKV LKWNFTTPRD EYIEQLKTQM
STCVAKWLQD EMFHSDFQHH NKALAVMVDH LESEKDGVIS CLDLILKWLT LRFFDTNTSV
LMKALEYLKL LFTLLSEEEY HLTENEASSF IPYLILKVGE PKDVIRKDVR AILNRMCLVY
PASKMFPFIM EGTKSKNSKQ RAECLEELGC LIESYGMNVC QPTPGKALKE IAIHIGDRDN
AVRNAALNTI VTVYNVHGDQ VFKLIGNLSE KDMSMLEERI KRSAKRPSAA PVKQAEEKPQ
RTQNINSNAN MLRKGPAEDM SSKLNQARSL SGHPEAAQMV RREFQLDLDE IENDNGTVRC
EMPELVQHKL DDIFEPVLIP EPKIRAVSPH FDDMHSNTAS TINFIISQVA SGDINTSIQA
LTQIDEVLRQ EDKAEAMSGH IDQFLIATFM QLRLIYSTHM ADEKLDKDEI IKLYSCIIGN
MISLFQIESL AREASTGVLK DLMHGLITLM LDSRIEDLEE GQQVIRSVNL LVVKVLEKSD
QTNILSALLV LLQDSLLATA SSPKFSELVM KCLWRMVRLL PDTINSINLD RILLDIHIFM
KVFPKEKLKQ CKSEFPIRTL KTLLHTLCKL KGPKILDHLT MIDNKNESEL EAHLCRMMKH
SMDQTGSKSD KETEKGASRI DEKSSKAKVN DFLAEIFKKI GSKENTKEGL AELYEYKKKY
SDTDIEPFLK NSSQFFQSYV ERGLRVIEME RESKGRIPTS TGISPQMEVT CVPTPTSTVS
SLGNTNGEEV GPSVYLERLK ILRQRCGLDN TKQDDRPPLT SLLSKPAIPP VASSTDMLHS
KLSQLRESRE QHQHSDLDSN QTHSAGTMTS SSSTTNIDDL KKRLERIKSS RK
