KTNB1_MOUSE
ID KTNB1_MOUSE Reviewed; 658 AA.
AC Q8BG40; Q8CD18; Q8R1J0; Q9CWV2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 {ECO:0000255|HAMAP-Rule:MF_03022};
DE Short=Katanin p80 subunit B1 {ECO:0000255|HAMAP-Rule:MF_03022};
DE AltName: Full=p80 katanin {ECO:0000255|HAMAP-Rule:MF_03022};
GN Name=Katnb1;
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 MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon, Testis, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 INTERACTION WITH DYNEIN; KATNA1; NDEL1 AND PAFAH1B1.
RX PubMed=16203747; DOI=10.1093/hmg/ddi339;
RA Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T., Toyoshima Y.Y.,
RA Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M., Hiraiwa N., Yoshiki A.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting
RT protein, is essential for mitotic cell division and neuronal migration.";
RL Hum. Mol. Genet. 14:3113-3128(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 DISRUPTION PHENOTYPE.
RX PubMed=25521379; DOI=10.1016/j.neuron.2014.12.017;
RA Hu W.F., Pomp O., Ben-Omran T., Kodani A., Henke K., Mochida G.H., Yu T.W.,
RA Woodworth M.B., Bonnard C., Raj G.S., Tan T.T., Hamamy H., Masri A.,
RA Shboul M., Al Saffar M., Partlow J.N., Al-Dosari M., Alazami A.,
RA Alowain M., Alkuraya F.S., Reiter J.F., Harris M.P., Reversade B.,
RA Walsh C.A.;
RT "Katanin p80 regulates human cortical development by limiting centriole and
RT cilia number.";
RL Neuron 84:1240-1257(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 485-656 IN COMPLEX WITH KATNA1,
RP FUNCTION, INTERACTION WITH ASPM, AND MUTAGENESIS OF GLY-607; VAL-608;
RP ASP-609; ILE-610; ARG-615 AND LYS-618.
RX PubMed=28436967; DOI=10.1038/ncb3511;
RA Jiang K., Rezabkova L., Hua S., Liu Q., Capitani G., Maarten Altelaar A.F.,
RA Heck A.J.R., Kammerer R.A., Steinmetz M.O., Akhmanova A.;
RT "Microtubule minus-end regulation at spindle poles by an ASPM-katanin
RT complex.";
RL Nat. Cell Biol. 19:480-492(2017).
CC -!- FUNCTION: Participates in a complex which severs microtubules in an
CC ATP-dependent manner. May act to target the enzymatic subunit of this
CC complex to sites of action such as the centrosome. Microtubule severing
CC may promote rapid reorganization of cellular microtubule arrays and the
CC release of microtubules from the centrosome following nucleation.
CC Microtubule release from the mitotic spindle poles may allow
CC depolymerization of the microtubule end proximal to the spindle pole,
CC leading to poleward microtubule flux and poleward motion of chromosome.
CC The function in regulating microtubule dynamics at spindle poles seems
CC to depend on the association of the katanin KATNA1:KATNB1 complex with
CC ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can
CC enhance ASPM blocking activity on microtubule minus-end growth.
CC Microtubule release within the cell body of neurons may be required for
CC their transport into neuronal processes by microtubule-dependent motor
CC proteins. This transport is required for axonal growth.
CC {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28436967}.
CC -!- SUBUNIT: Interacts with KATNA1. This interaction enhances the
CC microtubule binding and severing activity of KATNA1 and also targets
CC this activity to the centrosome (PubMed:16203747). This interaction is
CC weakly competed by KATNBL1 which has a lower affinity for it (By
CC similarity). Interacts with ASPM; the katanin complex formation
CC KATNA1:KATNB1 is required for the association of ASPM
CC (PubMed:28436967). Interacts with dynein, microtubules, NDEL1 and
CC PAFAH1B1 (PubMed:16203747). Interacts with KATNAL1; this interaction is
CC weakly competed by KATNBL1 which has a lower affinity for it (By
CC similarity). Interacts with CAMSAP2 and CAMSAP3; leading to regulate
CC the length of CAMSAP-decorated microtubule stretches (By similarity).
CC {ECO:0000250|UniProtKB:Q9BVA0, ECO:0000255|HAMAP-Rule:MF_03022,
CC ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:28436967}.
CC -!- INTERACTION:
CC Q8BG40; Q9WV86: Katna1; NbExp=8; IntAct=EBI-7692933, EBI-7692898;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03022}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton
CC {ECO:0000255|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9BVA0}. Note=Predominantly cytoplasmic.
CC Localized to the interphase centrosome and mitotic spindle poles (By
CC similarity). Localizes within the cytoplasm, partially overlapping with
CC microtubules, in interphase and to the mitotic spindle and spindle
CC poles during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9BVA0,
CC ECO:0000255|HAMAP-Rule:MF_03022}.
CC -!- DISRUPTION PHENOTYPE: Homozygous loss of the gene is embryonic lethal.
CC Mutant animals have dramatically reduced body size, reduced limb bud
CC outgrowth, microphthalmia to anophthalmia and forebrain abnormalities
CC ranging from microcephaly to holoprosencephaly. Brains of mutant mice
CC have reduced cycling and proliferating radial neuroepithelial
CC progenitor cells compared to wild-type, with a more profound loss of
CC cells that depend upon asymmetrical cell divisions. These cells also
CC show evidence of increased apoptosis. {ECO:0000269|PubMed:25521379}.
CC -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03022}.
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DR EMBL; AK010364; BAB26884.1; -; mRNA.
DR EMBL; AK031630; BAC27487.1; -; mRNA.
DR EMBL; AK034103; BAC28588.1; -; mRNA.
DR EMBL; AK049345; BAC33697.1; -; mRNA.
DR EMBL; AK087973; BAC40067.1; -; mRNA.
DR EMBL; BC024500; AAH24500.1; -; mRNA.
DR EMBL; BC045200; AAH45200.1; -; mRNA.
DR CCDS; CCDS22555.1; -.
DR RefSeq; NP_083081.2; NM_028805.2.
DR RefSeq; XP_006531473.1; XM_006531410.3.
DR RefSeq; XP_006531474.1; XM_006531411.3.
DR RefSeq; XP_006531475.1; XM_006531412.1.
DR PDB; 5LB7; X-ray; 1.50 A; A=485-656, A=481-658.
DR PDB; 5NBT; X-ray; 2.40 A; A/C=481-658.
DR PDB; 5OW5; X-ray; 1.70 A; A/C=481-658.
DR PDB; 6GZC; X-ray; 2.00 A; A/C=481-658.
DR PDBsum; 5LB7; -.
DR PDBsum; 5NBT; -.
DR PDBsum; 5OW5; -.
DR PDBsum; 6GZC; -.
DR AlphaFoldDB; Q8BG40; -.
DR SMR; Q8BG40; -.
DR BioGRID; 216559; 5.
DR IntAct; Q8BG40; 2.
DR MINT; Q8BG40; -.
DR STRING; 10090.ENSMUSP00000034239; -.
DR iPTMnet; Q8BG40; -.
DR PhosphoSitePlus; Q8BG40; -.
DR EPD; Q8BG40; -.
DR MaxQB; Q8BG40; -.
DR PaxDb; Q8BG40; -.
DR PeptideAtlas; Q8BG40; -.
DR PRIDE; Q8BG40; -.
DR ProteomicsDB; 264898; -.
DR Antibodypedia; 28973; 315 antibodies from 24 providers.
DR DNASU; 74187; -.
DR Ensembl; ENSMUST00000034239; ENSMUSP00000034239; ENSMUSG00000031787.
DR GeneID; 74187; -.
DR KEGG; mmu:74187; -.
DR UCSC; uc009mxt.1; mouse.
DR CTD; 10300; -.
DR MGI; MGI:1921437; Katnb1.
DR VEuPathDB; HostDB:ENSMUSG00000031787; -.
DR eggNOG; KOG0267; Eukaryota.
DR GeneTree; ENSGT00940000157918; -.
DR HOGENOM; CLU_007811_0_0_1; -.
DR InParanoid; Q8BG40; -.
DR OMA; AMDVQCP; -.
DR OrthoDB; 425951at2759; -.
DR PhylomeDB; Q8BG40; -.
DR TreeFam; TF332359; -.
DR BRENDA; 5.6.1.1; 3474.
DR BioGRID-ORCS; 74187; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Katnb1; mouse.
DR PRO; PR:Q8BG40; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BG40; protein.
DR Bgee; ENSMUSG00000031787; Expressed in seminiferous tubule of testis and 232 other tissues.
DR ExpressionAtlas; Q8BG40; baseline and differential.
DR Genevisible; Q8BG40; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0008352; C:katanin complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0060590; F:ATPase regulator activity; ISO:MGI.
DR GO; GO:0070840; F:dynein complex binding; IDA:MGI.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0051013; P:microtubule severing; ISO:MGI.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IEA:UniProtKB-UniRule.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 2.
DR HAMAP; MF_03022; Katanin_p80_B1; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR028021; Katanin_C-terminal.
DR InterPro; IPR026962; KTNB1.
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 Pfam; PF13925; Katanin_con80; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..658
FT /note="Katanin p80 WD40 repeat-containing subunit B1"
FT /id="PRO_0000051050"
FT REPEAT 18..58
FT /note="WD 1"
FT REPEAT 61..100
FT /note="WD 2"
FT REPEAT 103..142
FT /note="WD 3"
FT REPEAT 145..184
FT /note="WD 4"
FT REPEAT 187..226
FT /note="WD 5"
FT REPEAT 229..269
FT /note="WD 6"
FT REGION 1..300
FT /note="Interaction with centrosomes"
FT /evidence="ECO:0000250"
FT REGION 1..284
FT /note="Interaction with dynein"
FT REGION 285..437
FT /note="Interaction with PAFAH1B1"
FT /evidence="ECO:0000269|PubMed:16203747"
FT REGION 311..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..658
FT /note="Interaction with KATNA1 and NDEL1"
FT /evidence="ECO:0000269|PubMed:16203747"
FT COMPBIAS 311..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVA0"
FT MUTAGEN 538
FT /note="S->L: Disrupts KATNA1:KATNB1 interaction with ASPM."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 574
FT /note="Y->A: Disrupts KATNA1:KATNB1 interaction with ASPM;
FT abolishes localization to microtubules minus ends;
FT decreases ASPM localization to microtubules minus ends; no
FT enhancement of ASPM activity in blocking microtubule minus-
FT end growth."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 607
FT /note="G->A: Abolishes localization to microtubules."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 608
FT /note="V->A: Abolishes localization to microtubules."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 609
FT /note="D->A: Abolishes localization to microtubules."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 610
FT /note="I->A: Abolishes localization to microtubules."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 615
FT /note="R->A: Abolishes localization to microtubules minus
FT ends; decreases ASPM localization to microtubules minus
FT ends; no enhancement of ASPM activity in blocking
FT microtubule minus-end growth."
FT /evidence="ECO:0000269|PubMed:28436967"
FT MUTAGEN 618
FT /note="K->A: Abolishes localization to microtubules."
FT /evidence="ECO:0000269|PubMed:28436967"
FT CONFLICT 455
FT /note="P -> H (in Ref. 1; BAC27487)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="Missing (in Ref. 1; BAB26884)"
FT /evidence="ECO:0000305"
FT HELIX 487..495
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 498..519
FT /evidence="ECO:0007829|PDB:5LB7"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 537..547
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 556..569
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 575..600
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 612..637
FT /evidence="ECO:0007829|PDB:5LB7"
FT HELIX 644..653
FT /evidence="ECO:0007829|PDB:5LB7"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:5OW5"
SQ SEQUENCE 658 AA; 72639 MW; CB04B82DA34A19EF CRC64;
MATPVVTKTA WKLQEIVAHA SNVSSLVLGK ASGRLLATGG DDCRVNLWSI NKPNCIMSLT
GHTSPVESVR LNTPEELIVA GSQSGSIRVW DLEAAKILRT LMGHKANICS LDFHPYGEFV
ASGSQDTNIK LWDIRRKGCV FRYRGHSQAV RCLRFSPDGK WLASAADDHT VKLWDLTAGK
MMSEFPGHTG PVNVVEFHPN EYLLASGSSD RTIRFWDLEK FQVVSCIEGE PGPVRSVLFN
PDGCCLYSGC QDSLRVYGWE PERCFDVVLV NWGKVADLAI CNDQLIGVAF SQSNVSSYVV
DLTRVTRTGT VTQDPVQANQ PLTQQTPNPG VSLRRIYERP STTCSKPQRV KHNSESERRS
PSSEDDRDER ESRAEIQNAE DYNEIFQPKN SISRTPPRRS EPFPAPPEDD AATVKEVSKP
SPAMDVQLPQ LPVPNLEVPA RPSVMTSTPA PKGEPDIIPA TRNEPIGLKA SDFLPAVKVP
QQAELVDEDA MSQIRKGHDT MFVVLTSRHK NLDTVRAVWT TGDIKTSVDS AVAINDLSVV
VDLLNIVNQK ASLWKLDLCT TVLPQIEKLL QSKYESYVQT GCTSLKLILQ RFLPLITDIL
AAPPSVGVDI SREERLHKCR LCFKQLKSIS GLVKSKSGLS GRHGSAFREL HLLMASLD
