KI26B_MOUSE
ID KI26B_MOUSE Reviewed; 2112 AA.
AC Q7TNC6; D5MP63; E9PXV6; Q0VB48; Q8BHX2; Q8BKH6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Kinesin-like protein KIF26B;
GN Name=Kif26b;
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], FUNCTION, INTERACTION WITH MYH10, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=20439720; DOI=10.1073/pnas.0913748107;
RA Uchiyama Y., Sakaguchi M., Terabayashi T., Inenaga T., Inoue S.,
RA Kobayashi C., Oshima N., Kiyonari H., Nakagata N., Sato Y., Sekiguchi K.,
RA Miki H., Araki E., Fujimura S., Tanaka S.S., Nishinakamura R.;
RT "Kif26b, a kinesin family gene, regulates adhesion of the embryonic kidney
RT mesenchyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9240-9245(2010).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 494-2112.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1274-2112.
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 [5]
RP PHOSPHORYLATION AT THR-1859 AND SER-1962, MUTAGENESIS OF THR-1859 AND
RP SER-1962, AND FUNCTION.
RX PubMed=22768111; DOI=10.1371/journal.pone.0039714;
RA Terabayashi T., Sakaguchi M., Shinmyozu K., Ohshima T., Johjima A.,
RA Ogura T., Miki H., Nishinakamura R.;
RT "Phosphorylation of Kif26b promotes its polyubiquitination and subsequent
RT proteasomal degradation during kidney development.";
RL PLoS ONE 7:E39714-E39714(2012).
CC -!- FUNCTION: Essential for embryonic kidney development. Plays an
CC important role in the compact adhesion between mesenchymal cells
CC adjacent to the ureteric buds, possibly by interacting with MYH10. This
CC could lead to the establishment of the basolateral integrity of the
CC mesenchyme and the polarized expression of ITGA8, which maintains the
CC GDNF expression required for further ureteric bud attraction. Although
CC it seems to lack ATPase activity it is constitutively associated with
CC microtubules. {ECO:0000269|PubMed:20439720,
CC ECO:0000269|PubMed:22768111}.
CC -!- SUBUNIT: Interacts with MYH10. {ECO:0000269|PubMed:20439720}.
CC -!- INTERACTION:
CC Q7TNC6; Q61879: Myh10; NbExp=3; IntAct=EBI-15852098, EBI-400918;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20439720}.
CC Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20439720}.
CC -!- TISSUE SPECIFICITY: In newborn kidney, specifically expressed in the
CC mesenchyme. {ECO:0000269|PubMed:20439720}.
CC -!- DEVELOPMENTAL STAGE: In the developing kidney, only present in the
CC uncommitted mesenchyme and absent from more differentiated structures
CC including renal vesicles and comma-shaped bodies. First detected in the
CC metanephric mesenchyme at 10.5 dpc. After 11.5 dpc, observed in
CC mesenchymal cells surrounding the tips of ureteric buds in the
CC metanephroi. At 11.5 dpc, also detected in limb buds and central
CC nervous system. At 14.5 dpc, strongly expressed in the nephrogenic
CC zone.
CC -!- INDUCTION: Up-regulated by SALL1. {ECO:0000269|PubMed:20439720}.
CC -!- PTM: Phosphorylation at Thr-1859 and Ser-1962 by CDKs, mainly CDK2 and
CC CDK5, enhances the interaction with NEDD4, polyubiquitination, and
CC subsequent proteasomal degradation. Phosphorylation occurs upon loss of
CC interaction with microtubules. {ECO:0000269|PubMed:22768111}.
CC -!- PTM: Polyubiquitinated by NEDD4, resulting in proteasomal degradation.
CC -!- DISRUPTION PHENOTYPE: Mutant mice die within 24 hours after birth. Most
CC mice show bilateral kidney agenesis. The development of other organs
CC seems normal. Ureteric bud attraction is impaired after 11.0 dpc. The
CC ureteric buds are attracted close to the mesenchyme but fail to invade
CC and branch into the mesenchyme and the kidney disappears by 14.5 dpc.
CC The mesenchymal cells undergo apoptotic cell death at 12.5 dpc. ITGA8
CC is reduced at the ureteric bud/mesenchyme junction and does not exhibit
CC basolateral localization. GDNF is not properly maintained in the
CC mesenchyme at 11.5 dpc. {ECO:0000269|PubMed:20439720}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIF26 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56349.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36343.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB355846; BAJ06134.1; -; mRNA.
DR EMBL; AC117695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056349; AAH56349.1; ALT_INIT; mRNA.
DR EMBL; AK076435; BAC36343.1; ALT_INIT; mRNA.
DR CCDS; CCDS48464.1; -.
DR RefSeq; NP_001155137.1; NM_001161665.1.
DR RefSeq; XP_011237124.1; XM_011238822.2.
DR AlphaFoldDB; Q7TNC6; -.
DR SMR; Q7TNC6; -.
DR BioGRID; 234614; 2.
DR DIP; DIP-59327N; -.
DR IntAct; Q7TNC6; 2.
DR STRING; 10090.ENSMUSP00000124462; -.
DR CarbonylDB; Q7TNC6; -.
DR iPTMnet; Q7TNC6; -.
DR PhosphoSitePlus; Q7TNC6; -.
DR jPOST; Q7TNC6; -.
DR MaxQB; Q7TNC6; -.
DR PaxDb; Q7TNC6; -.
DR PRIDE; Q7TNC6; -.
DR ProteomicsDB; 264755; -.
DR Antibodypedia; 34719; 97 antibodies from 23 providers.
DR DNASU; 269152; -.
DR Ensembl; ENSMUST00000161017; ENSMUSP00000124462; ENSMUSG00000026494.
DR GeneID; 269152; -.
DR KEGG; mmu:269152; -.
DR UCSC; uc007dvh.2; mouse.
DR CTD; 55083; -.
DR MGI; MGI:2447076; Kif26b.
DR VEuPathDB; HostDB:ENSMUSG00000026494; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156992; -.
DR InParanoid; Q7TNC6; -.
DR OMA; CRPTSII; -.
DR OrthoDB; 29955at2759; -.
DR PhylomeDB; Q7TNC6; -.
DR TreeFam; TF105235; -.
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; 269152; 3 hits in 70 CRISPR screens.
DR PRO; PR:Q7TNC6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q7TNC6; protein.
DR Bgee; ENSMUSG00000026494; Expressed in trigeminal ganglion and 205 other tissues.
DR ExpressionAtlas; Q7TNC6; baseline and differential.
DR Genevisible; Q7TNC6; MM.
DR GO; GO:0005737; C:cytoplasm; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0072092; P:ureteric bud invasion; IMP:MGI.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Developmental protein; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..2112
FT /note="Kinesin-like protein KIF26B"
FT /id="PRO_0000307302"
FT DOMAIN 450..801
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1899..1971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1705..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 546..553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1859
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22768111"
FT MOD_RES 1962
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22768111"
FT MUTAGEN 1859
FT /note="T->A: Reduced polyubiquitination when co-expressed
FT with NEDD4; when associated with Ala-1962."
FT /evidence="ECO:0000269|PubMed:22768111"
FT MUTAGEN 1962
FT /note="S->A: Reduced polyubiquitination when co-expressed
FT with NEDD4; when associated with Ala-1859."
FT /evidence="ECO:0000269|PubMed:22768111"
FT CONFLICT 870
FT /note="P -> L (in Ref. 3; AAH56349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1547
FT /note="H -> R (in Ref. 4; BAC36343)"
FT /evidence="ECO:0000305"
FT CONFLICT 2050
FT /note="K -> R (in Ref. 1; BAJ06134 and 3; AAH56349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2112 AA; 225511 MW; ACAC968F636DC4D6 CRC64;
MNSVAGNKER LAVSTRGKKY GVNEMCSPTK PSAPCSPESW YRKAYEESRA GSRPTPEGAG
SALGSSGTPS PGSGTSSPSS FTGSPGPASP GIGTSSPGSL GGSPGFGTGS PGSGSGGGSS
PGSDRGVWCE NCNARLVELK RQALKLLLPG PLPGKDPAFS AVIHDKLQVP NTIRKSWNDR
DNRCDICATH LNQLKQEAIQ MVLTLEQAAG SEHYDTSLGS PPPISSIPTL VGSRHMGGLQ
QPREWAFVPA PYATSTYTGL VNKHSGKPNS LGVSNGAEKK SGSPTHQAKV SLQMATSPSN
GNILNSVAIQ AHQYLDGTWS LSRTNGVTLY PYQISQLMTE TGREGLTESA LNRYNADKPA
ASSVPAPQGS CVASETSTGT SVAASFFARA AQKLNLSSKK KKHRPSTPSV AEAPLFATSF
SGILQTSPPP APPCLLRAVN KVKDTPGMGK VKVMLRICST SARDTSESSS FLKVDPRKKQ
ITLYDPLTCG GQNAFQKRSS QVPPKMFAFD AVFPQDASQA EVCAGTVAEV IQSVVNGADG
CVFCFGHAKL GKSYTMIGRD DSMQNLGIIP CAISWLFKLI NERKEKTGAR FSVRISAVEV
WGKEENLRDL LSEVATGSLQ DGQSPGVYLC EDPICGTQLQ NQSELRAPTA EKAAFFLDAA
IASRRSNQQD CDEDDHRNSH MLFTLHIYQY RMEKSGKGGM SGGRSRLHLI DLGSCVKALS
KNREGGSGLC LSLSALGNVI LALVNGSKHI PYKESKLTML LRESLGNVNC RTTMIAHISA
AASSYAETLS TIQIASRVLR MKKKKTKYTS SSSGGESSCE EGRMRRPTQL RPFHARAPVD
PEFPLAPLSS DPDYSSSSEQ SCDTVIYIGP NGTALSDKEL TDNEGPPDFV PIVPALQKTR
GDSRPGEAAE AAASKSERDC LKCNTFAELQ ERLDCIDGSE EPSKFPFEEL PIQFGPEQAG
RCAPLSQAVG PDTPSESEKE DNGSDNGQLT EREGTELPAS KAQRNRSPAP TVTRSSSPSP
ASPRSIPGSS SQHSTSQLTQ SPSLQSSRES LNSCGFVEGK PRPMGSPRLG IASLSKTSEY
KPPSSPSQRC KVYTQKGVLP SSAPPPSLSK DSGMVSSESL LQPDVRTPPV GMSPQVLKKS
MSAGSEGFPG TLVDGEDQEG PPADSKKEIL STTMVTVQQP LELNGEDELV FTLVEELTIS
GVLDSGRPTS IISFNSDCSV QALASGSRPV SIISSISEDL ECYSSMAPVS EVSITQFLPL
PKLGLDEKAR DAGSRRSSIS SWLSEMSAGS DGEQSCHSFI AQTCFGHGEA MAEPPASEFV
SSIQNTAVVC REKPEVGPDN LLILSEMGEE SGNKAAPIKG CKISTVGKAM VTISNTASLS
SCEGYIPMKT NITVYPCIAM SPRNVQEPES STATPKVSPK ASQAQESKEP STRREMKFED
PWLKREEEVK RENAYSSEEG VKCEPLPSSL KTEGKSEQEL DGRPSSGNRL SSSSSEAAAF
QGTDNVRRVV DGCEMALPGL VAQSPLHVNR NLKSSSLPRA FQKADRHEEL DSFYHCLADS
NGFSAASGIP SSKTTLERKV ASPKHCVLAR PKGTPPLPPV RKSSLDQKNR ASPQHGGGSS
NTSSPLNQPA TFLACFPDES NGKTKDVSSS SKLFSAKLEQ LASRSNSLGR TTVSHYECLS
LERAESLSSV SSRMHAGKDS TMPRTGRSLG RSTGASPPSC GITQSTGASP KASQSKISAV
SKLLLASPKS RSSLSTSTTK TLSFSTKSLP QSVGQSSNLP PSGKHMSWST QSLSRNRGSG
LASKLPLRAV NGRISELLQG SAGPRSAQLR AEAEERSGAP SEDKPAAAHL LPSPYSKITP
PRKPHRCSSG HGSDNSSVLS GELPPAMGKT ALFYHSGGSS GYESMMRDSE ATGSASSAQD
SMSENSSSVG GRCRSLKNQK KRSNSGSQRR RLIPALSLDT PSPVRKTASS TGVRWVDGPL
RSTQRSLGEP FEIKVYEIDD VERLQRRRGA TSKEVMCFNA KLKILEHRQQ RIAEVRAKYE
WLMKELEATK QYLMLDPNKW LREFDLEQVL QLDSLEYLEA LEGVTERLES RVNFCKAHLM
MITCFDITSR RR
