DYHC1_PLAF7
ID DYHC1_PLAF7 Reviewed; 5065 AA.
AC Q8IBG1; A0A143ZY83; C0H4Q3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dynein heavy chain-like protein 1 {ECO:0000305};
GN ORFNames=MAL7P1.162, PF3D7_0729900;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP SYNTHESIS OF 1677-1703, DEVELOPMENTAL STAGE, AND POSSIBLE CANDIDATE MALARIA
RP EPITOPE.
RX PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT "Rapid identification of malaria vaccine candidates based on alpha-helical
RT coiled coil protein motif.";
RL PLoS ONE 2:E645-E645(2007).
CC -!- FUNCTION: Acts as a motor for the intracellular retrograde motility of
CC vesicles and organelles along microtubules. Dynein has ATPase activity;
CC the force-producing power stroke is thought to occur on release of ADP
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual cell-cycle on the
CC cell surface of the host erythrocytes. {ECO:0000269|PubMed:17653272}.
CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC (which binds cargo and interacts with other dynein components), and the
CC head or motor domain. The motor contains six tandemly-linked AAA
CC domains in the head, which form a ring. A stalk-like structure (formed
CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC and terminates in a microtubule-binding site. A seventh domain may also
CC contribute to this ring; it is not clear whether the N-terminus or the
CC C-terminus forms this extra domain. There are four well-conserved and
CC two non-conserved ATPase sites, one per AAA domain. Probably only one
CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC regulatory function. {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC determined by epitope response in sera. {ECO:0000269|PubMed:17653272}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000255}.
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DR EMBL; AL844506; CZT62681.1; -; Genomic_DNA.
DR RefSeq; XP_002808800.1; XM_002808754.1.
DR SMR; Q8IBG1; -.
DR STRING; 5833.MAL7P1.162; -.
DR PRIDE; Q8IBG1; -.
DR EnsemblProtists; CZT62681; CZT62681; PF3D7_0729900.
DR VEuPathDB; PlasmoDB:PF3D7_0729900; -.
DR InParanoid; Q8IBG1; -.
DR OMA; FIMDEAN; -.
DR PhylomeDB; Q8IBG1; -.
DR Proteomes; UP000001450; Chromosome 7.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051293; P:establishment of spindle localization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; ISS:UniProtKB.
DR GO; GO:0072382; P:minus-end-directed vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 5.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR043160; Dynein_C_barrel.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676; PTHR10676; 1.
DR Pfam; PF12774; AAA_6; 2.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Merozoite;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..5065
FT /note="Dynein heavy chain-like protein 1"
FT /id="PRO_0000356828"
FT REGION 1..1957
FT /note="Stem"
FT /evidence="ECO:0000250|UniProtKB:P34036"
FT REGION 1958..2179
FT /note="AAA 1"
FT /evidence="ECO:0000250|UniProtKB:P34036"
FT REGION 2203..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2281..2632
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2507..2529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2751..3004
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 3097..3367
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3386..3701
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3754..3983
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 4289..4507
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT REGION 4686..4727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1677..1705
FT /evidence="ECO:0000255"
FT COILED 3388..3466
FT /evidence="ECO:0000255"
FT COILED 3970..3997
FT /evidence="ECO:0000255"
FT COMPBIAS 4686..4708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4709..4727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1996..2003
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2319..2326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2790..2797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 3135..3142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 5065 AA; 591698 MW; 0C548A290C5207F9 CRC64;
MELEKTHLIN YFLEICPTVL DCSRKELQSV LIKKEEEKIR KFLLDKNINL IVIGKEGNDN
VEREMDDKEN DNVDINMNEE YNSMRTSNLD NKYNNFLFVE LMINYKCVTK SISIAFMKRN
KENFLSLNDK IDNRNKINLS NELLMFVCGQ NDCNTPLDLV YLYLSQGFNN IFDAASGYGQ
NISGPDSSHF NYGTKKDVEN MFSINNKYIG YEGENKVSNI LMNNVSKKLN ELLISMKNAQ
IDLNIPIINL HVDKRIKKLL EENPNVDDMK PDKLKQLCES QEFINQLQKD VTKWIEDIQK
LTRLNGEFKS GGSALSEINF WIGYENALYQ LESQLKNPEV ILTLHILKNA KRYFATMSFD
SDIQLKQSKE YVLNVNILMK DFPIEDLLGA TSIQQIIQAV RNIFNHLKKL KNTTKYPLSR
SYNFVESLSR DLNNTMKKVL CTQSLMNMDY EEFDVLISGC VEIFRLWNEE MRIFKDMVRE
LIKKRSFNER APAKMVFEHI HLQERLDEIK KFRKQHEKFK SVISTVFGSN NKSLGINLYK
DINTAYNIFL SLDPLDLSKN GEDNWEKAKL SYESKVNRVE SQITFKLRDQ LGGSKTSAEM
FHAFSKFNPL FFRPKIRGAI QEYQNTLIQI VVDDLRKLQM IYINGYLKSD SQKVSTIRDI
PLVAGSIIWA KQIERKLEDS LKRIENVLGR GWEQHSEGKI LRQNIDNFKN LLSQNKTFEK
WLKNIKSADK FDMYDNIINI KKLGGNNYEI LANYDFQFFN IFKEVRYLQS INLRVPYSIK
VKADETKLIY PYALTLQKTF RTYMKICISM DNQAKDVPFN QTIKKLVAAI HNTVQNKIKE
GIYLHWDSDI IETYVRKLSE TINTFEFMVD EAMNKNKIVL DSLEKMKTCE VCFDCNELKS
LIEIIQKKAD ELYLEHYRNV HIWIEELNIH INKILTERLE EIIKTWTCEF VNWPNNGKRF
ICKENIHEFK IKNQKFYLHP SIDSMRQIWF SKLSDAINII CGITRIKNIY QKKEKTNEKI
QIKSKGKNTN NEKDDDYIYY TNDSNNKNNI YKNKCDDNNN NIVINDVILD NTYKYIIYFI
DKKIYDNAIK SINDMVDKAQ KYESIWLQYK TLWQIEIGDI ISSFGEDIET WKIFMNEIKQ
TENTFDTLDT EKYFGPIVID YRILQSKVSS KFEIWQKEIV SEFSKKLGEK TLYLKEEIEK
ALYDLNTQSE LKNETEITAM HILSMTPKDI VGIMNTYDMD ILSKTCNSIY NFIEKINEIN
KKEELEWSKK CDLLKQSEVL LEKQRYTFPT NWLYIDNIIG KLETVKQICK YQIKLIKDYL
PYIQSMVLDF DRKVQNNIKE LFEEWNKNKP SHGNANSTKA LQIITTFEER IDIINEQYEI
SEKIRKLLEL ENSESEIGFH VSPNILKEEI NCVKGIWDEL KIIYSNICDM KKMLWSNVDP
KDVKHRLNNL LESIKKIPAK YRQYEIFDNV QNEIQQYLKT YSLLLDLKSE SLKERHWKLI
LQKLNIKIYY NKLTLGNLWS LHLCIHENVL SEILNQAQGE MALEQFLRGL KDTWNEYELE
LVQYQNKCKL IKGWNDIFST IDDHLNAIQS MKISSYIKIF EEETFTWDDK LNRLRNLLDV
WMNVQRKWVY LEGVLKGSSD IKSLLPQEYN RFKIIDSDFI NIMKKTSDKP KLLELFQMEG
FQKQLDRLSD SLSKIQKALG EYLEKQRNKF PRFYFVGDED LLEMIGNSKD AKIIQRNVNK
MFAGINSFIL KENTNDIILG MSSREGEEVL FLEALNISSF NTLKEWLIVL EKSMKSSLEF
YLDEAAKEIL EMDMIECTKI ENNKILLWSE KYPNQIILLC LQILWTTNIE NELINFSKNP
PDESNTLFHK SEKICLNLLE FLAVNVVKQK DHRTRQKFVQ MITELVHQRD VIRILIDKNV
NNVNSFIWLQ YMRYYWDSKK KENKINLIIK MADATFEYGY EYLGMCEKLV QTELTDACFL
TLTQALKMKL GGNPFGPAGT GKTESVKALG AQLGRYVLVF NCDESFDFTA MGRIFVGLCQ
VGAWGCFDEF NRLEERILSA VSEQILTIQT SLVQRKNEIE ILNKKIGLNK NVGIFVTMNP
GYAGRSNLPD NLKQLFRSFA MIEPNKQLIV EVTLFSQGFI SAEHLSSKIV SLFDLCSEQL
SKQPHYDFGL RSLKSVLNSA GNLKRLTLLK DESKYVQNNQ IGFNETLDNN NNNDNNNERK
TTTNTNESNI ISMEQTLLLK SVCDTVYPKL VSSDIILIQS LLKGVFPNVN VGDLEEKGLI
NEIHRLCKLR HFTPEEKWIT KICQIYQIMK LQHGVMLVGD VGTGKSSAWK ILLDSLEALD
NIKGVSYVID AKSLDKEEIY GKLDNINLEW TDGVFTGILR KIIYNSSTQS GNTNKRHWIV
FDGDVDPEWA ENLNSVLDDN KLLTLPNGER LPIPESVRIL FEVDTLKHAT LATVSRCGMI
WFSRDILSPI ILFKHKLNML KYGDNDYPRK MDKFKLLLIN NNERITEKNQ NGNENGNENE
KKNINIINNN NSNNSNNIYS MNHMNNYNVN ANEHNLQQFD NIDSENIMDN IRMNSRIFFE
ENEQETSSSY IIRTIPYRAV NIISDYFEEN EFVHQCLVEA ENYEHVMDYE YIRVIESTCL
LLQKGFDNLV KKNEKINNTL SDDDIEKYIS KWLVVSILWG IGGSLNLETR EKFSMFVQSI
CSIPLPNDLL SKGKMPNMDN TNKISNTLLD YQPNIEDGEW INWKELVQII DVDRTEISDA
TLVIETMDTI RHETILEGWL HLKKPFILCG PPGSGKTMTL TSVLKKSSEF DIASLNFSSG
SLPNLLLQTF DHYCEYVKTT SELVLRPLQP GKWLIIFADE INLPTPDKYD TQRIIMFMRQ
IYESQGFWKY DVNNNSWNWV KIERITFAGA CNPPTDAGRN PLSNRFLRHT SVLYVDFPGY
ESLKQIYGTF NRAILRKFPQ SSHMADNLTQ AMVDFYTKFS ETFTIDMQPH YIYSPRELTR
WKLALYETLE SCDELKTKDL VRLCICEGLR IFQDRLIYKK EKKETDKIID DIFKYSFPDI
TKEDLLRPIL FNSYMKNYYT EIDKKDLKVL ILSKLKIFNE EEINVQLVLF DDVLDHITRI
DRVLRLPLGH LLLVGASGAG KTILSRFVSW INGLSVFQIR AGRNYTTESF EADLRHIMKR
AGIKEEKITF IFDESNVLGP AFLERMNALL ASGEVPGLFE GDNYITLINE CKSAYRSNIG
LDESDIFKKF TKQVQQNLHI VFTMNPANPD FANRQATSPA LFNRCVIDWF GDWPYSALLQ
VASEFIFNLI LPDNNFYMDY VGNEDGPIKG KIQYKNNKAY FLSRAIVEIH NSVVHINNVL
MKKGNRYNYM TPRDFLDFIK HFLKIIDEKK EEVSSQKNHL NSGLNKLKDT EIQVAELRNS
LAIKKKTLAE KDLEAEEKMK LMIEQQTETE DKKKKAEILS KKLDEQFIII DQRKEVVRKE
LSEVEPKFRE AEEAVKNIPK KNFDELRAMA NPPILVRNAV EAVAILIMNE GDKNVTWEDA
RKIMKGQDFI NKVLYLDKKA VKPQTSSQIK KRINNNDWDV ERINKASRAA GPLAKWVESV
ITFLNILETV QPLEKEIEKL QEETKVAEDQ YNEQRDIICE LEKKLVQYKN DYAQLISQVQ
NIKQEMEMVE NKIKRSINLI DNLKSEKERW SETFINLEEA SETFVGDCLI AAAFCAYIGF
FEHYERQRLK RTWGEIIKMH YIKYRNDLSF IEFLSRPSER LQWIGNELPS DDLSIENAII
INNYIRYPMI IDPSDQATTF LLNQYSDKKI LKTSFSDKNF IKNLESALRF GSTLLVYDVE
KIDAILNSVL NQETHKQGGR LLITIGDSEV DFSPSFNLFL TSRDAHFQFT PDLCSRVTFV
NFTLTPSSLQ NQCLNMILKN ERPDIDKKRC DLLKLQGEYK VKIRELEESL LLELSNVKGN
ILDDDNVIST MEKLKVQGAE ASKEVNIAEE VMVEVENVSN QYLFLAQGSA RIYFILQHLC
NINFLYQYDL NFFFNIMKDM FNNDHLLSIV KKKDHYKERL KVLEDLLFSL TYNRVARGLL
QEDRYVFGLQ LCYVKSIINP NIDMDQSYLH YLLKDHYSNQ EIDEFEHKKI EKNLLPEYND
EQINALNNLI KHKSFSNLKK CILNNKQKWI ELLHSAEPEE LVCSILNDMN MSEESMDKSD
EMLNKNKNLN ILNNVEFGKD DDIPEEKRYI NNDNTNMDTT TKNNNNMNNN NNMNNNNNYM
LQNKNDISSC LKESLIIKAI RPDKLENCFN KIINHILGRD FLWIPELSMN DFEKYVKENA
NGNIPIVLIS SPGFDPSNKV QQLSEKCKIP LFSIAMGSEE GYISAERVIF TAQSNGGWVL
LKNIHISTKW LHELEKNIHK ATTNKNFRLF LTMEFNPRIP QSLMRISLTF MFEPPVGIKF
SILRSFSLFL ENRELCEPKI ARLRLYFIVS YLHAIILERR RYTPIGWTKK YEFSDSDLMC
ALSVVDSWLD KASTKIGKNV SEHIDPCNIP WEAIKKILNE AIYGGRLDNM VDQKILDTFI
DHLMNSNSFE TDFKLNICNS TSLNKDFLVS PDLFRNINDY INWTNNMSNT DLPAWLGFGQ
QAEGLLTTRT NFSIISKWNI LYSKSRSDVY EPLPHSPLTK SLNEEKYISF EQYKIKNIKE
KTIKDKDKNK DEDKNKNKEN DDNNKKHIGN NKLVISSSER TESETSESSC TVSRSIHVYS
NNENILFINK ILENLPQNIP CLEKNEEKLR NAVFRCFERE NNLFSDLLKL IKTNLNQLKN
VLEEKVKYTN KIRALAKDLN SFNVPSNWLL DGNTTNLNLT NWLKELINRL YQIIVITLEF
NEKSCIDINE KKKQKNINIE NNEDHNLNDF YKRNNDNILS HFKLNNKEKK LSINFIWLGG
LFYPRAFITA TRQLSAFKFK NSLDDLELSV LIGNNNNMKY DDMIHFTITC LSIEGAEWSN
KDNCLILSDE LTIDLPPVTL TWEKKEILKQ KQKESSSSLH FMNLPIYLDK SRNSFIGFWN
FPVSKGISEQ IWYQRGVAIF LSKTY
