DYH7_RAT
ID DYH7_RAT Reviewed; 4057 AA.
AC Q63170; Q62821;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dynein axonemal heavy chain 7;
DE AltName: Full=Axonemal beta dynein heavy chain 7;
DE AltName: Full=Axonemal dynein heavy chain b;
DE AltName: Full=Ciliary dynein heavy chain 7;
DE AltName: Full=Dynein-like protein 7;
GN Name=Dnah7; Synonyms=Axob, Dlp7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1369-1529, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7657712; DOI=10.1242/jcs.108.5.1883;
RA Tanaka Y., Zhang Z., Hirokawa N.;
RT "Identification and molecular evolution of new dynein-like protein
RT sequences in rat brain.";
RL J. Cell Sci. 108:1883-1893(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1372-1459, AND INDUCTION.
RC TISSUE=Trachea;
RX PubMed=8741840; DOI=10.1091/mbc.7.1.71;
RA Andrews K.L., Nettesheim P., Asai D.J., Ostrowski L.E.;
RT "Identification of seven rat axonemal dynein heavy chain genes: expression
RT during ciliated cell differentiation.";
RL Mol. Biol. Cell 7:71-79(1996).
CC -!- FUNCTION: Force generating protein of respiratory cilia. Produces force
CC towards the minus ends of microtubules. Dynein has ATPase activity; the
CC force-producing power stroke is thought to occur on release of ADP (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The dynein complex consists of at least two heavy chains and a
CC number of intermediate and light chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:7657712}.
CC -!- INDUCTION: Up-regulated during ciliogenesis.
CC {ECO:0000269|PubMed:8741840}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; AABR03068169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03068266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03068762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03068958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03068975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03069173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03069339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03069471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03070154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03072256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D26498; BAA05506.1; -; mRNA.
DR EMBL; U32180; AAC52363.1; -; mRNA.
DR PIR; I70177; I70177.
DR SMR; Q63170; -.
DR STRING; 10116.ENSRNOP00000016465; -.
DR CarbonylDB; Q63170; -.
DR PaxDb; Q63170; -.
DR PRIDE; Q63170; -.
DR UCSC; RGD:621798; rat.
DR RGD; 621798; Dnah7.
DR eggNOG; KOG3595; Eukaryota.
DR InParanoid; Q63170; -.
DR PhylomeDB; Q63170; -.
DR PRO; PR:Q63170; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0036156; C:inner dynein arm; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0003341; P:cilium movement; ISO:RGD.
DR GO; GO:0036159; P:inner dynein arm assembly; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; 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; 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; IPR042228; Dynein_linker_3.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF12774; AAA_6; 1.
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; 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; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Dynein; Microtubule; Motor protein; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..4057
FT /note="Dynein axonemal heavy chain 7"
FT /id="PRO_0000317667"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1544
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1604..1835
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 1971..2222
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2335..2588
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2605..2906
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 2987..3217
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3430..3653
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 716..779
FT /evidence="ECO:0000255"
FT COILED 2602..2646
FT /evidence="ECO:0000255"
FT COILED 2860..2916
FT /evidence="ECO:0000255"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1361..1368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1642..1649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2009..2016
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2374..2381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 1449..1451
FT /note="TEL -> NRT (in Ref. 2; BAA05506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4057 AA; 464557 MW; ECFA19724BABCFD4 CRC64;
MSSEQVRAGS PGSRVPGARR TGAVWTAPSE NLDSSTIPAL CVSLLFPSQP LDVVVTMGHN
TLGMRQLWKL ALQRPQLLSG STGVKPQWQQ TAPSFHLNVK QENPIEPYNV KNEQSYAEYM
EHFGKKGKLL DQIDDTRSAP STSRSKVKSP HKERENFRST LVNVIMQQDS SLEPDVTDES
GIPKATTSAI EKDILRYYYY IHHGIDTDNV APMEDSWLEH VLQLVPQHLK VLTNSITVLS
DEMREDYLLS VKKSIVDFVL KDPREKEDDT KITELPPHRA EMEVLPKPWR RSFLSACSYI
RDHLNAMNPT MLAVLDLWHS TFKKLRLVDI EEFHNRQDAL ELSGFQNIVI KHMESAKETL
LKTWFPEVQN IYYQGNKKKQ LPTGDSSAKL ESFFNCAATL MTLQLQDLIL VSMQDFTDLI
AQPPESIRAF EHPGFIMRLV LDKKAVKFEP EFTDYIDILV NVYEIMIKAV SFVPRVETKL
YSKWESKSKP TTLKPIILDE IIDAHKEKIR EVVLRESVAP TEHLKMYDKY QFLITRQAEQ
DIEEFLTQSQ NYERLIEEIR KYQKLGEEIQ YTSRKTVRLG MFEMHCEELI RSLVKRADII
CGKLIAKMFR DHQEVNTMLC EEFEKIAEKA LSTPPNTAEL MEMKAHIQKV ETTDMLDLGQ
RLVDSKNCLA FLIECVNFSP ADIRLNNSVF QWYGRMGEIF DEHRKIIKDK TEQYQEGLKL
RCERFVEELE SYAKQAEEFY TFGDLQDVQR YLKKAQVLNS KLDAAADKIE QFNAEEEAFG
WIPSVYPQRK KIQDGLNPYL RLYETAVEFS TKHRAWTEGP YHKVNPDQVE ADVGNYWRGL
YKLEKAFHDS PNALAMTKKV RARVEDFKQY IPLVQVICNP GLRPRHWEAM SAIVGYPLQP
SDDSTVFSFI DMNLEPFLDR FEGISEAASK EYSLEKSMDK MMTEWEAMEF VIHPYRESGT
FILSAVDDIQ MLLDDHIIKT QTMRGSPFIK PYEKQMREWE GKLLLLQEIL DEWLKVQATW
LYLEPIFSSP DIMSQMPEEG RRFTAVDKTW RDVMKMVVQN KHVLAVVTIE RMLERMKKSN
ELLELILKGL NEYLEKKRLF FPRFFFLSND ELLEILSETK DPTRVQPHLK KCFEGIARVE
FTETLDITHM KSSEGEVVEL VDTISTTKAR GQVEKWLVEL ERIMIKSIHK VIGDAITAYT
KNARINWVRD WPGQTVLCVS QTFWTVEVQV AIPMGHKALE DYLGKCNHQI DDIVTLVRGK
LSKQNRVTLG ALVVLDVHAR DVLANLVKKR ISDDTDFEWL SQLRYYWHEN NLETKMINAG
LRYGYEYLGN SPRMVLAPFC DYCFLTLFGA LHLHLGGAPE GPAGTGKTET TKDLAKAVAK
QCVVFNCSDG LDYLALGKFF KGLLSCGAWA CFDEFNRIDL EVLSVVAQQI LTIQIGINSG
TELLVFEGTE LKLDPTCAVF ITMNPGYAGR SELPDNLKAL FRTVAMMVPD YAMIAEIVLY
SCGFVTARPL SIKIVATYRL CSEQLSSQHH YDYGMRAVKS VLTAAGNLKL KYPNENEEIL
LLRSIIDVNL PKFLSHDLPL FEGITSDLFP GVKLPKPDYN DLLAAIRENC HSMNLQMTNF
FSEKILQIYE MMIVRHGFMI VGEPFGGKTS AYRVLAGALG DICEKGLMEE NKVQITVLNP
KSVTMGQLYG QFDLVSHEWS DGILAVSFRA FAASSTPDRK WLIFDGPVDA VWIENMNTVL
DDNKKLCLMS GEIIQMSPQM NLIFEPMDLE VASPATVSRC GMIYMEPQML GWRPLMVSWI
NTLPQSVSII QKEFIEGLFD RMVPLSVEFI RRHTKELSPT SDTNLVRSLM NLIDCFMDDF
ADENKQKERN DRENFSLLEG IFLFSLIWSV GASCTADDRI KYNKILRELM EGPISDLTRN
KFKLLSGTEQ TSSKALTVPF PEKGTIYDYQ FIPEGLGRWD QWIKKLADTP PIPKDVQFNE
IIVPTLDTVR YSALMSLLTT HQKPSIFVGP TGTGKSVYII NFLLNQLNKD IYKPLIVNFS
AQTTAAQTQN IIMSKLDKRR KGVFGPPLGK RMIVFVDDVN MPAREVYGAQ PPIELLRQWL
DHWNWYDLKD CSMIKLVDIQ IMCAMGPPGG GRNPITPRYM RHFNIITINE FSDKSMFTIF
SRILTWHLRT CYKFPDDFLD LTTQIVNGTM TLYKDAMKNL LPTPAKSHYL FNLRDFSRVI
QGVCLSRPET AENKEAIKRL WVHEVLRVYY DRLLDNADRS WLVNYIQEIL RNYMQEDFHD
LFKNLDFDND GIVEEDDLRS LMFCDFHDPK REDFGYREIP NVDALRVIVE GHLDEYNNMS
KKPMNLVLFR FAIEHISRIS RILKQPRSHA LLVGVGGSGR QSVTRLAAHM ADYSLFQVEI
SKGYGSHEWH EDLKVILRKC AEGDMQGVFL FTDTQIKRES FLEDVNNLLN AGEVPNLFAL
DEKQEICEKM RQLDRQRDKT KQTDGSPIAL FNMFIDRCRN QLHVVLAMSP IGDAFRIRLR
KFPALVNCCT IDWFQSWPED ALEAVASRFL EDIEMSEEIR EGCIDMCKSF HTSTINLSTT
FHNELQRYNY VTPTSYLELI STFKLLLEKK RNEVMKMKRR YEVGLDKLDS ASSQVATMQG
ELEALHPQLK VASRQVDDMM IMIEKESIEV AKTEKIVKAD ETVANDQAMA AKAIKDECDA
DLAEALPILE SALAALDTLT AQDITVVKSM KSPPAGVKLV MEAICILKGI KADKIPDPTG
SGKKIEDFWG PAKRLLGDIR FLQSLHEYDK DNIPPAYMNI IRKSYIPNPD FVPEKIRNAS
TAAEGLCKWV IAMDSYDKVA KIVAPKKIKL AAAEGELRIA MEGLRKKQAA LREVQDKLAK
LQDTLELNKQ KKADLENQVD LCSKKLERAE QLIGGLGGEK TRWSNSALEL GHLYVNLTGD
ILISSGVVAY LGAFTSNYRQ HQTKEWSHSC KERDIPCSDD YSLMGTLGEA VTIRAWNIAG
LPSDLFSIDN GIIIMNARRW PLMIDPQGQA NKWIKNMEKT NSLQLIKLSD PDYVRTLENC
IQFGTPVLLE NVGEELDPIL EPLLLKQTFK QGGSTCIRLG DSTIEYAPDF RFYITTKLRN
PHYLPETSVK VTLLNFMITP EGMQDQLLGI VVARERPDLE EEKQALILQG AENKRQLKEI
EDKILEVLSS SEGNILEDET AIKILSSSKA LANEISQKQE VAEETEKKID NTRMGYRPIA
VHSSILFFSI ADLANIEPMY QYSLTWFINL FILSIENSEK SDILSQRLHI LRDHFTYSLY
VNICRSLFEK DKMLFSFCLT VNLLIHENAI NKAEWRFLLT GGIGLDNPYT NPCTWLPQKS
WDEICRLDEL HAFKTIRREF MRLKEGWKKV YDSMEPHHEI FPEEWENKAN DFQRMLIIRC
LRPDKVIPML QEFIIKKLGR SFIEPPPFDL AKAFGDSNCC APLIFVLSPG ADPMNALLKF
ADDQGYGGSK LSSLSLGQGQ GPIAMKMLEK AVKDGTWVVL QNCHLATSWM PTLEKVCEEL
SPESTHPDFR IWLTSYPSPN FPVSVLQNGV KMTNEAPKGL RANIIRSYLM DPISDPEFFG
SCRKPEEFKK LLYGLCFFHA LVQERRKFGP LGWNIPYEFN ETDLRISVQQ LHMFLNQYEE
LPYDALRYMT GECNYGGRVT DDWDRRTLRS ILNKFFCTEL VENPQYKFDS SGIYFVPPSG
DHKSYIEYTK TLPLIPDPEI FGMNANADIT KDQSETQLLF DNILLTQSRS SGSGAKSSDE
VVNEVAGDIL GKLPNNFDIE SAMRRYPTTY TQSMNTVLVQ EMGRFNKLLI TIRESCINIQ
KAIKGLVVMS TELEEVVSSI LNVKIPGMWM GKSYPSLKPL GSYVNDFLAR LKFLQQWYEV
GPPPVFWLSG FFFTQAFLTG AQQNYARKFT IPIDLLGFDY EVMDDKEYKN APEDGVYIHG
LFLDGASWNR KTKKLAESHP KVLYDTVPVM WLKPCKKSDI PKRPSYVAPL YKTSERRGTL
STTGHSTNFV IAMILPSDQP KEHWIGRGVA LLCQLNS