DYH12_HUMAN
ID DYH12_HUMAN Reviewed; 3092 AA.
AC Q6ZR08; A6NGI2; Q6ZTR8; Q8N7R9; Q8WXK2; Q92816;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Dynein axonemal heavy chain 12;
DE AltName: Full=Axonemal beta dynein heavy chain 12;
DE AltName: Full=Axonemal dynein heavy chain 12-like protein;
DE AltName: Full=Axonemal dynein heavy chain 7-like protein;
DE AltName: Full=Ciliary dynein heavy chain 12;
DE AltName: Full=Dynein axonemal heavy chain 7-like;
DE AltName: Full=Dynein heavy chain domain-containing protein 2;
GN Name=DNAH12;
GN Synonyms=DHC3, DLP12, DNAH12L, DNAH7L, DNAHC3, DNHD2, HDHC3, HL19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANTS
RP ALA-32 AND SER-2893.
RC TISSUE=Testis, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1116-1311 (ISOFORM 1).
RX PubMed=8666668; DOI=10.1083/jcb.133.4.831;
RA Vaisberg E.A., Grissom P.M., McIntosh J.R.;
RT "Mammalian cells express three distinct dynein heavy chains that are
RT localized to different cytoplasmic organelles.";
RL J. Cell Biol. 133:831-842(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.
CC Involved in sperm motility; implicated in sperm flagellar assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZR08-1; Sequence=Displayed;
CC Name=4;
CC IsoId=Q6ZR08-4; Sequence=VSP_039335, VSP_039336;
CC Name=2;
CC IsoId=Q6ZR08-2; Sequence=VSP_036920, VSP_036924;
CC Name=3;
CC IsoId=Q6ZR08-3; Sequence=VSP_036921, VSP_036922, VSP_036923;
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}.
CC -!- CAUTION: Was originally derived from a readthrough transcript including
CC ASB14 and DNAH12. DNHD2 was thought to be a distinct gene.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB09729.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK097746; BAC05158.1; -; mRNA.
DR EMBL; AK126276; BAC86512.1; -; mRNA.
DR EMBL; AK128592; BAC87517.1; -; mRNA.
DR EMBL; AC092418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U53532; AAB09729.1; ALT_FRAME; mRNA.
DR CCDS; CCDS33771.1; -. [Q6ZR08-4]
DR RefSeq; NP_940966.2; NM_198564.3. [Q6ZR08-4]
DR SMR; Q6ZR08; -.
DR BioGRID; 128396; 6.
DR ELM; Q6ZR08; -.
DR IntAct; Q6ZR08; 5.
DR STRING; 9606.ENSP00000312554; -.
DR iPTMnet; Q6ZR08; -.
DR PhosphoSitePlus; Q6ZR08; -.
DR BioMuta; DNAH12; -.
DR DMDM; 226693521; -.
DR EPD; Q6ZR08; -.
DR jPOST; Q6ZR08; -.
DR MassIVE; Q6ZR08; -.
DR PaxDb; Q6ZR08; -.
DR PeptideAtlas; Q6ZR08; -.
DR PRIDE; Q6ZR08; -.
DR ProteomicsDB; 68106; -. [Q6ZR08-1]
DR ProteomicsDB; 68107; -. [Q6ZR08-2]
DR ProteomicsDB; 68108; -. [Q6ZR08-3]
DR ProteomicsDB; 68109; -. [Q6ZR08-4]
DR Antibodypedia; 48520; 72 antibodies from 13 providers.
DR DNASU; 201625; -.
DR Ensembl; ENST00000311202.7; ENSP00000312554.6; ENSG00000174844.15. [Q6ZR08-4]
DR Ensembl; ENST00000351747.6; ENSP00000295937.3; ENSG00000174844.15. [Q6ZR08-1]
DR GeneID; 201625; -.
DR KEGG; hsa:201625; -.
DR UCSC; uc003dit.2; human. [Q6ZR08-1]
DR CTD; 201625; -.
DR DisGeNET; 201625; -.
DR GeneCards; DNAH12; -.
DR HGNC; HGNC:2943; DNAH12.
DR HPA; ENSG00000174844; Group enriched (brain, choroid plexus, fallopian tube, lung, testis).
DR MIM; 603340; gene.
DR neXtProt; NX_Q6ZR08; -.
DR OpenTargets; ENSG00000174844; -.
DR PharmGKB; PA27397; -.
DR VEuPathDB; HostDB:ENSG00000174844; -.
DR GeneTree; ENSGT00940000154280; -.
DR HOGENOM; CLU_000038_0_2_1; -.
DR InParanoid; Q6ZR08; -.
DR OrthoDB; 2079at2759; -.
DR PhylomeDB; Q6ZR08; -.
DR TreeFam; TF333463; -.
DR PathwayCommons; Q6ZR08; -.
DR SignaLink; Q6ZR08; -.
DR BioGRID-ORCS; 201625; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; DNAH12; human.
DR GenomeRNAi; 201625; -.
DR Pharos; Q6ZR08; Tbio.
DR PRO; PR:Q6ZR08; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6ZR08; protein.
DR Bgee; ENSG00000174844; Expressed in bronchial epithelial cell and 112 other tissues.
DR ExpressionAtlas; Q6ZR08; baseline and differential.
DR Genevisible; Q6ZR08; HS.
DR GO; GO:0005858; C:axonemal dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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; 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; 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; IPR027417; P-loop_NTPase.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 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 SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..3092
FT /note="Dynein axonemal heavy chain 12"
FT /id="PRO_0000370324"
FT REGION 1..1214
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1215..1436
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1496..1636
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 1853..2104
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2218..2660
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2661..2795
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 2874..3051
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT COILED 592..665
FT /evidence="ECO:0000255"
FT COILED 731..762
FT /evidence="ECO:0000255"
FT MOTIF 1253..1260
FT /note="GPAGTGKT motif"
FT MOTIF 1303..1309
FT /note="CFDEFNR motif"
FT BINDING 1253..1260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1534..1541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1892..1899
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2257..2264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..2367
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036920"
FT VAR_SEQ 1..1985
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036921"
FT VAR_SEQ 446..457
FT /note="FIEKFLSLASEI -> ELDCWVVWEVYF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039335"
FT VAR_SEQ 458..3092
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039336"
FT VAR_SEQ 1986..2296
FT /note="GHWYDLKDTSKITLVDIELIAAMGPPGGGRNPVTPRCIRHFNICSINSFSDE
FT TMVRIFSSIVAFYLRTHEFPPEYFVIGNQIVNGTMEIYKQSVENLLPTPTKSHYTFNLR
FT DFSRVIRGCLLIERDAVANKHTMIRLFVHEVLRVFYDRLINDDDRRWLFQLTKTVIKDH
FT FKESFHSIFSHLRKQNAPVTEEDLRNLMFGDYMNPDLEGDDRVYIEIPNIHHFSDVVDQ
FT CLDEYNQTHKTRMNLVIFRYVLEHLSRICRVLKQSGGNALLVGLGGSGRQSLTRLATSM
FT AKMHIFQPEISKSYGMNEWREDM -> MLCKKKKIPCSEEFLLSKTLGDPVKIRAWNIA
FT GLPTDTFSIDNGVIVNNCRRWPLMIDPQGQANKWIKNSERENQLSVIKLSDSDYMRTLE
FT NCIQFGTPLLLENVGEELDPSLEPLLLRQTFKQGGIDCIRLGEVIIEYSFDFKFYITTK
FT LRNPHYMPELATKVSLLNFMITPEGLEDQLLGIVVAKERPELEEERNALILQSAANKKQ
FT LKDIEKKILETLSSSEGNILEDESAIKVLDSAKMMSNEITKKQQIAEKTELKIAESREG
FT YRPIAKHSSVLFFSIADLANIDPMYQYSLTWFVNLYINSIHDS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036922"
FT VAR_SEQ 2297..2310
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036923"
FT VAR_SEQ 2641..2686
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036924"
FT VARIANT 32
FT /note="V -> A (in dbSNP:rs9311651)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_034829"
FT VARIANT 139
FT /note="S -> N (in dbSNP:rs6778837)"
FT /id="VAR_034830"
FT VARIANT 224
FT /note="D -> E (in dbSNP:rs6445902)"
FT /id="VAR_034831"
FT VARIANT 231
FT /note="T -> A (in dbSNP:rs7629743)"
FT /id="VAR_034832"
FT VARIANT 467
FT /note="T -> P (in dbSNP:rs6806444)"
FT /id="VAR_060142"
FT VARIANT 1549
FT /note="D -> N (in dbSNP:rs6773904)"
FT /id="VAR_060143"
FT VARIANT 1704
FT /note="Y -> H (in dbSNP:rs4462937)"
FT /id="VAR_060144"
FT VARIANT 1748
FT /note="R -> C (in dbSNP:rs17050836)"
FT /id="VAR_060145"
FT VARIANT 1754
FT /note="K -> N (in dbSNP:rs17793014)"
FT /id="VAR_060146"
FT VARIANT 1763
FT /note="T -> I (in dbSNP:rs4681982)"
FT /id="VAR_060147"
FT VARIANT 2740
FT /note="Y -> F (in dbSNP:rs17057989)"
FT /id="VAR_037390"
FT VARIANT 2893
FT /note="G -> S (in dbSNP:rs4060726)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037391"
FT CONFLICT 13
FT /note="K -> R (in Ref. 1; BAC86512)"
FT /evidence="ECO:0000305"
FT CONFLICT 1125
FT /note="S -> G (in Ref. 3; AAB09729)"
FT /evidence="ECO:0000305"
FT CONFLICT 1170
FT /note="H -> R (in Ref. 3; AAB09729)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310..1311
FT /note="IE -> NS (in Ref. 3; AAB09729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3092 AA; 356942 MW; C40401DD227DDCD7 CRC64;
MSDANKAAIA AEKEALNLKL PPIVHLPENI GVDTPTQSKL LKYRRSKEQQ QKINQLVIDG
AKRNLDRTLG KRTPLLPPPD YPQTMTSEMK KKGFNYIYMK QCVESSPLVP IQQEWLDHML
RLIPESLKEG KEREELLESL INEVSSDFEN SMKRYLVQSV LVKPPVKSLE DEGGPLPESP
VGLDYSNPWH SSYVQARNQI FSNLHIIHPT MKMLLDLGYT TFADTVLLDF TGIRAKGPID
CESLKTDLSI QTRNAEEKIM NTWYPKVINL FTKKEALEGV KPEKLDAFYS CVSTLMSNQL
KDLLRRTVEG FVKLFDPKDQ QRLPIFKIEL TFDDDKMEFY PTFQDLEDNV LSLVERIAEA
LQNVQTIPSW LSGTSTPVNL DTELPEHVLH WAVDTLKAAV HRNLEGARKH YETYVEKYNW
LLDGTAVENI ETFQTEDHTF DEYTEFIEKF LSLASEIMLL PQWIHYTMVR LDCEDLKTGL
TNKAKAFANI LLNDIASKYR KENECICSEF EAIKEHALKV PETTEEMMDL ISYVEKARTV
GIEELILRIQ ESKRQMSYFL DVFLFPQEDL ALNATVLMWP RKINPIFDEN DELIENAKHK
KENELMAKRE KLILEIEKES RRMEEFTEFA ELERMQQYVT DVRQLQKRIQ ESEEAVQFIN
KEEELFKWEL TKYPELDKLK VNIEPYQKFF NFVLKWQRSE KRWMDGGFLD LNGESMEADV
EEFSREIFKT LKFFQTKLKK ELQEKRKAAR KRSLEEEKIE EEPKDNATIT MCRMRARHWK
QISEIVGYDL TPDSGTTLRK VLKLNLTPYL EQFEVISAGA SKEFSLEKAM NTMIGTWEDI
AFHISLYRDT GVCILSSVDE IQAILDDQII KTQTMRGSPF IKPFEHEIKA WEDRLIRIQE
TIDEWLKVQA QWLYLEPIFC SEDIMQQMPE EGRQFQTVDR HWRDIMKFCA KDPKVLAATS
LTGLLEKLQN CNELLEKIMK GLNAYLEKKR LFFPRFFFLS NDEMLEILSE TKDPLRVQPH
LKKCFEGIAK LEFLPNLDIK AMYSSEGERV ELIALISTSA ARGAVEKWLI QVEDLMLRSV
HDVIAAARLA YPESARRDWV REWPGQVVLC ISQMFWTSET QEVISGGTEG LKKYYKELQN
QLNEIVELVR GKLSKQTRTT LGALVTIDVH ARDVVMDMIK MGVSHDTDFL WLAQLRYYWE
NENARVRIIN CNVKYAYEYL GNSPRLVITP LTDRCYRTLI GAFYLNLGGA PEGPAGTGKT
ETTKDLAKAL AVQCVVFNCS DGLDYLAMGK FFKGLASSGA WACFDEFNRI ELEVLSVVAQ
QILCIQRAIQ QKLVVFVFEG TELKLNPNCF VAITMNPGYA GRSELPDNLK VLFRTVAMMV
PNYALIAEIS LYSYGFLNAR PLSVKIVMTY RLCSEQLSSQ FHYDYGMRAV KAVLVAAGNL
KLKYPNENED ILLLRSIKDV NEPKFLSHDI PLFNGITSDL FPGIKLPEAD YHEFLECAHE
ACNVHNLQPV KFFLEKIIQT YEMMIVRHGF MLVGEPFAAK TKVLHVLADT LTLMNEHGYG
EEEKVIYRTV NPKSITMGQL FGQFDPVSHE WTDGIVANTF REFALSETPD RKWVVFDGPI
DTLWIESMNT VLDDNKKLCL MSGEIIQMSP QMSLIFETMD LSQASPATVS RCGMIYLEPS
QLGWEPLVSS WLNSLKGPLC EPEYQALLRG LFAWLIPPSL NQRVELFQLN YLYTTIVSKI
LKILITFRIS NYFKYVPLKT QCTFIKFFLH QQACFIFSLI WSIGGSCDTD GRRVFDTFIR
LIILGKDDEN PVPDSVGKWE CPFDEKGLVY DYMYELKNKG RWVHWNELIK NTNLGDKQIK
IQDIIVPTMD TIRYTFLMDL SITYAKPLLF VGPTGTGKSV YVKDKLMNHL EKDQYFPFYI
NLSARTSANQ VQNIIMARLD KRRKGVFGPP MGKKCIIFID DMNMPALEKY GAQPPIELLR
QFFDCGHWYD LKDTSKITLV DIELIAAMGP PGGGRNPVTP RCIRHFNICS INSFSDETMV
RIFSSIVAFY LRTHEFPPEY FVIGNQIVNG TMEIYKQSVE NLLPTPTKSH YTFNLRDFSR
VIRGCLLIER DAVANKHTMI RLFVHEVLRV FYDRLINDDD RRWLFQLTKT VIKDHFKESF
HSIFSHLRKQ NAPVTEEDLR NLMFGDYMNP DLEGDDRVYI EIPNIHHFSD VVDQCLDEYN
QTHKTRMNLV IFRYVLEHLS RICRVLKQSG GNALLVGLGG SGRQSLTRLA TSMAKMHIFQ
PEISKSYGMN EWREDMKSFI AVPVTNRIVD NKSKILEKRL RYLNDHFTYN LYCNICRSLF
EKDKLLFSFL LCANLLLARK EIEYQELMFL LTGGVSLKSA EKNPDPTWLQ DKSWEEICRA
SEFPAFRGLR QHFCEHIYEW REIYDSKEPH NAKFPAPMDK NLNELQKIII LRCLRPDKIT
PAITNYVTDK LGKKFVEPPP FDLTKSYLDS NCTIPLIFVL SPGADPMASL LKFANDKSMS
GNKFQAISLG QGQGPIAAKM IKAAIEEGTW VCLQNCHLAV SWMPMLEKIC EDFTSETCNS
SFRLWLTSYP SSKFPVTILQ NGVKMTNEPP TGLRLNLLQS YLTDPVSDPE FFKGCRGKEL
AWEKLLFGVC FFHALVQERK KFGPLGWNIP YGFNESDLRI SIRQLQLFIN EYDTIPFEAI
SYLTGECNYG GRVTDDWDRR LLLTMLADFY NLYIVENPHY KFSPSGNYFA PPKGTYEDYI
EFIKKLPFTQ HPEIFGLHEN VDISKDLQQT KTLFESLLLT QGGSKQTGAS GSTDQILLEI
TKDILNKLPS DFDIEMALRK YPVRYEESMN TVLVQEMERF NNLIITIRNT LRDLEKAIKG
VVVMDSALEA LSGSLLVGKV PEIWAKRSYP SLKPLGSYIT DFLARLNFLQ DWYNSGKPCV
FWLSGFFFTQ AFLTGAMQNY ARKYTTPIDL LGYEFEVIPS DTSDTSPEDG VYIHGLYLDG
ARWDRESGLL AEQYPKLLFD LMPIIWIKPT QKSRIIKSDA YVCPLYKTSE RKGTLSTTGH
STNFVIAMLL KTDQPTRHWI KRGVALLCQL DD
