DYH14_HUMAN
ID DYH14_HUMAN Reviewed; 3507 AA.
AC Q0VDD8; A6NG62; A6NNL2; Q0VDD9; Q4VXC7; Q4VXG4; Q4VXG5; Q5VU33; Q5VU34;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Dynein axonemal heavy chain 14;
DE AltName: Full=Axonemal beta dynein heavy chain 14;
DE AltName: Full=Ciliary dynein heavy chain 14;
GN Name=DNAH14; Synonyms=C1orf67;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS SER-220
RP AND LEU-274.
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).
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=Q0VDD8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VDD8-2; Sequence=VSP_031314, VSP_031315, VSP_031316,
CC VSP_031317;
CC Name=3;
CC IsoId=Q0VDD8-3; Sequence=VSP_031314, VSP_031315, VSP_038241,
CC VSP_038242;
CC Name=4;
CC IsoId=Q0VDD8-4; Sequence=VSP_031314, VSP_031315, VSP_031316,
CC VSP_038243, VSP_038244, VSP_038245,
CC VSP_038246, VSP_038247, VSP_038248,
CC VSP_038249, VSP_038250, VSP_038251,
CC VSP_038252, VSP_038253, VSP_038254,
CC VSP_038255;
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 -!- SEQUENCE CAUTION:
CC Sequence=AAI19717.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI19718.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAW69735.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC093560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC119716; AAI19717.1; ALT_INIT; mRNA.
DR EMBL; BC119717; AAI19718.1; ALT_INIT; mRNA.
DR CCDS; CCDS41472.1; -. [Q0VDD8-3]
DR CCDS; CCDS44322.1; -. [Q0VDD8-2]
DR RefSeq; NP_001138626.1; NM_001145154.1. [Q0VDD8-2]
DR RefSeq; NP_001364.1; NM_001373.1.
DR RefSeq; NP_659426.2; NM_144989.2. [Q0VDD8-3]
DR SMR; Q0VDD8; -.
DR BioGRID; 126070; 27.
DR IntAct; Q0VDD8; 11.
DR GlyGen; Q0VDD8; 1 site.
DR iPTMnet; Q0VDD8; -.
DR PhosphoSitePlus; Q0VDD8; -.
DR BioMuta; DNAH14; -.
DR DMDM; 172046085; -.
DR EPD; Q0VDD8; -.
DR jPOST; Q0VDD8; -.
DR MassIVE; Q0VDD8; -.
DR MaxQB; Q0VDD8; -.
DR PeptideAtlas; Q0VDD8; -.
DR PRIDE; Q0VDD8; -.
DR Antibodypedia; 34641; 79 antibodies from 14 providers.
DR DNASU; 127602; -.
DR Ensembl; ENST00000366848.5; ENSP00000355813.1; ENSG00000185842.16. [Q0VDD8-3]
DR Ensembl; ENST00000366850.7; ENSP00000355815.3; ENSG00000185842.16. [Q0VDD8-3]
DR Ensembl; ENST00000400952.7; ENSP00000383737.3; ENSG00000185842.16. [Q0VDD8-2]
DR Ensembl; ENST00000430092.5; ENSP00000414402.1; ENSG00000185842.16. [Q0VDD8-4]
DR Ensembl; ENST00000439375.6; ENSP00000392061.2; ENSG00000185842.16. [Q0VDD8-4]
DR Ensembl; ENST00000445597.6; ENSP00000409472.2; ENSG00000185842.16. [Q0VDD8-1]
DR GeneID; 127602; -.
DR KEGG; hsa:127602; -.
DR UCSC; uc001hou.5; human. [Q0VDD8-1]
DR CTD; 127602; -.
DR DisGeNET; 127602; -.
DR GeneCards; DNAH14; -.
DR HGNC; HGNC:2945; DNAH14.
DR HPA; ENSG00000185842; Tissue enhanced (testis).
DR MIM; 603341; gene.
DR neXtProt; NX_Q0VDD8; -.
DR OpenTargets; ENSG00000185842; -.
DR PharmGKB; PA27399; -.
DR VEuPathDB; HostDB:ENSG00000185842; -.
DR GeneTree; ENSGT00940000160505; -.
DR HOGENOM; CLU_000038_6_0_1; -.
DR InParanoid; Q0VDD8; -.
DR OMA; MFYNDCI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q0VDD8; -.
DR TreeFam; TF342240; -.
DR PathwayCommons; Q0VDD8; -.
DR SignaLink; Q0VDD8; -.
DR BioGRID-ORCS; 127602; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; DNAH14; human.
DR GenomeRNAi; 127602; -.
DR Pharos; Q0VDD8; Tdark.
DR PRO; PR:Q0VDD8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q0VDD8; protein.
DR Bgee; ENSG00000185842; Expressed in left testis and 104 other tissues.
DR ExpressionAtlas; Q0VDD8; baseline and differential.
DR Genevisible; Q0VDD8; HS.
DR GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR GO; GO:0030286; C: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:0016887; F:ATP hydrolysis activity; 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:0060285; P:cilium-dependent cell motility; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.40.50.300; -; 6.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR026980; DNAH6/14.
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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46454:SF6; PTHR46454:SF6; 6.
DR Pfam; PF12774; AAA_6; 2.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 2.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF12777; MT; 1.
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; Glycoprotein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..3507
FT /note="Dynein axonemal heavy chain 14"
FT /id="PRO_0000286560"
FT REGION 91..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..381
FT /evidence="ECO:0000255"
FT MOTIF 1164..1171
FT /note="GPAGTGKT motif"
FT /evidence="ECO:0000250"
FT BINDING 1164..1171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1427..1434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 1818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..177
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031314"
FT VAR_SEQ 249
FT /note="E -> EDYLRESIIQQHMVSPEPASLKEKGKSRRKKDQTHACPNVRKARPVS
FT YDRT (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031315"
FT VAR_SEQ 344
FT /note="K -> KVINIVGSVKEVELIPTLEWLSERRHYYLLRQFKIFSDFRMNKAFVT
FT WKLNVKRIKTEKSRSFLYHHLFLADDLFQTCLVYIRGLCEDAINLKNYNDHENNLSAIC
FT LVK (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031316"
FT VAR_SEQ 345..355
FT /note="LDSSRTYSLDE -> RYLVICGAVYI (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038241"
FT VAR_SEQ 356..3507
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038242"
FT VAR_SEQ 473..3507
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031317"
FT VAR_SEQ 609
FT /note="A -> DTEIETEFENKYMYYEFPEFPTNLFIDPNRLEFSVKIQNMLTNMEKC
FT IT (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038243"
FT VAR_SEQ 744
FT /note="V -> SLDYQSECLLYIDNVIHMSHTLIQSVIEKKNKNLLEVV (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038244"
FT VAR_SEQ 979
FT /note="K -> KGLPKSDMVTHLKQVVTEFKQELPIIIALGNPCLKPRHWEALQEIIG
FT KSVPLDKNCKVENLLALKMFQYENEINDMSTSATNEAALEKMLFKIIDFWNTTPLPLIL
FT HHT (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038245"
FT VAR_SEQ 1017
FT /note="K -> KDLVNEWDQNLTLFSYTLEEWMNCQRNWLYLEPVFHSSEIRRQLPAE
FT TELFSQVISMWKKIMSKIQNKQNALQITTSAGVLEILQNCNIHLEHIKKSLEDYLEVKR
FT LIFPRFYFLSNAELLDILADSRNPESVQPHLVKCFENIKQLLIWKQDIGPPAVKMLISA
FT EGEGLVLPKKIRVRSAVEQWLVNVEKSMFDVLKKERYIYNIILLFQ (in isoform
FT 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038246"
FT VAR_SEQ 1180..1219
FT /note="CALFAFKCNTALIKLPNSLIVLTCFGLEKTVLVMNTVMSF -> SLGKHCVV
FT FNCFEDLDYKIVRKFFFGLVQSGAWSCFDEFNLIDLEVLSVIASQILTIKAAKDNYSA
FT (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038247"
FT VAR_SEQ 1332..1336
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038248"
FT VAR_SEQ 1823
FT /note="G -> GWKHWGQSQGRRRKGNC (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038249"
FT VAR_SEQ 1861
FT /note="R -> RGTSLLTNLQRSGGNFLKITECGECINYTATRDTTCLSFLMSLLLKN
FT SCPVLLTGESGVGKTAAINQMLEKLEGPGAFDIKHGSILGDTLLYSEIKKSSSLKQNIT
FT ILIPETHKTATGSS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038250"
FT VAR_SEQ 2011
FT /note="Q -> QAHLGIYFSINNFTPEVQKSKDQIISCSLAIYHQVRQNMLPTPTKCH
FT YMFNLRDMFKLLLGLLQADRTVVNSKEMAALLFVHEATRVFHDRLIDFTDKSLFYRLLS
FT RELENCFQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038251"
FT VAR_SEQ 2495
FT /note="L -> LVEEHLLFLQAAYKDTVAEKQLLANRKTMASRRFQCASVLLTVLEDE
FT KTRWQETINQIDNKLEGILGDILLSAACIVYSGILTPEFRQLIVNKWETFCIENGISLS
FT SKFSLIKVMAQKYE (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038252"
FT VAR_SEQ 2573..2582
FT /note="SCQASTWRKK -> NLLETLAPGLKAILKKDIYQKKGHYFIRVGDAEFEYNS
FT NFR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038253"
FT VAR_SEQ 2949..3016
FT /note="KHTFCLLLRAINHTGTDLGPVGRGQWLTSTACDRHTDVCSFSFALNDGVPDV
FT EHVQDIFYGHCVDKYH -> TELLNENKETCNPINFPWEKLTSFQRLIL (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038254"
FT VAR_SEQ 3069
FT /note="G -> GIDLTNILLRFAQELKGTTHHVTIISLGRDQAAKAEDLILKALTKTQ
FT QWVFLQNCHLATSFMPRLCTIVESFNSPNVTIDPEFRLWLSSKSYSSFPIPVLKKGLKI
FT AVESPQGLKSNLLQTFGCTGSGEVTEEIFENPDCGQWWKKLLFSLCFFNAVINERKNYG
FT ILGWNIAYKFNSSDLGVAIKVLENSLRGQPSISWQALRYLIGEVIYGGRVIDNWDKRCL
FT KTLLYKFCNPEVLKDDFSFSR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038255"
FT VARIANT 220
FT /note="T -> S (in dbSNP:rs41267347)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032116"
FT VARIANT 274
FT /note="P -> L (in dbSNP:rs41267349)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032117"
FT VARIANT 2671
FT /note="K -> E (in dbSNP:rs6667999)"
FT /id="VAR_057764"
FT CONFLICT 424
FT /note="F -> L (in Ref. 3; AAI19718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3507 AA; 399895 MW; CF0471356846EEA9 CRC64;
MGRRSQWIWA MRCQMLVPVL SLHIGLARAL GCGCIASKIE CLIRCNAPFP LLDAVGSVAS
QELQSLTGTV GVTSGAAAYP RWNLARARAP PHLPGTQDPL RRVRDPTPIV ASSPGRRRGS
WSGGYGQEAS EPGVVGLCCA VLPIHPSLAL AGVGGPDLRR FQEGPQRPSD HGAAEKHMET
FIPIDLTTEN QEMDKEETKT KPRLLRYEEK KYEDVKPLET QPAEIAEKET LEYKTVRTFS
ESLKSEKTEE PKDDDVIRNI IRLREKLGWQ TILPQHSLKY GSSKIAIQKI TLKKPLEDDG
EFVYCLPRKS PKSLYNPYDL QVVSAHTAKH CKEFWVITAS FISKLDSSRT YSLDEFCEEQ
LQQATQALKQ LEDIRNKAIS EMKSTFLKVA EKNEIKEYFE SKLSEDDTTH FKLPKYRRLL
ETFFKFVMLV DYIFQELIRQ LMNTAVTLLL ELFNGSAGMP FSVEKKNENL IRTFKDNSFP
TGKTTNDCEE LVDNSKLHAI SVQKSEVKTD TDINEILNSV EVGKDLRKTY APIFEVNLCL
RIPAESDSSE NSKENFHESD QCPEECVMFE DEMSENKDNC VKKHSSEELL PKAKKSKEIS
YNLEDIISAT ITPLCQDPQL SIFIDLVSIM DLPNKTGSII HYKEQTRWPD CHILFETDPA
YQNIIVNLLT IIGNSMGLVN AYSHKFIKYC TMTEKAKIMS MKISSMGELT SKEFEAILNR
FRNYFRHIVN MAIEKRIGIF NVVVESSLQQ LECDPTEIEE FLEHFIFLNA ISSKISKLEK
EFLTMSQLYS VAKHHQIHIS EEQIAIFQVL LLKFSQLKSS MKLSKINKDT AITKFRDNLE
ACISGLHVDV GNLKAKIRTP LLLCAGTQVS TAMEMIQTLS GEAASLTNKA KAYSHYQDCF
SDSQSHMHSV NVEEITQIVL SEISDIEGDL TLRKKLWEAQ EEWKRASWEW RNSSLQSIDV
ESVQRNVSKL MHIISVLEKE IYSIFIIPSI DDISAQLEES QVILATIKGS PHIGPIKSQI
MFYNDCVKSF VSSYSREKLE KVHAGLMCHL EEVADLVVLD TSNSRTKAIL GALLILYVHC
RDIVINLLLK NIFNAEDFEW TRHLQYKWNE KQKLCYVSQG NASFTYGYEY LGCTSRLVIT
PLTDRCWLTL MEALHLNLGG CPAGPAGTGK TETVKDLAKC ALFAFKCNTA LIKLPNSLIV
LTCFGLEKTV LVMNTVMSFR FVLEGKEIRI NMSCAVFITM NPRYGGGVEL PDNLKSLFRP
VAMMVPHYQM IAEIILFSFG FKSANSLSGK LTNLYELARK QLSQQDHYNF GLRSLKIVLI
MAGTKKREFK CDTSDSLSEA DETLIVIEAI REASLPKCPP EDVPLFENII GDIFPEVTVL
KVNQLALEKV IYTATQQLGL QNWSSQKEKI IQFYNQLQVC VGVMLVGPTG GGKTTVRRIL
EKALTLLPIA DFLSVAERKS ASKISERKGK VDICVLNPKC VTLSELYGQL DPNTMEWTDG
LLSATIRSYV YFNTPKNTKK DIDLRLKSRI SDLSNVFKLD SSDTTETDDN IFEEIEKVVK
IPENHNFDWQ WIILDGPVDT FWVENLNSVL DDTRTLCLAN SERIALTNKI RVIFEVDNLS
QASPATVSRC AMVYMDPVDL GWEPYVKSWL LKTSKIISQS GVDCLEFMIK NSVTDGLQFI
RNRQKFQPYP MEDITVVITL CRILDAFFDF MGKNGGFEQS DDLNDTSSKE ANSQRESVTF
KDIEKRDENT WYPEKNPDKL TKIIQKLFVF AFTWAFGGAL NREDEHRENI PFCPSLEPDS
LAKVTYDFDK LVHELFGNSS QVGINLPTGE CSIFGYFVDI EQCEFIPWSD LVPNDQTLIQ
RDNPTKKPEV RTNKKLLKNN DHKGVVVSTI NFSTNVTAAK TKEMILKKLI RRTKDTLGAP
KNNRILIFID DMNMPVSDMY GAQPPLELIR QLLDLGGVYD TEKNTWKNIQ DLSIVAACVP
VVNDISPRLL KHFSMLVLPH PSQDILCTIF QIGIDGCGKK TCATLACYLT DNKLYRVPIS
HKCAYIEFKE VFKKVFIHAG LKGKPTVLMV PNLNIEQDSF LEDLNYIISS GRIPDLFENV
ELDSIAMKIR YLTEQSGHMD NRQSLLSFFQ KRIYKNLHIF VIMSPEGPSF RQNCRVYPSM
ISSCTIDWYE RWPEEALLIV ANSFLKEKVN FENRENLKEK LAPTCVQIHK SMKDLNRKYF
EETGRFYYTT PNSYLQFMET FAHILRAREE EMQTKRDRFH MGLSTILEAT TLVTEMQEEL
LILGPQVEQK TKETETLMEK LRKDSQVVEK VQMLVKQDEE IVAEEVRIVE DYAQKTANEL
KSVLPAFDKA IVALNALDKA DVAELRVYTR PPFLVLTVMN AVCILLQKKP NWATAKLLLS
ETGFLKKLIN LDKDSIPDKV FVKLKKIVTL PDFNPHKISL VSVACCSLCQ WVIALNNYHE
VQKVVGPKQI QVAEAQNVLK IARQRLAEKQ RGLQLISRWH NQGLPHGQYS VENAILIKNG
QQWPLLIDPH RQAHKWIRQM EGSRLQKLSI EDSNYTKKIE NAMKTGGSVL LQSCQASTWR
KKLYLSTEID NPHFLPSVYN FVTMINFTVT FQGLQDQLLS TVVTHEVPHL EDQRSKLLES
ISLDAITLEE LEEKTLNLLQ KALGSILDDD KIVDTLRKSK MTSNEISKRI EATKKAESEI
QAIRKNYLPI ATRGALLYFL VADLTQINYM YQFSLDWFHQ VFVSSVVSKS KEQEHSFKRE
KVSPKEVHEF ISISKEPNLE NEKNLLDKHI KSAIDMLTKS IFKVVSSALF NEDKLCFSFR
LCTVIMQNNA NGNLIQDDIG FLPEEEWNIF LYSGILINIK SALSQSRLTS TFEIGESQHL
QWLSDSRWRQ CQYVSTHLEP FSLLCKSLLS NVSQWDTFKN SKAVYSLIST PFSSENASLE
ENTKPPEEKH TFCLLLRAIN HTGTDLGPVG RGQWLTSTAC DRHTDVCSFS FALNDGVPDV
EHVQDIFYGH CVDKYHVKVL RPESLNNSVR KFITEKMGNK YLQRTGVNLK DAYKGSNART
PLILIQTHGS ASIKDYIHII QSLPDDDLPE VLGIHPEAIR SCWETQGEKF IENLIAMQPK
TTTANLMIRP EQSKDELVME ILSDLLKRLP LTVEKEEIAV GTPSTLKSMM SSSIWESLSK
NLKDHDPLIH CVLLTFLKQE IKRFDKLLFV IHKSLKDLQL AIKGEIILTQ ELEEIFNSFL
NMRVPTLWQK HAYRSCKPLS SWIDDLIQRL NFFNTWAKVA YTAIQRRYMR FVTVWKQSIP
STSQKCKHPE DSENNFFEGF PSRYWLPAFF FPQAFLAAVL QDYGRSRGIA VDALTFTHHV
ISNTTDKDEK FSVFMPKKLN IVRRAFKGSA SSHTGVYIFG LFIEGARWNR EQKILEDSLP
LEMCCDFPDI YFLPTKISTK TPNASNQTDS ELYAFECPVY QTPERSRILA TTGLPTNFLT
SVYLSTKKPP SHWITMRVAL LCEKNEK
