DYHC1_RAT
ID DYHC1_RAT Reviewed; 4644 AA.
AC P38650; Q63178;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cytoplasmic dynein 1 heavy chain 1;
DE AltName: Full=Cytoplasmic dynein heavy chain 1;
DE AltName: Full=Dynein heavy chain, cytosolic;
DE AltName: Full=MAP 1C;
GN Name=Dync1h1; Synonyms=Dhc1, Dnch1, Dnchc1, Dnec1, Dyhc, Map1c;
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 [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7690137; DOI=10.1073/pnas.90.17.7928;
RA Zhang Z., Tanaka Y., Nonaka S., Aizawa H., Kawasaki H., Nakata T.,
RA Hirokawa N.;
RT "The primary structure of rat brain (cytoplasmic) dynein heavy chain, a
RT cytoplasmic motor enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7928-7932(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7684232; DOI=10.1016/0896-6273(93)90195-w;
RA Mikami A., Paschal B.M., Mazumdar M., Vallee R.B.;
RT "Molecular cloning of the retrograde transport motor cytoplasmic dynein
RT (MAP 1C).";
RL Neuron 10:787-796(1993).
RN [3]
RP SUBUNIT.
RX PubMed=2140361; DOI=10.1016/s0021-9258(19)38944-6;
RA Neely M.D., Erickson H.P., Boekelheide K.;
RT "HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer
RT composed of nearly identical subunits.";
RL J. Biol. Chem. 265:8691-8698(1990).
RN [4]
RP INTERACTION WITH DYNC1LI1; DYNC1LI2 AND DYNC1I2.
RX PubMed=10893223; DOI=10.1074/jbc.m001537200;
RA Tynan S.H., Gee M.A., Vallee R.B.;
RT "Distinct but overlapping sites within the cytoplasmic dynein heavy chain
RT for dimerization and for intermediate chain and light intermediate chain
RT binding.";
RL J. Biol. Chem. 275:32769-32774(2000).
CC -!- FUNCTION: Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules.
CC Dynein has ATPase activity; the force-producing power stroke is thought
CC to occur on release of ADP. Plays a role in mitotic spindle assembly
CC and metaphase plate congression. {ECO:0000250|UniProtKB:Q14204}.
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC dynein LCs assemble on the IC dimer (PubMed:2140361). Interacts with
CC DYNC1LI1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1.
CC Interacts with DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind mutually exclusive
CC to DYNC1H1. Interacts with DYNC1I2 (PubMed:10893223). Interacts with
CC BICD2 (By similarity). Interacts with DNALI1 (By similarity).
CC {ECO:0000250|UniProtKB:Q14204, ECO:0000250|UniProtKB:Q9JHU4,
CC ECO:0000269|PubMed:10893223, ECO:0000269|PubMed:2140361}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; D13896; BAA02996.1; -; mRNA.
DR EMBL; L08505; AAA41103.1; -; mRNA.
DR PIR; A38905; A38905.
DR RefSeq; NP_062099.3; NM_019226.3.
DR BMRB; P38650; -.
DR SMR; P38650; -.
DR BioGRID; 248131; 14.
DR CORUM; P38650; -.
DR IntAct; P38650; 9.
DR MINT; P38650; -.
DR STRING; 10116.ENSRNOP00000066312; -.
DR BindingDB; P38650; -.
DR ChEMBL; CHEMBL3694; -.
DR jPOST; P38650; -.
DR PaxDb; P38650; -.
DR PRIDE; P38650; -.
DR GeneID; 29489; -.
DR KEGG; rno:29489; -.
DR UCSC; RGD:2511; rat.
DR CTD; 1778; -.
DR RGD; 2511; Dync1h1.
DR eggNOG; KOG3595; Eukaryota.
DR InParanoid; P38650; -.
DR OrthoDB; 26380at2759; -.
DR PhylomeDB; P38650; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:P38650; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISO:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; ISO:RGD.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0002177; C:manchette; IDA:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1905243; P:cellular response to 3,3',5-triiodo-L-thyronine; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051293; P:establishment of spindle localization; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 GO; GO:0033962; P:P-body assembly; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0032388; P:positive regulation of intracellular transport; ISS:UniProtKB.
DR GO; GO:1905832; P:positive regulation of spindle assembly; ISS:UniProtKB.
DR GO; GO:0090235; P:regulation of metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IEP:RGD.
DR GO; GO:0034063; P:stress granule assembly; ISO:RGD.
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; 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 Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 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; 4.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT CHAIN 2..4644
FT /note="Cytoplasmic dynein 1 heavy chain 1"
FT /id="PRO_0000114629"
FT REGION 2..1865
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 446..701
FT /note="Interaction with DYNC1I2"
FT /evidence="ECO:0000269|PubMed:10893223"
FT REGION 649..800
FT /note="Interaction with DYNC1LI2"
FT /evidence="ECO:0000269|PubMed:10893223"
FT REGION 1866..2097
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2178..2450
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2389..2409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2554..2803
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2897..3166
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3187..3498
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3551..3780
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 4003..4219
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 48..69
FT /evidence="ECO:0000255"
FT COILED 179..200
FT /evidence="ECO:0000255"
FT COILED 453..476
FT /evidence="ECO:0000255"
FT COILED 541..564
FT /evidence="ECO:0000255"
FT COILED 1169..1201
FT /evidence="ECO:0000255"
FT COILED 1229..1250
FT /evidence="ECO:0000255"
FT COILED 1355..1371
FT /evidence="ECO:0000255"
FT COILED 3187..3273
FT /evidence="ECO:0000255"
FT COILED 3394..3498
FT /evidence="ECO:0000255"
FT COILED 3735..3798
FT /evidence="ECO:0000255"
FT COMPBIAS 2389..2406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1904..1911
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2222..2229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2593..2600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2935..2942
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 1123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHU4"
FT MOD_RES 3478
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 4160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 4281
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT MOD_RES 4364
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14204"
FT CONFLICT 1024..1025
FT /note="SR -> MP (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 1772
FT /note="N -> D (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 2098
FT /note="P -> A (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 2139
FT /note="F -> V (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 2175
FT /note="D -> A (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 2185
FT /note="K -> Q (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 2366
FT /note="L -> V (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 2382
FT /note="T -> S (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 2463
FT /note="G -> A (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 3219
FT /note="A -> D (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 4131
FT /note="R -> K (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 4366
FT /note="F -> S (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
FT CONFLICT 4511
FT /note="A -> G (in Ref. 2; AAA41103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4644 AA; 532252 MW; 8C6ABDBEDF875D82 CRC64;
MSETGGGEDG SAGLEVSAVQ NVADVSVLQK HLRKLVPLLL EDGGDAPAAL EAALEEKSAL
EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN INIDIHYGVK SNSLAFIKRA
PVIDADKPVS SQLRVLTLSE DSPYETLHSF ISNAVAPFFK SYIRESGKAD RDGDKMAPSV
EKKIAELEMG LLHLQQNIEI PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL
NQLQSGVNRW IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD
ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK IRQALVAIFT
HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM HVAYEEFEKV MVACFEVFQT
WDDEYEKLQV LLRDIVKRKR EENLKMVWRI NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR
VLRPQVTAVA QQNQGEAPEP QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG
TEAWEAAMKR YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR
EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK QIDRQLTAYM
KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTIES
ARVRGRSGNV LKLKVNFLPE IITLSKEVRN LKWLGFRVPL AIVNKAHQAN QLYPFAISLI
ESVRTYERTC EKVEERNTIS LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN
FQEKVDDLLI IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK
LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE PKIKNVVHEL
RITNQVIYLN PPIEECRYKL YQEMFAWKMI VLSLPRIQSQ RYQVGVHYEL TEEEKFYRNA
LTRSRDGPVA LEESYSAVMG IVTEVEQYVK VWLQYQCLWD MQAENIYNRL GEDLSKWQAL
LVQIRRARGT FDNAETKKEF GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF
HSQISKSRQE LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF
QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES RTTDLLTDWE
KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE ALELTDTGLL SGSEERVQVA
LEELQDLKGV WSELSKVWEQ IDQMKEQPWV SVQPRKLRQN LDGLLNQLKN FPARLRQYAS
YEFVQRLLKG YMKINMLVIE LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN
EAIVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN
SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT GSADIKHLLP
VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE RLADLLGKIQ KALGEYLERE
RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK HFKKMFAGVS SIILNEDSSV VLGISSREGE
EVMFKTPVSI TEHPKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI
DKYQAQLVVL SAQIAWSENV ENALSNVGGG GNVGPLQSVL SNVEVTLNVL ADSVLMEQPP
LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD VLQQLSIQMA
NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG SPFGPAGTGK TESVKALGHQ
LGRFVLVFNC DETFDFQAMG RIFVGLCQVG AWGCFDEFNR LEERMLSAVS QQVQCIQEAL
REHSNPNYDK TSAPITCELL NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT
KPDRQLIAQV MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSPGN
VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSFC ETMVPKLVAE DIPLLFSLLS
DVFPGVQYHR GEMTDLREEL KKVCKEMYLT YGDGEEVGGM WVEKVLQLYQ ITQINHGLMM
VGPSGSGKSM AWRVLLKALE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH
VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM
FEVQDLKYAT LATVSRCGMV WFSEDLLSTD MIFNNFLARL RTIPLDEGED EAQRRRKGKE
DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL RCLGSLFSML
HQGCRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL SGDSRLKMRA ELGEYIRRIT
TVPLPTAPNI PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTVRHEALLY
TWLAEHKPLV LCGPPGSGKT MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR
RTPNGVVLAP VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK
LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN RAMLRLIPSL
RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW VRGIFEALRP LETLPVEGLI
RIWAHEALRL FQDRLVEDEE RRWTDENIDM VALKHFPNID KEKAMSRPIL YSNWLSKDYI
PVDQEELRDY VKARLKVFYE EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG
KTTLSRFVAW MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS
GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK WFTSQVIRNL
HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNYIV
PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ TLHQANARLA KRGGRTMAIT PRHYLDFINH
YANLFHEKRS ELEEQQMHLN VGLRKIKETV DQVEELRRAL RIKSQELEVK NAAANDKLKK
MVKDQQEAEK KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ
HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV NFSAEEISDA
IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY ADMLKRVEPL RNELQKLEDD
AKDNQQKANE VEQMIRDLEA SIARYKEEYA VLISEAQAIK ADLAAVEAKV NRSTALLKSL
SAERERWEKT SETFKNQMST IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ
FRTDIARTEY LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN
EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE VRRTGGRVLI
TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT VTRSSLQSQC LNEVLKAERP
DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA LNEVKGRILD DDTIITTLEN LKREAAEVTR
KVEETDIVMQ EVETVSQQYL PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE
NPNLKGATDH TQRLSVITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTMGEPTYD
AEFQHFLRGK EIVLSAGSTP KVQGLTVEQA EAVARLSCLP AFKDLIAKVQ ADEQFGIWLE
SSSPEQTVPY LWTEETPATP IGQAIHRLLL IQAFRPDRLL AMAHMFVSTN LGESFMSIME
QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS GHVEDLAAEQ NTQITSIAIG SAEGFNQADK
AINTAVKSGR WVMLKNVHLA PGWLMQLEKK LHSLQPHACF RLFLTMEINP RVPVNLLRAG
RIFVFEPPPG VKANMLRTFS SIPVSRMCKS PNERARLYFL LAWFHAVIQE RLRYAPLGWS
KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY GGRVDNEFDQ
RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR EEFVQWVELL PDAQTPSWLG
LPNNAERVLL TTQGVDMISK MLKMQMLEDE DDLAYAETEK KTRTDFTSDG RPAWMRTLHT
TASNWLHLIP QTLSPLKRTV ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK
KQTNYLRTLI NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAAAGGAK
ELKNIHVCLG ALFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSTT LDACSFGVTG
LKLQGATCSN NKLSLSNAIS TVLPLTQLRW GKQTSAEKKA SVVTLPVYLN FTRADLIFTV
DFEIATKEDP RSFYERGVAV LCTE
