DYHC_YEAST
ID DYHC_YEAST Reviewed; 4092 AA.
AC P36022; D6VXB5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Dynein heavy chain, cytoplasmic;
DE AltName: Full=Dynein heavy chain, cytosolic;
DE Short=DYHC;
GN Name=DYN1; Synonyms=DHC1; OrderedLocusNames=YKR054C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8248224; DOI=10.1073/pnas.90.23.11172;
RA Eshel D., Urrestarazu L.A., Vissers S., Jauniaux J.-C.,
RA van Vliet-Reedijk J.C., Planta R.J., Gibbons I.R.;
RT "Cytoplasmic dynein is required for normal nuclear segregation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11172-11176(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-3457.
RX PubMed=8234262; DOI=10.1073/pnas.90.21.10096;
RA Li Y.-Y., Yeh E.Y., Hays T., Bloom K.S.;
RT "Disruption of mitotic spindle orientation in a yeast dynein mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10096-10100(1993).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DYN3.
RX PubMed=15642746; DOI=10.1083/jcb.200407036;
RA Lee W.-L., Kaiser M.A., Cooper J.A.;
RT "The offloading model for dynein function: differential function of motor
RT subunits.";
RL J. Cell Biol. 168:201-207(2005).
CC -!- FUNCTION: Cytoplasmic dynein 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. Required to maintain uniform nuclear
CC distribution in hyphae. May play an important role in the proper
CC orientation of the mitotic spindle into the budding daughter cell
CC yeast. Probably required for normal progression of the cell cycle.
CC {ECO:0000269|PubMed:15642746}.
CC -!- SUBUNIT: The dynein complex consists of at least two heavy chains and a
CC number of intermediate and light chains. Interacts with DYN3.
CC {ECO:0000269|PubMed:15642746}.
CC -!- INTERACTION:
CC P36022; P40960: PAC11; NbExp=3; IntAct=EBI-6230, EBI-30551;
CC P36022; P32908: SMC1; NbExp=3; IntAct=EBI-6230, EBI-17402;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15642746}.
CC Note=Concentrates at motile dots in the cytoplasm corresponding to the
CC plus ends of cytoplasmic microtubules.
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 -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; Z21877; CAA79923.1; -; Genomic_DNA.
DR EMBL; L15626; AAA16055.1; -; Unassigned_DNA.
DR EMBL; Z28279; CAA82132.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09205.1; -; Genomic_DNA.
DR PIR; S38128; S38128.
DR RefSeq; NP_012980.1; NM_001179844.1.
DR PDB; 3J67; EM; 34.00 A; A=1554-4092.
DR PDB; 3J68; EM; 30.00 A; A=1554-4092.
DR PDB; 3QMZ; X-ray; 6.00 A; A/B=1364-4092.
DR PDB; 4AI6; X-ray; 3.40 A; A/B=1364-4092.
DR PDB; 4AKG; X-ray; 3.30 A; A/B=1364-4092.
DR PDB; 4AKH; X-ray; 3.60 A; A/B=1364-4092.
DR PDB; 4AKI; X-ray; 3.70 A; A/B=1364-4092.
DR PDB; 4W8F; X-ray; 3.54 A; A/B=1364-3038, A/B=3292-4092.
DR PDB; 5AFR; X-ray; 5.00 A; A/B=1-557.
DR PDB; 5VH9; EM; 7.70 A; A=1448-4092.
DR PDB; 5VLJ; EM; 10.50 A; A=1448-4092.
DR PDB; 6KIO; EM; 3.94 A; M=3095-3224.
DR PDB; 6KIQ; EM; 3.62 A; M=3095-3224.
DR PDB; 6KJN; NMR; -; A=3095-3232.
DR PDB; 6KJO; NMR; -; A=3095-3232.
DR PDB; 7MI1; X-ray; 4.50 A; A=1364-3038, A=3064-3076, A=3292-4092.
DR PDB; 7MI3; EM; 3.50 A; A=1364-3038, A=3064-3076, A=3292-4092.
DR PDB; 7MI6; EM; 3.90 A; A=1364-3038, A=3064-3076, A=3292-4092.
DR PDB; 7MI8; EM; 3.70 A; A=1364-3038, A=3064-3076, A=3292-4092.
DR PDBsum; 3J67; -.
DR PDBsum; 3J68; -.
DR PDBsum; 3QMZ; -.
DR PDBsum; 4AI6; -.
DR PDBsum; 4AKG; -.
DR PDBsum; 4AKH; -.
DR PDBsum; 4AKI; -.
DR PDBsum; 4W8F; -.
DR PDBsum; 5AFR; -.
DR PDBsum; 5VH9; -.
DR PDBsum; 5VLJ; -.
DR PDBsum; 6KIO; -.
DR PDBsum; 6KIQ; -.
DR PDBsum; 6KJN; -.
DR PDBsum; 6KJO; -.
DR PDBsum; 7MI1; -.
DR PDBsum; 7MI3; -.
DR PDBsum; 7MI6; -.
DR PDBsum; 7MI8; -.
DR BMRB; P36022; -.
DR SMR; P36022; -.
DR BioGRID; 34185; 353.
DR ComplexPortal; CPX-1178; Cytoplasmic dynein complex.
DR DIP; DIP-2644N; -.
DR IntAct; P36022; 11.
DR MINT; P36022; -.
DR STRING; 4932.YKR054C; -.
DR iPTMnet; P36022; -.
DR MaxQB; P36022; -.
DR PaxDb; P36022; -.
DR PRIDE; P36022; -.
DR EnsemblFungi; YKR054C_mRNA; YKR054C; YKR054C.
DR GeneID; 853928; -.
DR KEGG; sce:YKR054C; -.
DR SGD; S000001762; DYN1.
DR VEuPathDB; FungiDB:YKR054C; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000156103; -.
DR HOGENOM; CLU_000038_7_0_1; -.
DR InParanoid; P36022; -.
DR OMA; FIMDEAN; -.
DR BioCyc; YEAST:G3O-32023-MON; -.
DR BRENDA; 5.6.1.2; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9646399; Aggrephagy.
DR PRO; PR:P36022; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36022; protein.
DR GO; GO:0000235; C:astral microtubule; IDA:SGD.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IPI:SGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:SGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
DR GO; GO:0051293; P:establishment of spindle localization; IBA:GO_Central.
DR GO; GO:0000741; P:karyogamy; IEA:UniProtKB-KW.
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:0000070; P:mitotic sister chromatid segregation; IGI:SGD.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:SGD.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 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; 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; 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; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 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 3D-structure; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein;
KW Karyogamy; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..4092
FT /note="Dynein heavy chain, cytoplasmic"
FT /id="PRO_0000114643"
FT REGION 1..1757
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1758..1979
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2036..2273
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2379..2628
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2722..2984
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2993..3300
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3370..3599
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3760..3970
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 154..175
FT /evidence="ECO:0000255"
FT COILED 486..508
FT /evidence="ECO:0000255"
FT COILED 542..566
FT /evidence="ECO:0000255"
FT COILED 932..959
FT /evidence="ECO:0000255"
FT COILED 1042..1063
FT /evidence="ECO:0000255"
FT COILED 1681..1705
FT /evidence="ECO:0000255"
FT COILED 2993..3092
FT /evidence="ECO:0000255"
FT COILED 3242..3300
FT /evidence="ECO:0000255"
FT COILED 3532..3608
FT /evidence="ECO:0000255"
FT BINDING 1796..1803
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2074..2081
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2418..2425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2760..2767
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 589
FT /note="Y -> C (in Ref. 4; AAA16055)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="V -> A (in Ref. 4; AAA16055)"
FT /evidence="ECO:0000305"
FT CONFLICT 1364
FT /note="E -> A (in Ref. 4; AAA16055)"
FT /evidence="ECO:0000305"
FT CONFLICT 2118..2119
FT /note="ML -> IV (in Ref. 1; CAA79923)"
FT /evidence="ECO:0000305"
FT HELIX 1366..1378
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1384..1387
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1389..1391
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1393..1396
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1399..1414
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 1420..1424
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1425..1458
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1464..1468
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1470..1491
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1497..1501
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1505..1533
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1537..1540
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1542..1550
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 1551..1554
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1556..1558
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1559..1565
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1567..1574
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1576..1584
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1589..1597
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1604..1631
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1636..1640
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1645..1666
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1669..1688
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1692..1717
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1721..1730
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1733..1736
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1743..1745
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1747..1751
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1754..1757
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1773..1787
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1791..1795
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1802..1811
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 1812..1814
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1818..1821
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1828..1841
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1844..1849
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1855..1874
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1877..1880
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1882..1887
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1893..1898
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1902..1905
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1910..1913
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 1916..1920
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1926..1938
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1942..1959
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1970..1986
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 1991..2001
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2003..2005
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2008..2021
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2029..2032
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2033..2045
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2051..2066
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2068..2073
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2080..2094
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2098..2104
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2106..2108
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2111..2114
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2120..2122
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2130..2138
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2142..2145
FT /evidence="ECO:0007829|PDB:7MI3"
FT STRAND 2146..2154
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2160..2164
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2167..2170
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2175..2177
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2179..2181
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2183..2185
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2188..2197
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2204..2209
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2210..2214
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2222..2238
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2243..2256
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2259..2270
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2280..2297
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2300..2302
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2303..2305
FT /evidence="ECO:0007829|PDB:4AI6"
FT HELIX 2307..2327
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2333..2345
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2348..2350
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2358..2361
FT /evidence="ECO:0007829|PDB:7MI3"
FT STRAND 2363..2365
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2368..2371
FT /evidence="ECO:0007829|PDB:7MI3"
FT HELIX 2383..2385
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2395..2410
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2413..2417
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2424..2433
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2439..2444
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2451..2461
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2465..2467
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2468..2470
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2471..2480
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2482..2487
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2488..2490
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2496..2498
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2501..2511
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2513..2516
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2518..2520
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2523..2535
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2548..2551
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2554..2558
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2563..2565
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2566..2578
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2579..2581
FT /evidence="ECO:0007829|PDB:7MI3"
FT HELIX 2583..2588
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2589..2606
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2609..2611
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2619..2634
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2641..2656
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2657..2659
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2664..2680
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2691..2693
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2696..2703
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2709..2726
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2736..2750
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2751..2759
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2761..2763
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2766..2776
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2780..2782
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2792..2808
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2813..2818
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2819..2821
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2825..2836
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2837..2839
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 2841..2843
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2847..2863
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2870..2884
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2886..2892
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2897..2904
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2906..2911
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2912..2916
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2922..2932
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2942..2944
FT /evidence="ECO:0007829|PDB:7MI3"
FT TURN 2945..2950
FT /evidence="ECO:0007829|PDB:7MI3"
FT HELIX 2961..2979
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 2983..2985
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 2991..3027
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3098..3100
FT /evidence="ECO:0007829|PDB:6KJO"
FT HELIX 3104..3107
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3109..3114
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3117..3125
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3131..3144
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3151..3158
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3163..3169
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3180..3188
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3196..3202
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3206..3218
FT /evidence="ECO:0007829|PDB:6KJN"
FT HELIX 3219..3221
FT /evidence="ECO:0007829|PDB:6KJN"
FT TURN 3222..3224
FT /evidence="ECO:0007829|PDB:6KJN"
FT STRAND 3227..3230
FT /evidence="ECO:0007829|PDB:6KJO"
FT HELIX 3300..3304
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3305..3307
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3308..3333
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3334..3336
FT /evidence="ECO:0007829|PDB:4AI6"
FT HELIX 3339..3355
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3366..3370
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3373..3382
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3388..3399
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3402..3408
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3410..3412
FT /evidence="ECO:0007829|PDB:7MI3"
FT HELIX 3414..3422
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3423..3425
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3426..3429
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3436..3445
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3449..3453
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3455..3457
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3460..3462
FT /evidence="ECO:0007829|PDB:7MI3"
FT HELIX 3463..3466
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3477..3480
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3482..3487
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3493..3498
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3507..3512
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3513..3517
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3523..3537
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3539..3572
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3573..3576
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3580..3638
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3646..3655
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3670..3686
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3692..3710
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3713..3726
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3727..3729
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3738..3740
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3743..3752
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3756..3765
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3774..3780
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3784..3790
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3797..3805
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3806..3808
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3813..3815
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3819..3835
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3839..3842
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3844..3847
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3848..3853
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3855..3861
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3865..3867
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3868..3870
FT /evidence="ECO:0007829|PDB:4AI6"
FT STRAND 3873..3876
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3879..3881
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3886..3891
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3892..3897
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3903..3913
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3914..3917
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3923..3944
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3946..3949
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 3950..3952
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3958..3974
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3980..3982
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 3983..3991
FT /evidence="ECO:0007829|PDB:4AKG"
FT TURN 3995..3997
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 4001..4014
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 4018..4020
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 4023..4026
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 4038..4051
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 4058..4061
FT /evidence="ECO:0007829|PDB:4AKG"
FT STRAND 4063..4065
FT /evidence="ECO:0007829|PDB:4AKG"
FT HELIX 4067..4090
FT /evidence="ECO:0007829|PDB:4AKG"
SQ SEQUENCE 4092 AA; 471348 MW; 3D9DF447E8E2D6BB CRC64;
MCKNEARLAN ELIEFVAATV TGIKNSPKEN EQAFIDYLHC QYLERFQFFL GLLDGREFDT
LFVFLFEELD RTIVTIDIGE EAIYDANLAN KKYSTLLIIK SRSVIVDAEP IATQISAIYL
PGPVNAGNLA SIITHGVSSV FGQLIKSDTK TYSVETIDKT RRKLDDISKQ FQQLHTSIET
PDLLAMVPSI IKLAVSKGAT SHDYANYLPS NDLESMRFLN ILQSIANKWF LVLKQTLAID
RDIKNGSFLD EVEFWSNFYE VLKSLIEQTQ SQEFQVCLSV LTNAKRFHNL TNLLNEGSLS
DKFKLADKYN QFLSSIPIDE VRQASNLEDL QELFPVLASS LKKFRYSGYP VQRFVVLMDK
ISQEVMDAIL SNLSDLFQLE YGSFLGLYEK SAGMIEEWDD IVQDVNLLIR EDLRKRAPQE
LLIQKLTFTS ASVKATLDEI LSTRKRFFSL AETIKSISPS TYHEEIQRLY HPFEQIHDIS
VNFRLKLEQA ESEFSKNMLD LEKKLQNTLA SFMDSDHCPT EKLSYLVKFK PLMELCPRIK
VKVLENQQIL LLEIKKDIRQ LETGLELLPK ILHVEALNNI PPISARISYF LNVQSRIDNI
VQYLEALFGS NWNDTLEGRS ISTSIVQLRK ETNPHDVFLH WLGNFPEKAT ANLLTTPILK
LIRNNEDDYE LKVNFDFALA AAYSELRSLT YMAFQVPSHI VRIARTYMYL YPRAINLVEL
IQTFFSLSKS LSYTFYTNIF LKRNVQTVWL LLQQILITPW ESLQEESSEM SCSVHSLARL
EKSIDGILSD YQILKNSEPQ FAKEFSGLKS FDGTADDLHE VEEIISNIQA IFENLFTKGL
TNVSDHISTF NNLIISIILE KVRLNLKKMH FPKHVLKLSF NEGRITSSPS LAAMKRSLLK
DIEALLNKVV LINFLHDPDH PLSTTLTFNS LVIKLKDDIQ NCIEQVQNLH CKINSYVKEW
QKMEFLWQIT EEAFLEVVDN STQRCFGILK GLLDSQSKFD LIISRNNFSK NLVLHTEDAQ
RHIRSKMDSW ILYVSKHLLT IYERDARKLH EDMNRDREAV EDMDINFTSL KNITVIIEAV
NVNKRHLTER DIQIKLLGSV MRALTKLKVR FPSHFVYIDQ LDNDFSSLRQ SLSYVEQELQ
KHRVVIAKSL EEGVENINNL SQSLNESWSV RKPISPTLTP PEALKILEFF NESITKLKKK
MHSVAAAAKM LLIPVVLNDQ LTHVVEEVKT YDLVWRSIKN LWEDVQRTFE TPWCRVDVLL
LQSDLANFLR RADELPRAVK QFEMYKSLFS QVNMLTSVNK ILVELKDGAL KPRHWNMIFR
DIGKRQIQKN LLDKLEFSLK DVMVLNLTLN EILLTKIIER AQKEFVIEKS LNRIKKFWKE
AQYEVIEHSS GLKLVREWDV LEQACKEDLE ELVSMKASNY YKIFEQDCLD LESKLTKLSE
IQVNWVEVQF YWLDLYGILG ENLDIQNFLP LETSKFKSLT SEYKMITTRA FQLDTTIEVI
HIPNFDTTLK LTIDSLKMIK SSLSTFLERQ RRQFPRFYFL GNDDLLKIIG SGKHHDQVSK
FMKKMFGSIE SIIFLEDFIT GVRSVEGEVL NLNEKIELKD SIQAQEWLNI LDTEIKLSVF
TQFRDCLGQL KDGTDIEVVV SKYIFQAILL SAQVMWTELV EKCLQTNQFS KYWKEVDMKI
KGLLDKLNKS SDNVKKKIEA LLVEYLHFNN VIGQLKNCST KEEARLLWAK VQKFYQKNDT
LDDLNSVFIS QSGYLLQYKF EYIGIPERLI YTPLLLIGFA TLTDSLHQKY GGCFFGPAGT
GKTETVKAFG QNLGRVVVVF NCDDSFDYQV LSRLLVGITQ IGAWGCFDEF NRLDEKVLSA
VSANIQQIQN GLQVGKSHIT LLEEETPLSP HTAVFITLNP GYNGRSELPE NLKKSFREFS
MKSPQSGTIA EMILQIMGFE DSKSLASKIV HFLELLSSKC SSMNHYHFGL RTLKGVLRNC
SPLISEFGEG EKTVVESLKR VILPSLGDTD ELVFKDELSK IFDSAGTPLN SKAIVQCLKD
AGQRSGFSMS EEFLKKCMQF YYMQKTQQAL ILVGKAGCGK TATWKTVIDA MAIFDGHANV
VYVIDTKVLT KESLYGSMLK ATLEWRDGLF TSILRRVNDD ITGTFKNSRI WVVFDSDLDP
EYVEAMNSVL DDNKILTLPN GERLPIPPNF RILFETDNLD HTTPATITRC GLLWFSTDVC
SISSKIDHLL NKSYEALDNK LSMFELDKLK DLISDSFDMA SLTNIFTCSN DLVHILGVRT
FNKLETAVQL AVHLISSYRQ WFQNLDDKSL KDVITLLIKR SLLYALAGDS TGESQRAFIQ
TINTYFGHDS QELSDYSTIV IANDKLSFSS FCSEIPSVSL EAHEVMRPDI VIPTIDTIKH
EKIFYDLLNS KRGIILCGPP GSGKTMIMNN ALRNSSLYDV VGINFSKDTT TEHILSALHR
HTNYVTTSKG LTLLPKSDIK NLVLFCDEIN LPKLDKYGSQ NVVLFLRQLM EKQGFWKTPE
NKWVTIERIH IVGACNPPTD PGRIPMSERF TRHAAILYLG YPSGKSLSQI YEIYYKAIFK
LVPEFRSYTE PFARASVHLY NECKARYSTG LQSHYLFSPR ELTRLVRGVY TAINTGPRQT
LRSLIRLWAY EAWRIFADRL VGVKEKNSFE QLLYETVDKY LPNQDLGNIS STSLLFSGLL
SLDFKEVNKT DLVNFIEERF KTFCDEELEV PMVIHESMVD HILRIDRALK QVQGHMMLIG
ASRTGKTILT RFVAWLNGLK IVQPKIHRHS NLSDFDMILK KAISDCSLKE SRTCLIIDES
NILETAFLER MNTLLANADI PDLFQGEEYD KLLNNLRNKT RSLGLLLDTE QELYDWFVGE
IAKNLHVVFT ICDPTNNKSS AMISSPALFN RCIINWMGDW DTKTMSQVAN NMVDVIPMEF
TDFIVPEVNK ELVFTEPIQT IRDAVVNILI HFDRNFYQKM KVGVNPRSPG YFIDGLRALV
KLVTAKYQDL QENQRFVNVG LEKLNESVLK VNELNKTLSK KSTELTEKEK EARSTLDKML
MEQNESERKQ EATEEIKKIL KVQEEDIRKR KEVVMKSIQD IEPTILEAQR GVKNIKKQQL
TEIRSMVNPP SGVKIVMEAV CAILGYQFSN WRDIQQFIRK DDFIHNIVHY DTTLHMKPQI
RKYMEEEFLS DPNFTYETIN RASKACGPLY QWVNAQINFS KVLENVDPLR QEMKRIEFES
LKTKANLLAA EEMTQDLEAS IEVSKRKYSL LIRDVEAIKT EMSNVQANLD RSISLVKSLT
FEKERWLNTT KQFSKTSQEL IGNCIISSIY ETYFGHLNER ERADMLVILK RLLGKFAVKY
DVNYRFIDYL VTLDEKMKWL ECGLDKNDYF LENMSIVMNS QDAVPFLLDP SSHMITVISN
YYGNKTVLLS FLEEGFVKRL ENAIRFGSVV IIQDGEFFDP IISRLISREF NHAGNRVTVE
IGDHEVDVSG DFKLFIHSCD PSGDIPIFLR SRVRLVHFVT NKESIETRIF DITLTEENAE
MQRKREDLIK LNTEYKLKLK NLEKRLLEEL NNSQGNMLEN DELMVTLNNL KKEAMNIEKK
LSESEEFFPQ FDNLVEEYSI IGKHSVKIFS MLEKFGQFHW FYGISIGQFL SCFKRVFIKK
SRETRAARTR VDEILWLLYQ EVYCQFSTAL DKKFKMIMAM TMFCLYKFDI ESEQYKEAVL
TMIGVLSESS DGVPKLTVDT NNDLRYLWDY VTTKSYISAL NWFKNEFFVD EWNIADVVAN
SENNYFTMAS ERDVDGTFKL IELAKASKES LKIIPLGSIE NLNYAQEEIS KSKIEGGWIL
LQNIQMSLSW VKTYLHKHVE ETKAAEEHEK FKMFMTCHLT GDKLPAPLLQ RTDRFVYEDI
PGILDTVKDL WGSQFFTGKI SGVWSVYCTF LLSWFHALIT ARTRLVPHGF SKKYYFNDCD
FQFASVYLEN VLATNSTNNI PWAQVRDHIA TIVYGGKIDE EKDLEVVAKL CAHVFCGSDN
LQIVPGVRIP QPLLQQSEEE ERARLTAILS NTIEPADSLS SWLQLPRESI LNYERLQAKE
VASSTEQLLQ EM
