DYHC_SCHPO
ID DYHC_SCHPO Reviewed; 4196 AA.
AC O13290; Q9P6L0; Q9UTP8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Dynein heavy chain, cytoplasmic;
DE AltName: Full=Dynein heavy chain, cytosolic;
DE Short=DYHC;
GN Name=dhc1; ORFNames=SPAC1093.06c, SPAC30C2.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=CRL152;
RX PubMed=10366596; DOI=10.1083/jcb.145.6.1233;
RA Yamamoto A., West R.R., McIntosh J.R., Hiraoka Y.;
RT "A cytoplasmic dynein heavy chain is required for oscillatory nuclear
RT movement of meiotic prophase and efficient meiotic recombination in fission
RT yeast.";
RL J. Cell Biol. 145:1233-1249(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 for nuclear movement during
CC meiotic prophase. {ECO:0000269|PubMed:10366596}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- INTERACTION:
CC O13290; O42667: ssm4; NbExp=2; IntAct=EBI-1112490, EBI-1556587;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10366596}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:10366596}.
CC Note=Localized at the astral microtubules and the spindle pole body
CC (SPB) during nuclear movements associated with meiotic prophase.
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; AB006784; BAA22056.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB60251.1; -; Genomic_DNA.
DR PIR; T43274; T43274.
DR PIR; T50069; T50069.
DR RefSeq; XP_001713108.1; XM_001713056.2.
DR SMR; O13290; -.
DR BioGRID; 280476; 16.
DR IntAct; O13290; 3.
DR STRING; 4896.SPAC1093.06c.1; -.
DR iPTMnet; O13290; -.
DR PaxDb; O13290; -.
DR PRIDE; O13290; -.
DR EnsemblFungi; SPAC1093.06c.1; SPAC1093.06c.1:pep; SPAC1093.06c.
DR PomBase; SPAC1093.06c; dhc1.
DR VEuPathDB; FungiDB:SPAC1093.06c; -.
DR eggNOG; KOG3595; Eukaryota.
DR HOGENOM; CLU_000038_7_0_1; -.
DR InParanoid; O13290; -.
DR OMA; FIMDEAN; -.
DR PhylomeDB; O13290; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-9646399; Aggrephagy.
DR PRO; PR:O13290; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:PomBase.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISO:PomBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:1990574; C:meiotic spindle astral microtubule; IDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
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:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IDA:PomBase.
DR GO; GO:0051293; P:establishment of spindle localization; IBA:GO_Central.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:PomBase.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:PomBase.
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:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0007097; P:nuclear migration; 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; 3.20.180.20; -; 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; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
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; 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; 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 ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..4196
FT /note="Dynein heavy chain, cytoplasmic"
FT /id="PRO_0000114642"
FT REGION 1..1851
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1852..2069
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2135..2379
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2484..2728
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2822..3082
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3315..3403
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3471..3696
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3874..4085
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 1217..1252
FT /evidence="ECO:0000255"
FT COILED 3315..3403
FT /evidence="ECO:0000255"
FT COILED 3649..3666
FT /evidence="ECO:0000255"
FT BINDING 1890..1897
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2169..2176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2174..2181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2520..2527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 4196 AA; 484318 MW; 8F10AE370184FC0C CRC64;
MDKNDNSQCQ LSTVSDEILI FLKKLLSLSV SDNLDDICET IALQSTFVDT FRSFINDEYY
TVIYLYGSPC LTSSPTSPDS CTFGNMTFQW TSLLQDVFSG TSAFAIFKRF PLTDTPLTLQ
NMLYINQLPI LKGGHKSNEI PERPINAIFL YTKYVMSCYF TAYLAMESVD DRSTIDLNSP
SKGKELELTC QKFADFERSF TFFCREYQNS DTILQHHPLI LSTIKHAEEN NLDLSVRLLP
SKVLSDSEFY KSLSNLVNVW LKTTRSLIKL FHDQISKTAL EEFNFWQFYY RSLSRLNDQL
HSRPVLFVLD ILAFGKRFHT IASFNSETNI QCFVDKVGKI DALFKEISLD IFLSSSTLES
LQLSAALLYS TFSKKWRNTG YPETRVLDFI NFITEDLLKL ISRLLPALGA LSLSNVDFSH
RTAVSSDILS LCYIRLKDFL RISGSLKEEQ SYYGLKNSIK QIKAFENKLK YIQSFHEKHQ
QLIGALSEVY GLTHLTELEI LEHLNKKEHV FNILTVFKDL QSLNVLDISL KGVNAWNSLE
TSYYNCMTVL EDEVIAQLKS LLQYSKTSSQ MFTTLMRFQP LFFRTRVRTS ISDCLHLLVN
RIKQELDLLK TRFTEDVSDT ELIAMNELRN LPMASSAIIW ATQLKNRLHE YTKNINIIFG
EDWNNFPDGF ELKVECITLQ KRLDTNLIFT NWINDVSSRN LNFDFDSKIF YLTQSESAES
PLRLSVSIDF DPCSFCKEIR TLAHLGYNIP SQLMELASCL QRIQLIAMCL IDSVQSFNDV
SFEISKTEEE RFLLQEYELA VRQHIVTGLF ISWNDFIVGN LSTPPKCAIG KRNFLKNIHP
NVENYAYQFS SLTSLLMNKR NAISHTYMQI QEQLFQLDIC EYSGDIFLTI QRKLQDLIDL
LYVNGYSNLP PFVRALNLRF QDLLISRCRK FLSFFKTTIL TSGNENNDLK SKFSSDMYEK
LRGFLKPTNL TIQRNIIEFD PPVYRKKEDS IYLLDMCLQS VVNIPLLSIK TTAQRNCTLI
GFFPVINRLE SEILGIFESL LFHFDSILGY QNYWKKVEPF LNLNSLNLLL KSELFQLDQC
YSLSLYLIHL KSEVDEIGKV TDFKIFSVNN TEFKSQVYLY LREWINALFD RFTFLLGKES
EHLLNELDDT HSSLSTVDFT VNNTESLINS LKIFKKAGCY KLNVEHKIIT YQNYEMTFND
CDAFSEFNFS LLKDITSKWK DLLESFECRR LKLENNKDEI LRNFSEFAKR VNTETLSLIS
EWCASSLSLI KANYDEFSST VDDFLFRFSK ATEQCLMVKY IKKDLEIEIE ESCDFSIQTE
EIHLYKKFKD VISSNLEFIV EIKNTRWKLF DTATLSVQTT HQINALESVH TSFQHFKLFT
NTKQSLNQLK DCTLLLQKLK SCPLKPVHWI SLFEITKSTE QLDFEKLLVS DILGIDLQAH
ESFITTLLNS AVVEANLENQ FNEVHSFWKN SYFSFKSFKG RNYIVVGCQE LIDAVEKNMD
SLNLIKTSRH FKDGDMNITD LQSKMKIIVK FLNIWKEIQQ IWTHLSAIFY ESTYIQQLLP
ELAASFFNSS KTYMHLVTLL KERSYLYKVS NIPSLLESAA KLSTTLEDSK KSLLKYFELQ
RHKISRLYFL GDDDLMELIS NPCDPFVINK QIIKLYPGIR SLIVDTENTN INGCTTNEGN
ELLFDNPICL LDNTQPLHWI SSLEPFLKAT LFQLFSTSFQ QIRDFYYNKS RNVFCKEWFL
RYPSQITLLS LRCTLCHEIE TGIADCCLDA VFNFINDGIS SLVLLADENE LSIKKKVTLM
FNELLHFKET VGLLCKNSFN NYFWSREVKA FYREDHDDEA VVIKMFSLEF IYAFEYSELD
DPIVYTDLTR NCFSVLLHSI ASNLGGSPIG PAGTGKTETV KAVSAYLGKN VFVFNCDNAF
NYKTIQRILS GLAQIGTYIC FDEFNRLDSG TLSAISYDIQ RIQSLVSHSD GLCQSPILLD
APTIFVTMNP GYLGRFKLPS NLKKLFRPIW MGSPDNKKIC EILFLSFGFK ESSLLSQVLD
SFFLCCSGSL SNCLHYDFGL RAMKVVIKAA KRIKGFLKKK NTICQELEIL WYAIREVLYP
SLIYQDIPLF FKAEESYFNF PAVKANAFID PDNFEVNIEQ TLSKNFFGNN QYLKLKIMQL
YQMSEAYNGI ILLGKTGSGK SQIFRILQSA LLNIGIDCIV YVISPKALTK ESLFGSMNMD
TREWTDGVFT KLLRKTRDSC YYKRYMFVFD DELSPEWVEA MNSLLDDNKT LTLSNGERIA
LQPYVKIFFE ADSVASLTRA TISRCGLICI SNIDDNILSS TDKMLSFTSG ATNYPLGSSN
DEFSTVFSKV LTDEVMMNLI SSCYKFSVDL QHIMNFTKQR FFTTFYSLLD QTKLFTRSSN
ITESLSFKEL CNYLKKKICY ILAWCCTGDT DAKSRERFTH WLMQNASVDL PEIKDFEHVS
ILDFDVSLET QSWYPIAGKT LKSSALKYAG NTVIPTLDTV RYAEFLNFSL TKNRCVIFCG
PPGSGKSMLM LGTLRSRQDV EVIALNFSIS TSSKSVVSFL EQSTVYYRST GMTIMCPKNH
EKVLVLFCDE INLPRSRNCL AEDVICFLRH MLEHQGFWHP LHKEWVTIKN IFVCGACNPS
TDIGRNDFPE RFLRRTVLIF VDYPESYSLV TIYNALLEKS ALINQYKTII LNIVKASVKF
YQVLRENFKS STQGYVYTPR DLTRWLISFK NYAESYAETN NLSLIKVWYH EACRVLLDRL
VSQKECSWGM TELQKVIVTD FGEFEVSVIF EKQIIFTDIL KNGLEFLDFA SLRPKLESLY
KKFYSSHPNN TLVFVDETIT HILRFHRILN NSGMHALLQG SVGLGQKAVV EFVCWLNSFS
LFELQKNQTY SIEDFEDNLK SILILAGTTN CKACLAINES IAGVPGFLDL LNNLLTNSEV
SNFFDQNDWA EIKKNLNKLN EFQPLKFDSE ESVTEIFMNN VFQNLCVVFY VYTSADVDFQ
TNSLSPALLN RCTIDYYHSW DYHSMLQIAN EVLQETISLN ALDHDNPNLK NIKGSSIYDA
VAQAVVNTHT SIVWEFKHLG KTSYFSCLHF IRFLNTFCLI FGRDANKLSK EKSRIENGFK
KIKETSQGID KFKEALSDQQ NVLFSKTKTA NDRLQCIIQT KQAVEAKKVY SLQAEASLQK
KSFLLNEKKN SVMKEVSYAK PAVIEARKSV SDIKKAHLIE LRSLSRPPMA IRITMEVVCK
LLGFSATDWK NVQQLLKRDD FIPKILNYNL EKELSINLRR KIEQDYFSNP IFTFDSVNRA
SKACGPLLLW IKSICNYSKV LEKLEPLNSE VDRLKLEQKN AEECIQETIA ACKDLDEKLL
QLQEEYASMI SEIHSMELQM DEVKCKMQRS IEVITDLSIE RNEWSGFLNL YPKRMWNLVG
ESLMEASFVV YAGNLDPSMR IFLRNKCEPI ISSFGFPISK SAVRTNIERC VQTSIESKYY
KNLTDYSLEN IYIIQENKSP LLIIDPSSQI LDILPSLYKG KASDLISFSN KSFQNQIKLA
LLSGSAIIIK DAELWDVSIE PLLKPEFFTG SGEVQTTFAK DTITITLPLN IIFFSEVQSN
ELENKASKFM NVVNFTLSIS LLETQMLKSV ISVQEPGVFK QKDNCFTLKL SIERQIRSLQ
EQLLKTLCSS NENIVGTDEI VVLLKNLKEK HETIRLAYSE SQSINRKVDE LIRRYKLSIK
SFLSVVVVFQ HFISLKKSYS FSFNFIWSTF HQMLNVVLEN RNQDFKSLIM DALRDLIRRC
FLYIFPEDRV LFLFLLMFFF FPKETESLRK LLIVNGKTLE LEQSYLNFFE TCSDSNERGG
LESLFFKTHA SNIQNFCTEV LANTHCEEDC LKLLYDLWSS AFKVEFSNIK YDFLKIINDE
SESRMPTIVY LMENCEIDSL LQNAKIPQNI KKLTVSLGSA ENESLADSYL KLASTEPLWL
FINNIHLSTP WAEKLPSKMS NHLHKNSRIV CLSEIHNQLP HQLLCISRSI VFNKQTSFKN
NLLNLLELLP TMTHTLPHNR FRLFFFLSWL HATLAEIYCF TCSSWKEPCY FDDSDFYFGT
KILCNILYRN VHLEEFSWGT FKDLLLNVVY GPKVSASSDF IALDKILKRL IAQFKTQISS
NILLTDNFKF ILPYEITFSS AKEVIGQLPD EIPPGWLDIP ENSKRKRTDI YFSMCI
