NOD_DROME
ID NOD_DROME Reviewed; 666 AA.
AC P18105; Q9VYW9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Kinesin-like protein Nod;
GN Name=nod; Synonyms=NODA; ORFNames=CG1763;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=2144792; DOI=10.1016/0092-8674(90)90383-p;
RA Zhang P., Knowles B.A., Goldstein L.S.B., Hawley R.S.;
RT "A kinesin-like protein required for distributive chromosome segregation in
RT Drosophila.";
RL Cell 62:1053-1062(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP VARIANT ALLELE NOD(DTW).
RX PubMed=1743485; DOI=10.1093/genetics/129.2.409;
RA Rasooly R.S., New C.M., Zhang P., Hawley R.S., Baker B.S.;
RT "The lethal(1)TW-6cs mutation of Drosophila melanogaster is a dominant
RT antimorphic allele of nod and is associated with a single base change in
RT the putative ATP-binding domain.";
RL Genetics 129:409-422(1991).
CC -!- FUNCTION: Required for the distributive chromosome segregation of non-
CC exchange chromosomes during meiosis. May be a microtubule motor
CC required to hold distributively 'paired' chromosomes at the metaphase
CC plate until anaphase.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In adult female, found in meiotically active
CC ovaries.
CC -!- DEVELOPMENTAL STAGE: Embryonic, larval, and pupal stages. Only
CC expressed in female adults.
CC -!- MISCELLANEOUS: The nod(DTW) mutation is a cold-sensitive recessive
CC lethal mutation.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; M36195; AAA28653.1; -; Genomic_DNA.
DR EMBL; M94188; AAC14452.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48064.2; -; Genomic_DNA.
DR EMBL; AY050238; AAK84937.1; -; mRNA.
DR PIR; A36026; A36026.
DR RefSeq; NP_001285129.1; NM_001298200.1.
DR RefSeq; NP_511125.2; NM_078570.3.
DR PDB; 3DC4; X-ray; 1.90 A; A=1-318.
DR PDB; 3DCB; X-ray; 2.50 A; A=1-318.
DR PDB; 3DCO; EM; 1.90 A; N=1-318.
DR PDB; 3PXN; X-ray; 2.60 A; A=1-322.
DR PDBsum; 3DC4; -.
DR PDBsum; 3DCB; -.
DR PDBsum; 3DCO; -.
DR PDBsum; 3PXN; -.
DR AlphaFoldDB; P18105; -.
DR SMR; P18105; -.
DR BioGRID; 58516; 7.
DR DIP; DIP-22708N; -.
DR IntAct; P18105; 1.
DR STRING; 7227.FBpp0073363; -.
DR PaxDb; P18105; -.
DR DNASU; 32107; -.
DR EnsemblMetazoa; FBtr0073516; FBpp0073363; FBgn0002948.
DR EnsemblMetazoa; FBtr0340297; FBpp0309258; FBgn0002948.
DR GeneID; 32107; -.
DR KEGG; dme:Dmel_CG1763; -.
DR CTD; 32107; -.
DR FlyBase; FBgn0002948; nod.
DR VEuPathDB; VectorBase:FBgn0002948; -.
DR eggNOG; KOG0244; Eukaryota.
DR HOGENOM; CLU_371847_0_0_1; -.
DR InParanoid; P18105; -.
DR OMA; EAPFRSF; -.
DR OrthoDB; 274914at2759; -.
DR PhylomeDB; P18105; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR BioGRID-ORCS; 32107; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; P18105; -.
DR GenomeRNAi; 32107; -.
DR PRO; PR:P18105; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0002948; Expressed in secondary oocyte and 35 other tissues.
DR ExpressionAtlas; P18105; baseline and differential.
DR Genevisible; P18105; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IMP:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:FlyBase.
DR GO; GO:0032837; P:distributive segregation; IMP:FlyBase.
DR GO; GO:0051296; P:establishment of meiotic spindle orientation; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:FlyBase.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP:FlyBase.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..666
FT /note="Kinesin-like protein Nod"
FT /id="PRO_0000125426"
FT DOMAIN 8..320
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 423..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 639..666
FT /evidence="ECO:0000255"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT VARIANT 94
FT /note="S -> N (in allele NOD(DTW))"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3DC4"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3DCB"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:3DC4"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:3DC4"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3DC4"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:3DC4"
SQ SEQUENCE 666 AA; 73908 MW; E3DEF72C08973FC2 CRC64;
MEGAKLSAVR IAVREAPYRQ FLGRREPSVV QFPPWSDGKS LIVDQNEFHF DHAFPATISQ
DEMYQALILP LVDKLLEGFQ CTALAYGQTG TGKSYSMGMT PPGEILPEHL GILPRALGDI
FERVTARQEN NKDAIQVYAS FIEIYNEKPF DLLGSTPHMP MVAARCQRCT CLPLHSQADL
HHILELGTRN RRVRPTNMNS NSSRSHAIVT IHVKSKTHHS RMNIVDLAGS EGVRRTGHEG
VARQEGVNIN LGLLSINKVV MSMAAGHTVI PYRDSVLTTV LQASLTAQSY LTFLACISPH
QCDLSETLST LRFGTSAKKL RLNPMQVARQ KQSLAARTTH VFRQALCTST AIKSNAANHN
SIVVPKSKYS TTKPLSAVLH RTRSELGMTP KAKKRARELL ELEETTLELS SIHIQDSSLS
LLGFHSDSDK DRHLMPPPTG QEPRQASSQN STLMGIVEET EPKESSKVQQ SMVAPTVPTT
VRCQLFNTTI SPISLRASSS QRELSGIQPM EETVVASPQQ PCLRRSVRLA SSMRSQNYGA
IPKVMNLRRS TRLAGIREHA TSVVVKNETD AIPHLRSTVQ KKRTRNVKPA PKAWMANNTK
CFLDLLNNGN VKQLQEIPGI GPKSAFSLAL HRSRLGCFEN LFQVKSLPIW SGNKWERFCQ
INCLDT
