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THR_DROME
ID   THR_DROME               Reviewed;        1379 AA.
AC   P42286; Q8MQL8; Q94525; Q9V894;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein three rows;
GN   Name=thr; ORFNames=CG5785;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R;
RX   PubMed=8270646; DOI=10.1242/jcs.106.1.87;
RA   Philp A.V., Axton J.M., Saunders R.D.C., Glover D.M.;
RT   "Mutations in the Drosophila melanogaster gene three rows permit aspects of
RT   mitosis to continue in the absence of chromatid segregation.";
RL   J. Cell Sci. 106:87-98(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8270646.
RA   Philp A.V., Axton J.M., Saunders R.D., Glover D.M.;
RL   J. Cell Sci. 107:1102-1102(1994).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-1209.
RC   STRAIN=Canton-S, and Oregon-R;
RX   PubMed=8305737; DOI=10.1091/mbc.4.11.1161;
RA   D'Andrea R.J., Stratmann R., Lehner C.F., John U.P., Saint R.;
RT   "The three rows gene of Drosophila melanogaster encodes a novel protein
RT   that is required for chromosome disjunction during mitosis.";
RL   Mol. Biol. Cell 4:1161-1174(1993).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=9927461; DOI=10.1093/genetics/151.2.685;
RA   Liu X., Kiss I., Lengyel J.A.;
RT   "Identification of genes controlling malpighian tubule and other epithelial
RT   morphogenesis in Drosophila melanogaster.";
RL   Genetics 151:685-695(1999).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH PIM AND SSE.
RX   PubMed=11581162; DOI=10.1101/gad.207301;
RA   Jager H., Herzig A., Lehner C.F., Heidmann S.;
RT   "Drosophila separase is required for sister chromatid separation and binds
RT   to PIM and THR.";
RL   Genes Dev. 15:2572-2584(2001).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-1035.
RX   PubMed=12231632; DOI=10.1101/gad.242202;
RA   Herzig A., Lehner C.F., Heidmann S.;
RT   "Proteolytic cleavage of the THR subunit during anaphase limits Drosophila
RT   separase function.";
RL   Genes Dev. 16:2443-2454(2002).
CC   -!- FUNCTION: Required specifically for chromosome disjunction during all
CC       mitoses; maternally provided protein is sufficient until mitosis 14
CC       then zygotic protein is required. Involved in formation and/or
CC       maintenance of epithelial structures: bud extension during Malpighian
CC       tubule development, and foregut and hindgut morphogenesis.
CC       {ECO:0000269|PubMed:11581162, ECO:0000269|PubMed:12231632,
CC       ECO:0000269|PubMed:8270646, ECO:0000269|PubMed:9927461}.
CC   -!- SUBUNIT: Interacts with pim and Sse. Cleavage of thr contributes to
CC       inactivation of Sse. {ECO:0000269|PubMed:11581162}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12231632}.
CC       Note=Cytoplasmic during interphase and distributed throughout the cell
CC       during early mitosis.
CC   -!- TISSUE SPECIFICITY: During embryogenesis, expressed in Malpighian
CC       tubule buds, and epithelia of foregut and hindgut.
CC       {ECO:0000269|PubMed:9927461}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:8270646}.
CC   -!- PTM: Proteolytically cleaved after the metaphase-to-anaphase
CC       transition, C-terminal cleavage product is degraded. Cleavage can only
CC       proceed within complexes that contain active Sse.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB29824.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAB60210.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAM75095.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA53148.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA53148.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; X75374; CAA53148.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE013599; AAF57778.3; -; Genomic_DNA.
DR   EMBL; AY128502; AAM75095.1; ALT_FRAME; mRNA.
DR   EMBL; U03276; AAB60210.1; ALT_FRAME; Unassigned_DNA.
DR   EMBL; S69585; AAB29824.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A49440; A49440.
DR   RefSeq; NP_001286552.1; NM_001299623.1.
DR   RefSeq; NP_725731.2; NM_166257.2.
DR   AlphaFoldDB; P42286; -.
DR   BioGRID; 62727; 7.
DR   IntAct; P42286; 1.
DR   STRING; 7227.FBpp0086004; -.
DR   PaxDb; P42286; -.
DR   PRIDE; P42286; -.
DR   GeneID; 37042; -.
DR   KEGG; dme:Dmel_CG5785; -.
DR   CTD; 37042; -.
DR   FlyBase; FBgn0003701; thr.
DR   VEuPathDB; VectorBase:FBgn0003701; -.
DR   eggNOG; ENOG502T8T7; Eukaryota.
DR   HOGENOM; CLU_255337_0_0_1; -.
DR   InParanoid; P42286; -.
DR   BioGRID-ORCS; 37042; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 37042; -.
DR   PRO; PR:P42286; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   ExpressionAtlas; P42286; baseline and differential.
DR   Genevisible; P42286; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007502; P:digestive tract mesoderm development; IMP:FlyBase.
DR   GO; GO:0007440; P:foregut morphogenesis; IMP:FlyBase.
DR   GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR   GO; GO:0008258; P:head involution; IMP:FlyBase.
DR   GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR   GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; TAS:FlyBase.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IMP:FlyBase.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Developmental protein; Mitosis;
KW   Reference proteome.
FT   CHAIN           1..1379
FT                   /note="Protein three rows"
FT                   /id="PRO_0000072526"
FT   REGION          1031..1037
FT                   /note="Separase cleavage-site"
FT   REGION          1206..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1248..1309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1328..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1248..1270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1285..1307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         392
FT                   /note="S -> T (in strain: Berkeley and Oregon-R)"
FT   VARIANT         427
FT                   /note="R -> K (in strain: Berkeley and Oregon-R)"
FT   VARIANT         428
FT                   /note="A -> T (in strain: Berkeley and Oregon-R)"
FT   VARIANT         927
FT                   /note="L -> P (in strain: Canton-S)"
FT   MUTAGEN         1035
FT                   /note="R->D: Abolishes proteolytic cleavage."
FT                   /evidence="ECO:0000269|PubMed:12231632"
FT   CONFLICT        18
FT                   /note="K -> N (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="A -> P (in Ref. 1 and 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="G -> A (in Ref. 5; AAM75095)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315
FT                   /note="H -> N (in Ref. 5; AAM75095)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="S -> L (in Ref. 5; AAM75095)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365
FT                   /note="E -> D (in Ref. 3; AAF57778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="S -> N (in Ref. 5; AAM75095)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="K -> N (in Ref. 1 and 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        630
FT                   /note="K -> M (in Ref. 5; AAM75095)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        633
FT                   /note="I -> M (in Ref. 5; AAM75095)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        718
FT                   /note="D -> S (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        756
FT                   /note="E -> Q (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        915
FT                   /note="N -> S (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        938
FT                   /note="C -> S (in Ref. 6; AAB60210/AAB29824)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1019
FT                   /note="S -> R (in Ref. 3; AAF57778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1105
FT                   /note="E -> D (in Ref. 3; AAF57778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1113
FT                   /note="N -> S (in Ref. 3; AAF57778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1214
FT                   /note="T -> I (in Ref. 3; AAF57778)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1379 AA;  157511 MW;  5716E099FA05D5DB CRC64;
     MSTDIATQLK GSRSDVEKVR KTVEAKFREL SGDGLPLRYE VNVLRHICLA LKDNLHQNSD
     LYCDIMGIML PRVVPCEEKP SLWEAHLSSL RYIHHGLFHQ RSIEACQKLY NLIRQQPCRL
     QEESDYKIYL DIHLTHFNGF HVLLQKQKLP LEATSQLCYA LESLGDLFAA MTQRQISLCA
     TLLVQLNESL FGKRSRSFFK SLSFLPSESL AKMFNALLML LASSTSSNLA NLFPECLSLT
     LALVQIDMFS PQSNQQMSLQ LLRMSKELFR QESNLCYALQ LMYYYIKLIF VREPTGDFKR
     TYIDLSSKFQ HFFEHKVASH AKEQWLADFL VAIQLLQVLI HQSNSKLQSP FQIFWQQFDG
     ESSPEIYTAH FQLLQTCASL AVNITRSPLG CSCSHEACKS VRRHCILAYG LCALDAYINW
     KPAAEQRANV SPHKPLLGVV KYSMDVAKTM KCLGPTSVEI IKLVRQLTYV ADQVTCPEQM
     SVLLPLLEPL QKLRPLVADQ DMSSLLRRLF KASSHCGDSN IACRIQASYL ASITNPARLR
     SQVCLYYHNL GKKGTEIKRC VYEWHESTPL PFPLTPDQKK QLYDTDFFAL LHYLRSPSTA
     HMESLIRCRT SDYHLVLLAR QMRKDDSISK KCIEVHDKLR QQRSLSRMDN LCLGHASVGL
     LLDALEAQKT KVSTKEITEN MFEELLLSKN LWQMNIQREQ RLVNYASEAI SAFSNFFDRA
     DQEPLSANET SIDWEALIDD AIATANALSS MGYQSEEDDA WLLLLRMGRL LEDRFTYLRA
     LNHFLSQNEV SSRLNLKLGE EVEVAEELLD DLWPQLKNGK FFKRQQTTVM LCFCHLASYY
     ARMECYSHAQ LLLLHVEQLR EEFPERQGKS DIVLLTLQTV RFRIGYQQRK PTNCRLPTPL
     RQLDILLDNV RSFCNLSSLD GGSLQLLLST LVRESTECSA NRLSERLSFS NIALHLVLQS
     GLALRAIEVF LAWLWTNLQM ESFDKAQSKL RLIEHCLGIK QLNPTSRPEK EAIKDVAISD
     LASNMHLLQL VEPIRKQQLL NMASPNLLKM RPHSPNPQLD LDRYITLDVA PANLRENSQL
     QCLYFVTGCL HARLRFLQRN SEQLEEFYGR AHNWMQEKPP MSSALYPMLH AQQLYHLNYL
     RFARKHVEAI STAQLGLKMR SRAVDINFEY NFLAQLKTAQ LELKPVGQDK PQVKILRRAL
     VFNHSPEDKK RTATGSVSAV KNTASKVKQS AKKAPRFRIY EELELRPPSA TSCSSSGGSG
     TENTPPSDHV DLNACQAIEI SDDDDSPLVS TKKTQPKSRE KAKPKATSKA CKVLTLDNSL
     EIVETPTITT STRSTRARLR QPVETPKTAT LSSKRTRRQV LEAQAPETES ISTRTRHRH
 
 
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