MA205_DROME
ID MA205_DROME Reviewed; 1185 AA.
AC P23226; Q53YG1; Q9V9S1;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=205 kDa microtubule-associated protein;
GN Name=Map205; ORFNames=CG1483;
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 [MRNA] (ISOFORM B3).
RC TISSUE=Embryo;
RX PubMed=1703540; DOI=10.1083/jcb.111.6.2563;
RA Irminger-Finger I., Laymon R.A., Goldstein L.S.B.;
RT "Analysis of the primary sequence and microtubule-binding region of the
RT Drosophila 205K MAP.";
RL J. Cell Biol. 111:2563-2572(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] (ISOFORM B3).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354; THR-721; SER-728;
RP SER-1075 AND SER-1121, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; TYR-450; SER-709;
RP SER-710; SER-712; SER-874 AND SER-1086, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: May play an important role in the regulation of microtubule
CC assembly and interaction.
CC -!- INTERACTION:
CC P23226; Q4KMI8: plk1; Xeno; NbExp=2; IntAct=EBI-239813, EBI-16066720;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC spindle. Note=Associated with cytoplasmic microtubules and with the
CC mitotic spindle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=J5;
CC IsoId=P23226-1; Sequence=Displayed;
CC Name=C2;
CC IsoId=P23226-2; Sequence=VSP_004319, VSP_004320, VSP_004321;
CC Name=B3; Synonyms=A;
CC IsoId=P23226-3; Sequence=VSP_004319;
CC -!- MISCELLANEOUS: Phosphorylation of various serine residues may play a
CC regulatory role. The basic domain contains numerous sequences that
CC match known consensus sequences of several different protein kinases.
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DR EMBL; X54061; CAA37996.1; -; mRNA.
DR EMBL; AE014297; AAF57214.1; -; Genomic_DNA.
DR EMBL; BT003276; AAO25033.1; -; mRNA.
DR PIR; A36685; A36685.
DR RefSeq; NP_524615.1; NM_079876.3. [P23226-3]
DR PDB; 4J7B; X-ray; 2.30 A; C/F=276-325.
DR PDBsum; 4J7B; -.
DR AlphaFoldDB; P23226; -.
DR SMR; P23226; -.
DR BioGRID; 68603; 18.
DR DIP; DIP-60545N; -.
DR ELM; P23226; -.
DR IntAct; P23226; 38.
DR STRING; 7227.FBpp0085235; -.
DR iPTMnet; P23226; -.
DR PaxDb; P23226; -.
DR PeptideAtlas; P23226; -.
DR PRIDE; P23226; -.
DR DNASU; 43765; -.
DR EnsemblMetazoa; FBtr0085875; FBpp0085234; FBgn0002645. [P23226-3]
DR EnsemblMetazoa; FBtr0334299; FBpp0306414; FBgn0002645. [P23226-2]
DR GeneID; 43765; -.
DR KEGG; dme:Dmel_CG1483; -.
DR CTD; 43765; -.
DR FlyBase; FBgn0002645; Map205.
DR VEuPathDB; VectorBase:FBgn0002645; -.
DR eggNOG; ENOG502SE79; Eukaryota.
DR InParanoid; P23226; -.
DR OMA; EEYAAFN; -.
DR SignaLink; P23226; -.
DR BioGRID-ORCS; 43765; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43765; -.
DR PRO; PR:P23226; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002645; Expressed in wing disc and 42 other tissues.
DR ExpressionAtlas; P23226; baseline and differential.
DR Genevisible; P23226; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1185
FT /note="205 kDa microtubule-associated protein"
FT /id="PRO_0000084542"
FT REGION 146..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..977
FT /note="Microtubule-binding"
FT /evidence="ECO:0000255"
FT REGION 856..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 450
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 721
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1075
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 557..578
FT /note="Missing (in isoform B3 and isoform C2)"
FT /evidence="ECO:0000303|PubMed:1703540, ECO:0000303|Ref.4"
FT /id="VSP_004319"
FT VAR_SEQ 650..703
FT /note="Missing (in isoform C2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004320"
FT VAR_SEQ 704
FT /note="D -> N (in isoform C2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004321"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4J7B"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:4J7B"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4J7B"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:4J7B"
SQ SEQUENCE 1185 AA; 126669 MW; 47B422E2CEE03F70 CRC64;
MEHHEDNAQL DNYLQNRLAE SLQICGGAGE HNPHLADATG GNGCAPGIAP SKSDEVDGEE
DEEWKYIHEV RQSEKLQQEK LPLTKETGNG FGPGRDSDNQ VHGNGAAAVF NLYEEDVEVI
KNDGDFSTNS NTTTSTDEVV ARQAQEPNQL PEQLQQQQQI ESQGVHEDPR QEDEDEHSSV
ATTYGTSSLS ENNSSPLDQE EVVMVAQTVG QEQLVDFDNK ENSYFVKNLE ENHSQLNPNA
VAFVPGVGSQ SSSPLPAAED PLPGVQPRPF LPGGTLDDLV AESPRKEFAR INMDGIAVPD
EREFDIEADM RPHELEQESD TFGAGHLEMQ LLNGIGTADQ AALRDVLDHG PETSVDMELP
LDQVPNDADI MKQSIYAEHN SSIEDILNSV QPLPIQTCDD KELIHVEEKE HVSKSPSTEE
LQFQSDFPNN QESHTLFNNT EQDPMQASFY LEHTSQKAQE GCQEQMQLPA ECSDIFADQS
LLLDTSAPQL SSEADSPVAK LELESQQAGI VDITPSPLSS TAEKHLVEDT KELVEEYTLD
PESHFFGVVS SQAPLQLFGK HTLPSIIHSC KHRVASEQND EENAVFESVS GYETQNFDEI
SSPPEGINPF AQPFTPAHLV IEQANTMMED VGGMPIPASE DFAICDKVAS KSSNEVEDHR
SEQQAFVKEE LLHPVGDVVA QVENLGTEKN FVVEEERLPI SVSDEIPLSS ASKEKLLPDT
TDEQLLTSAL EEKLRSVAPE ESVSTAADGQ SISQFDEYVI ASNKPLEDIL EPEKDVEVAK
SLSEKTSVAT VAGGAVVGAT KTHSATKAGS TAASAKSKTE TLVMKKTTAS STSVYGANKS
AAPRPSTARL GIKSTSIATK TSTTSSLTGN PRKSLSSNVG STVKPPTKLS GTRPATAPVS
KVTLGAKTIT NKPTASGTAS DNVTRTTLRP LVSTNARRPA TSGTGSVASS TARRPVTNAK
GSAPGSAAST KVRPAATMTA PVKPKVLSPR STISSTTTVR KVPSTSTPSF STRSPNKQQS
NGLGKNTSST TTSTATATIT KSFTARSAPK FTHSASLTYN NGSTSRRLLV PGSSSTTTTS
SLRKSSPLKA APGKAASKPL TPQSKDGTAK SSPAVLKARN STLMGGEGVA PSNECVPTPN
GQINAEEVVK LKGKGLAEEV KIIEEQKLHE QDVPAHNAEV PLLDF
