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MOB2_DROPS
ID   MOB2_DROPS              Reviewed;         562 AA.
AC   Q2LZ59;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=MOB kinase activator-like 2;
DE   AltName: Full=Mob as tumor suppressor protein 2;
DE   AltName: Full=Mps one binder kinase activator-like 2;
GN   Name=Mob1 {ECO:0000250|UniProtKB:Q8IQG1}; ORFNames=GA11155;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Required for the normal morphogenesis of a variety of
CC       polarized outgrowths including epidermal hairs, bristles, arista
CC       laterals, and dendrites. {ECO:0000250|UniProtKB:Q8IQG1}.
CC   -!- SUBUNIT: Interacts with and activates trc, also interacts with wts.
CC       {ECO:0000250|UniProtKB:Q8IQG1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IQG1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8IQG1}. Note=Trc colocalizes with Mob1 to the
CC       cell periphery in wing cells and wing hairs.
CC       {ECO:0000250|UniProtKB:Q8IQG1}.
CC   -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000255}.
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DR   EMBL; CH379069; EAL29650.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LZ59; -.
DR   SMR; Q2LZ59; -.
DR   STRING; 7237.FBpp0275415; -.
DR   eggNOG; KOG0440; Eukaryota.
DR   HOGENOM; CLU_022966_0_0_1; -.
DR   InParanoid; Q2LZ59; -.
DR   OMA; MYLWFDE; -.
DR   ChiTaRS; Mob2; fly.
DR   Proteomes; UP000001819; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR   Gene3D; 1.20.140.30; -; 1.
DR   InterPro; IPR005301; MOB_kinase_act_fam.
DR   InterPro; IPR036703; MOB_kinase_act_sf.
DR   PANTHER; PTHR22599; PTHR22599; 1.
DR   Pfam; PF03637; Mob1_phocein; 1.
DR   SMART; SM01388; Mob1_phocein; 1.
DR   SUPFAM; SSF101152; SSF101152; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Nucleus; Reference proteome; RNA editing; Zinc.
FT   CHAIN           1..562
FT                   /note="MOB kinase activator-like 2"
FT                   /id="PRO_0000279702"
FT   REGION          30..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..510
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H8S9"
SQ   SEQUENCE   562 AA;  59585 MW;  3ABFC05309825A6A CRC64;
     MKETLSSKVP TTRTVGVTFD SVSESKSKLK SGSVQGTTAT ATATGPPSPP SSYVIKCLLK
     TARFMWQVTT IPAKIGDTLG TLYRYAQDSV DTFLCVAGKA RRKERDGDQN STDTKLYLEE
     SVLERKLPEA DLKALVDLPA GLDYNEWLAS HTLALFEHVN LVYGTISEFC TQSGCADMTG
     PGNRTYLWFD EKGKKTRVAA PQYIDYVMTF TQKTVSDESI FPTKYANEFP GSFESIARKI
     LRLQFHVIAH LYAAHFREIA LLGLHTHLNL TFAHLTALHR RFNLIDEKET DVLRDLEVAL
     RLTDDTSGQD SSSSVHEHSS SSSSPPVQHQ QHQHQQQHNN SSSTSNSTSP AEALHVNSQS
     NSNSHSNSSN SHTTTASASA SLIDGDSAAP PICTQPEAGA GCKPAGSSGL LGGILGDLTS
     GEFGDTTRYC TSAVPQAAAS SSASAAGPGA DGAASAALNN GAGALHLNFS NNNNNNHNLN
     HLNHHHHHHH HQHHHQHHPH GHHGHQGHQG HQGHHQAPAS TTVPHSGLIQ CNAAGAVGAS
     AGGGGNAVSA ATGGATSASS TA
 
 
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