MAL3_SCHPO
ID MAL3_SCHPO Reviewed; 308 AA.
AC Q10113;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Microtubule integrity protein mal3;
GN Name=mal3; ORFNames=SPAC18G6.15;
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].
RX PubMed=9348288; DOI=10.1083/jcb.139.3.717;
RA Beinhauer J.D., Hagan I.M., Hegemann J.H., Fleig U.;
RT "Mal3, the fission yeast homologue of the human APC-interacting protein EB-
RT 1 is required for microtubule integrity and the maintenance of cell form.";
RL J. Cell Biol. 139:717-728(1997).
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).
RN [3]
RP FUNCTION, INTERACTION WITH TEA2, AND SUBCELLULAR LOCATION.
RX PubMed=15177031; DOI=10.1016/j.devcel.2004.05.008;
RA Busch K.E., Hayles J., Nurse P., Brunner D.;
RT "Tea2p kinesin is involved in spatial microtubule organization by
RT transporting tip1p on microtubules.";
RL Dev. Cell 6:831-843(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH TEA2.
RX PubMed=15665379; DOI=10.1074/jbc.m413620200;
RA Browning H., Hackney D.D.;
RT "The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by
RT recruiting it to the microtubule.";
RL J. Biol. Chem. 280:12299-12304(2005).
CC -!- FUNCTION: May play a role in regulating the integrity of microtubules
CC possibly by influencing their stability. Involved in an anchoring
CC mechanism to maintain tea2 and tip1 at growing microtubule ends.
CC Strongly stimulates the ATPase activity of tea2.
CC {ECO:0000269|PubMed:15177031, ECO:0000269|PubMed:15665379}.
CC -!- SUBUNIT: Interacts with tea2. {ECO:0000269|PubMed:15177031,
CC ECO:0000269|PubMed:15665379}.
CC -!- INTERACTION:
CC Q10113; O42874: peg1; NbExp=4; IntAct=EBI-1002268, EBI-1112382;
CC Q10113; O59757: spc7; NbExp=2; IntAct=EBI-1002268, EBI-1002205;
CC Q10113; Q1MTQ1: tea2; NbExp=3; IntAct=EBI-1002268, EBI-1107767;
CC Q10113; P79065: tip1; NbExp=3; IntAct=EBI-1002268, EBI-1102463;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15177031}. Note=Associated with microtubules.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR EMBL; Y09518; CAA70707.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA92392.1; -; Genomic_DNA.
DR PIR; T43413; T43413.
DR RefSeq; NP_593678.1; NM_001019110.2.
DR PDB; 4ABO; EM; 8.60 A; I=2-142.
DR PDB; 5M97; X-ray; 1.33 A; A/B=174-247.
DR PDB; 5M9E; X-ray; 2.83 A; A/B/C/D=174-247.
DR PDB; 5MJS; EM; 4.60 A; D=1-143.
DR PDBsum; 4ABO; -.
DR PDBsum; 5M97; -.
DR PDBsum; 5M9E; -.
DR PDBsum; 5MJS; -.
DR AlphaFoldDB; Q10113; -.
DR SMR; Q10113; -.
DR BioGRID; 278599; 136.
DR DIP; DIP-35342N; -.
DR IntAct; Q10113; 9.
DR MINT; Q10113; -.
DR STRING; 4896.SPAC18G6.15.1; -.
DR iPTMnet; Q10113; -.
DR MaxQB; Q10113; -.
DR PaxDb; Q10113; -.
DR PRIDE; Q10113; -.
DR EnsemblFungi; SPAC18G6.15.1; SPAC18G6.15.1:pep; SPAC18G6.15.
DR GeneID; 2542123; -.
DR KEGG; spo:SPAC18G6.15; -.
DR PomBase; SPAC18G6.15; mal3.
DR VEuPathDB; FungiDB:SPAC18G6.15; -.
DR eggNOG; KOG3000; Eukaryota.
DR HOGENOM; CLU_041744_2_1_1; -.
DR InParanoid; Q10113; -.
DR OMA; EQCGTGG; -.
DR PhylomeDB; Q10113; -.
DR PRO; PR:Q10113; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000235; C:astral microtubule; IDA:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0055028; C:cortical microtubule; IDA:PomBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:PomBase.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IDA:PomBase.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005880; C:nuclear microtubule; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IMP:PomBase.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0099609; F:microtubule lateral binding; IDA:PomBase.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:PomBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IMP:PomBase.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0035372; P:protein localization to microtubule; IDA:PomBase.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; IDA:PomBase.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR036133; EB1_C_sf.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF03271; EB1; 1.
DR SUPFAM; SSF140612; SSF140612; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51230; EB1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..308
FT /note="Microtubule integrity protein mal3"
FT /id="PRO_0000213431"
FT DOMAIN 2..103
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 173..247
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 117..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 177..220
FT /evidence="ECO:0007829|PDB:5M97"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:5M97"
SQ SEQUENCE 308 AA; 35094 MW; 9527D31CAA024256 CRC64;
MSESRQELLA WINQVTSLGL TRIEDCGKGY AMIQIFDSIY QDIPLKKVNF ECNNEYQYIN
NWKVLQQVFL KKGIDKVVDP ERLSRCKMQD NLEFVQWAKR FWDQYYPGGD YDALARRGNR
GPANTRVMNS SAGATGPSRR RQVSSGSSTP SMTKSSANNN NVSSTANTAA VLRAKQAQQQ
ITSLETQLYE VNETMFGLER ERDFYFNKLR EIEILVQTHL TTSPMSMENM LERIQAILYS
TEDGFELPPD QPADLTTALT DHDTNNVAEE AQMTDLKDSE TQRVPSAPDF VHARLQSLEV
DDDENITF