ALP21_SCHPO
ID ALP21_SCHPO Reviewed; 511 AA.
AC Q10303;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Cell polarity protein alp21;
DE AltName: Full=Altered polarity protein 21;
DE AltName: Full=Suppressor of tsm one protein 1;
GN Name=alp21; Synonyms=sto1; ORFNames=SPAC22H10.10;
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], DOMAINS LEUCINE-RICH REPEATS, AND
RP INTERACTION WITH ALP1 AND ALP11.
RX PubMed=10473641; DOI=10.1091/mbc.10.9.2987;
RA Radcliffe P.A., Hirata D., Vardy L., Toda T.;
RT "Functional dissection and hierarchy of tubulin-folding cofactor homologues
RT in fission yeast.";
RL Mol. Biol. Cell 10:2987-3001(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10341216; DOI=10.1242/jcs.112.12.1979;
RA Grishchuk E.L., McIntosh J.R.;
RT "Sto1p, a fission yeast protein similar to tubulin folding cofactor E,
RT plays an essential role in mitotic microtubule assembly.";
RL J. Cell Sci. 112:1979-1988(1999).
RN [3]
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).
CC -!- FUNCTION: Required for microtubule and spindle assembly. Involved in
CC the proper folding of alpha-tubulin. {ECO:0000269|PubMed:10341216}.
CC -!- SUBUNIT: Interacts with alp1 and alp11. {ECO:0000269|PubMed:10473641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10341216}.
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DR EMBL; AB008749; BAA23374.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93613.1; -; Genomic_DNA.
DR PIR; T43282; T43282.
DR RefSeq; NP_593747.1; NM_001019178.2.
DR AlphaFoldDB; Q10303; -.
DR SMR; Q10303; -.
DR BioGRID; 278338; 7.
DR STRING; 4896.SPAC22H10.10.1; -.
DR MaxQB; Q10303; -.
DR PaxDb; Q10303; -.
DR PRIDE; Q10303; -.
DR EnsemblFungi; SPAC22H10.10.1; SPAC22H10.10.1:pep; SPAC22H10.10.
DR GeneID; 2541847; -.
DR KEGG; spo:SPAC22H10.10; -.
DR PomBase; SPAC22H10.10; alp21.
DR VEuPathDB; FungiDB:SPAC22H10.10; -.
DR eggNOG; KOG3207; Eukaryota.
DR HOGENOM; CLU_584163_0_0_1; -.
DR InParanoid; Q10303; -.
DR OMA; VFERTKW; -.
DR PhylomeDB; Q10303; -.
DR PRO; PR:Q10303; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990727; C:tubulin folding cofactor complex; NAS:PomBase.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; NAS:PomBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR PANTHER; PTHR15140; PTHR15140; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Cytoskeleton; Leucine-rich repeat; Microtubule;
KW Reference proteome; Repeat.
FT CHAIN 1..511
FT /note="Cell polarity protein alp21"
FT /id="PRO_0000064569"
FT REPEAT 116..137
FT /note="LRR 1"
FT REPEAT 142..163
FT /note="LRR 2"
FT REPEAT 168..190
FT /note="LRR 3"
FT REPEAT 191..217
FT /note="LRR 4"
FT REPEAT 218..241
FT /note="LRR 5"
FT REPEAT 242..264
FT /note="LRR 6"
FT REPEAT 267..288
FT /note="LRR 7"
FT REPEAT 291..312
FT /note="LRR 8"
FT DOMAIN 325..364
FT /note="LRRCT"
SQ SEQUENCE 511 AA; 58591 MW; B6FD84864AD648B6 CRC64;
MHISTGMVRA SISNTLVTLT IEGNNDRYQV ILDKNVNAKQ FVKTCWRNKK PLIVKEGKIF
VDKGFPFDPC RTFLEALYEK YSYSSPLPSS VEFKSGKQVE FCGFEKIQSK QRDLKSLRVI
ILDNYRIEDI EIEYEYSKIL PEVIDLDLSR NLFHEFFPIL KLCSQLPSLR NLTLDSNLFS
NFISSNTVLL IPHLTQLSVN GCGLNSKDVQ WITETFPSLE VLYLEANEII LSKATSFKNL
QFLQTLSLAN NLNLYSADGY AVDVFQGINN LNLSSTSLAD VAELPVHTLH KLTFLDISEN
NIRDIRSLDH LRTLENLKHL RITLSYFNKP TDIAKLLVIA RIPSLVKLND VNISPNERLD
AELYYTSCIR KLVIDNEIKD VEELTKIEPF WEEIWKSHEL PSIQFHLEAS INDWTSGILK
NRITKGIKIS SINSGATMLL KLHYNWKLLD IKALISYHFA IPVHTSTFVF ASSERDVSFS
PKTVRDDQKR LFELPFTCTF IDVYAKESGN V