ID   ALP11_SCHPO             Reviewed;         234 AA.
AC   Q10235; Q9UTM6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 140.
DE   RecName: Full=Cell polarity protein alp11;
DE   AltName: Full=Altered polarity protein 11;
GN   Name=alp11; ORFNames=SPAC13D6.05, SPAC4G9.01;
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], AND FUNCTION.
RX   PubMed=10905343; DOI=10.1007/s004380000252;
RA   Radcliffe P.A., Toda T.;
RT   "Characterisation of fission yeast alp11 mutants defines three functional
RT   domains within tubulin-folding cofactor B.";
RL   Mol. Gen. Genet. 263:752-760(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH ALPHA-TUBULIN
RP   AND ALP21, AND SUBCELLULAR LOCATION.
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   [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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Required for microtubule function and cell polarity. Involved
CC       in the proper folding of alpha-tubulin. {ECO:0000269|PubMed:10473641,
CC       ECO:0000269|PubMed:10905343}.
CC   -!- SUBUNIT: Binds to monomeric alpha-tubulin. Interacts with alp21.
CC       {ECO:0000269|PubMed:10473641}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:10473641}.
CC   -!- SIMILARITY: Belongs to the TBCB family. {ECO:0000305}.
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DR   EMBL; AB008750; BAA23375.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB59431.1; -; Genomic_DNA.
DR   PIR; T43283; T43283.
DR   RefSeq; NP_593683.2; NM_001019115.2.
DR   AlphaFoldDB; Q10235; -.
DR   SMR; Q10235; -.
DR   BioGRID; 279261; 3.
DR   STRING; 4896.SPAC13D6.05.1; -.
DR   iPTMnet; Q10235; -.
DR   MaxQB; Q10235; -.
DR   PaxDb; Q10235; -.
DR   EnsemblFungi; SPAC13D6.05.1; SPAC13D6.05.1:pep; SPAC13D6.05.
DR   GeneID; 2542814; -.
DR   KEGG; spo:SPAC13D6.05; -.
DR   PomBase; SPAC13D6.05; alp11.
DR   VEuPathDB; FungiDB:SPAC13D6.05; -.
DR   eggNOG; KOG3206; Eukaryota.
DR   HOGENOM; CLU_067577_2_0_1; -.
DR   InParanoid; Q10235; -.
DR   OMA; IGVKYDE; -.
DR   PhylomeDB; Q10235; -.
DR   PRO; PR:Q10235; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:PomBase.
DR   GO; GO:0007021; P:tubulin complex assembly; ISO:PomBase.
DR   Gene3D; 2.30.30.190; -; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF14560; Ubiquitin_2; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF74924; SSF74924; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..234
FT                   /note="Cell polarity protein alp11"
FT                   /id="PRO_0000083512"
FT   DOMAIN          4..88
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          174..216
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   234 AA;  26672 MW;  7E4D8B5C3D9D5981 CRC64;
     MNEITLFIKS SSANAERRIN PQWTVSQLKT KLVPIVGTPE QYQKLTYEPA SSTVPGHVFT
     SEEENLDLGE FKLQPLGTIV VEDTRPPHLR LDFDDLSQVD KYVMPREQYE NRTDSVYAWK
     KRNQLGRFNP DFEASKASRQ ESLKRELVDL QKNLNSRCCA AGERYGTIRY IGLVPEINND
     NLWVGVEFDE PVGKNDGTVS GKRYFNAKNK HGSFLRSSEV EVGDFPPEDI LEGL