ALP1_SCHPO
ID ALP1_SCHPO Reviewed; 1105 AA.
AC Q10197; P78749;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Tubulin-folding cofactor D;
DE AltName: Full=Altered polarity protein 1;
GN Name=alp1; ORFNames=SPBC11C11.04c;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / HM123;
RX PubMed=9450991; DOI=10.1093/emboj/17.3.658;
RA Hirata D., Masuda H., Eddison M., Toda T.;
RT "Essential role of tubulin-folding cofactor D in microtubule assembly and
RT its association with microtubules in fission yeast.";
RL EMBO J. 17:658-666(1998).
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP INTERACTION WITH ALP21.
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).
CC -!- FUNCTION: Has a function in the folding of beta-tubulin. Microtubule-
CC associated protein that is essential to direct polarized cell growth
CC and to position the nucleus and septum to the center of the cell during
CC mitosis. {ECO:0000269|PubMed:9450991}.
CC -!- SUBUNIT: Interacts with alp21. {ECO:0000269|PubMed:10473641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9450991}. Note=Microtubule-associated.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA71193.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y10106; CAA71193.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CU329671; CAA20686.2; -; Genomic_DNA.
DR PIR; T39319; S67381.
DR RefSeq; NP_596393.2; NM_001022314.2.
DR AlphaFoldDB; Q10197; -.
DR BioGRID; 276224; 8.
DR STRING; 4896.SPBC11C11.04c.1; -.
DR MaxQB; Q10197; -.
DR PaxDb; Q10197; -.
DR PRIDE; Q10197; -.
DR EnsemblFungi; SPBC11C11.04c.1; SPBC11C11.04c.1:pep; SPBC11C11.04c.
DR GeneID; 2539669; -.
DR KEGG; spo:SPBC11C11.04c; -.
DR PomBase; SPBC11C11.04c; alp1.
DR VEuPathDB; FungiDB:SPBC11C11.04c; -.
DR eggNOG; KOG1943; Eukaryota.
DR HOGENOM; CLU_280203_0_0_1; -.
DR InParanoid; Q10197; -.
DR OMA; EPHEAWH; -.
DR PRO; PR:Q10197; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990727; C:tubulin folding cofactor complex; NAS:PomBase.
DR GO; GO:0048487; F:beta-tubulin binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; EXP:PomBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:PomBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033162; TBCD.
DR InterPro; IPR022577; Tubulin_specific_chaperoneD_C.
DR PANTHER; PTHR12658; PTHR12658; 1.
DR Pfam; PF12612; TFCD_C; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Cytoskeleton; Glycoprotein; Microtubule;
KW Reference proteome; Repeat.
FT CHAIN 1..1105
FT /note="Tubulin-folding cofactor D"
FT /id="PRO_0000064568"
FT REPEAT 308..345
FT /note="HEAT 1"
FT REPEAT 347..385
FT /note="HEAT 2"
FT REPEAT 401..446
FT /note="HEAT 3"
FT REPEAT 452..489
FT /note="HEAT 4"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 883
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 988..1001
FT /note="Missing (in Ref. 2; CAA20686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1105 AA; 126274 MW; 437AF21F25DE60E7 CRC64;
MEEEESLEGI ISIDESLITS RLSQILDDVL DDRSSSHSVE KLKDVAVKYL QFCQFQPTLL
DKLLSKYVPN LASYLLKVKN IGKCNSITVI LYQFCKIRGY KAVRVLFPVG VQYIKELYTL
LNESSNNTWH FHYIVLLWLS QALNTPFPLN SLDDSLDVKK TIYTIAIKYL ENSGIDKEAS
CLVLSRLFSR DDGLDLLLGF LHHCESSWFK RSIFYKIGCL FSLSSFLKIC PRNDCLQTVD
VAFQFLNVAR EDLVGQENSA LRKLLCKCYT RLGIVLLPVN SSPNWKYSIS NPDSFFQLPD
DSNEEVHIYL EVIVDFLLSS VSDIDSFVRW SAAKGLAKII SRLPWNLAEQ VIDAIIELMT
ENMFLNPIEN TVNISITSPL VWHGAILFFA KLAGAGLIKY SKCLHILPLI EVGLSYEVRY
GTRVTGQSIR DASCYFVWSF YHCYSKSAIE GLQTNLILCL LQTVLFDNEI NVRRAATAAL
FEVIGRHASI PDGLSLISHI NYVSVTDISN CYGDLCMKVA HFPQFRSCVF QRLFTNLQHW
DVKVQQLSAF SLRQLSIKYP KELSIYLPPI LDYLSVGNAD FIFGYTIGLA SIIGGFLSIS
FPFDINRIHD LLSHKNLLSL KKFSRQQQTK IILGILKGIQ QIFANDIRVD RAFFSEAFSV
IIAAIDLQEE TIIKDISDAY SVLVKFDDME ETLEVLLDYI RKCSTSKEAR IVYIILQNLP
NISFRYQKKI CKLLLDIYPQ LHSIDYQAPV ANALQNIIPF TYEKTESIEE FVKELLQVCS
NYLTDTRGDV GSWIRKPAMK AISSLLVKDS SGKKLSEDIV WCCISYIIRQ TFDKIDSLRG
LAYQALEQIR VHYLIRRCEA LTNIINRIRN NPNMDGEVLN ELNISLLEIP NLRLQAFYGI
TVFTADGFGS DLAVKCFEFY LSYVYQLEDS FKKSNSRYGK RDLLQLYIDI LSSEDEIARF
YFPIMKSFTS LLAYGCFTDF QNVKGMSKAI FIVQRRALTC KSPGGLSAIL ELYRTLFLSK
NELLRHHALK YTANLLLNPI EKVRYQAADT LLYAKSIGLL TFLPNELNQK LLTLDWFVPV
SQNATFVKQL RNIIQKQIDK LIADR
