TIP1_SCHPO
ID TIP1_SCHPO Reviewed; 461 AA.
AC P79065;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Tip elongation protein 1;
DE AltName: Full=Protein noc1;
GN Name=tip1; Synonyms=noc1; ORFNames=SPAC3C7.12;
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 [MRNA], AND SUBUNIT.
RX PubMed=9714741; DOI=10.1016/s0167-4781(98)00097-9;
RA Jannatipour M., Rokeach L.A.;
RT "A Schizosaccharomyces pombe gene encoding a novel polypeptide with a
RT predicted alpha-helical rod structure found in the myosin and intermediate-
RT filament families of proteins.";
RL Biochim. Biophys. Acta 1399:67-72(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11007487; DOI=10.1016/s0092-8674(00)00091-x;
RA Brunner D., Nurse P.;
RT "CLIP170-like tip1p spatially organizes microtubular dynamics in fission
RT yeast.";
RL Cell 102:695-704(2000).
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 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 [5]
RP INTERACTION WITH TEA1 AND TEA4.
RX PubMed=15809031; DOI=10.1016/j.devcel.2005.02.008;
RA Martin S.G., McDonald W.H., Yates J.R. III, Chang F.;
RT "Tea4p links microtubule plus ends with the formin for3p in the
RT establishment of cell polarity.";
RL Dev. Cell 8:479-491(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-289; SER-294;
RP SER-305 AND THR-367, AND IDENTIFICATION BY 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: Has a role in stabilizing and targeting the growing tips of
CC the microtubules along the long axis of the cell, directing them to the
CC ends of the cell. Acts as a cargo for tea2.
CC {ECO:0000269|PubMed:11007487, ECO:0000269|PubMed:15177031}.
CC -!- SUBUNIT: Monomer. Interacts with tea1 and tea2. Interacts with tea4 in
CC the presence of tea1. {ECO:0000269|PubMed:15177031,
CC ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:9714741}.
CC -!- INTERACTION:
CC P79065; Q10113: mal3; NbExp=3; IntAct=EBI-1102463, EBI-1002268;
CC P79065; O42874: peg1; NbExp=4; IntAct=EBI-1102463, EBI-1112382;
CC P79065; P87061: tea1; NbExp=5; IntAct=EBI-1102463, EBI-875376;
CC P79065; Q1MTQ1: tea2; NbExp=6; IntAct=EBI-1102463, EBI-1107767;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11007487, ECO:0000269|PubMed:15177031}.
CC Note=Located at the microtubule tips.
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DR EMBL; U59915; AAC33366.1; -; mRNA.
DR EMBL; CU329670; CAB16742.1; -; Genomic_DNA.
DR PIR; T38698; T38698.
DR RefSeq; NP_593613.1; NM_001019044.2.
DR AlphaFoldDB; P79065; -.
DR SMR; P79065; -.
DR BioGRID; 279479; 112.
DR DIP; DIP-35371N; -.
DR IntAct; P79065; 9.
DR STRING; 4896.SPAC3C7.12.1; -.
DR iPTMnet; P79065; -.
DR MaxQB; P79065; -.
DR PaxDb; P79065; -.
DR PRIDE; P79065; -.
DR EnsemblFungi; SPAC3C7.12.1; SPAC3C7.12.1:pep; SPAC3C7.12.
DR GeneID; 2543044; -.
DR KEGG; spo:SPAC3C7.12; -.
DR PomBase; SPAC3C7.12; tip1.
DR VEuPathDB; FungiDB:SPAC3C7.12; -.
DR eggNOG; KOG4568; Eukaryota.
DR HOGENOM; CLU_582851_0_0_1; -.
DR InParanoid; P79065; -.
DR OMA; QIPNVGR; -.
DR PhylomeDB; P79065; -.
DR PRO; PR:P79065; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; EXP:PomBase.
DR GO; GO:1904511; C:cytoplasmic microtubule plus-end; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990752; C:microtubule end; IDA:PomBase.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; IDA:PomBase.
DR GO; GO:1905759; C:post-anaphase array microtubule; IDA:PomBase.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:PomBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:PomBase.
DR GO; GO:0071964; P:establishment of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; EXP:PomBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:PomBase.
DR GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1990896; P:protein localization to cell cortex of cell tip; IDA:PomBase.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..461
FT /note="Tip elongation protein 1"
FT /id="PRO_0000083544"
FT DOMAIN 22..69
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 278..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..418
FT /evidence="ECO:0000255"
FT COMPBIAS 278..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 461 AA; 52607 MW; 66CCDB96146F86D6 CRC64;
MFPLGSVVEV ITGERGFVRY AGEVENRKGV YVGLELLPEF AEFGKNRGVV DGREYFKTKN
NEKTGIFVPF DKCKLASSIS SSPSPKIDGT AASIGMGFPP MSPNLQSSIP RLTNVSSSSN
LSMNTISSTA LTPTEKILQK RIEDLLYERQ NHQQQLEEVL ATVDQLQSLV TNFNDQQDEV
DELRERITLK EERIQQMRNE ASQRRFEFKT TIECLEESSN RAIETYENRI AELEAQLEMY
MSGKSEDDLL FSLQQERDYA LNQVEILQER VDTLMKQKAN SSTANEKLSH MESSSPTLTN
ASFESPKRGK GSNDLPENHP QRRQTLEFYE IEIEVLREKV EKLQALSDEK DFYISKLEKS
LDRNDTTPVP SDEKLSNYAA EKENLVSRIS ELEHTIEQLT INNERDNERM SPAEFELETT
QEVEENDSDS HDDEETWCEV CETNNHSLQE CPTVFGSTDE A
