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Tip elongation protein 1 (Protein noc1)

 TIP1_SCHPO              Reviewed;         461 AA.
P79065;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
07-NOV-2018, entry version 132.
RecName: Full=Tip elongation protein 1;
AltName: Full=Protein noc1;
Name=tip1; Synonyms=noc1; ORFNames=SPAC3C7.12;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
PubMed=9714741; DOI=10.1016/S0167-4781(98)00097-9;
Jannatipour M., Rokeach L.A.;
"A Schizosaccharomyces pombe gene encoding a novel polypeptide with a
predicted alpha-helical rod structure found in the myosin and
intermediate-filament families of proteins.";
Biochim. Biophys. Acta 1399:67-72(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11007487; DOI=10.1016/S0092-8674(00)00091-X;
Brunner D., Nurse P.;
"CLIP170-like tip1p spatially organizes microtubular dynamics in
fission yeast.";
Cell 102:695-704(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[4]
FUNCTION, INTERACTION WITH TEA2, AND SUBCELLULAR LOCATION.
PubMed=15177031; DOI=10.1016/j.devcel.2004.05.008;
Busch K.E., Hayles J., Nurse P., Brunner D.;
"Tea2p kinesin is involved in spatial microtubule organization by
transporting tip1p on microtubules.";
Dev. Cell 6:831-843(2004).
[5]
INTERACTION WITH TEA1 AND TEA4.
PubMed=15809031; DOI=10.1016/j.devcel.2005.02.008;
Martin S.G., McDonald W.H., Yates J.R. III, Chang F.;
"Tea4p links microtubule plus ends with the formin for3p in the
establishment of cell polarity.";
Dev. Cell 8:479-491(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-289;
SER-294; SER-305 AND THR-367, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Has a role in stabilizing and targeting the growing tips
of the microtubules along the long axis of the cell, directing
them to the ends of the cell. Acts as a cargo for tea2.
{ECO:0000269|PubMed:11007487, ECO:0000269|PubMed:15177031}.
-!- SUBUNIT: Monomer. Interacts with tea1 and tea2. Interacts with
tea4 in the presence of tea1. {ECO:0000269|PubMed:15177031,
ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:9714741}.
-!- INTERACTION:
Q10113:mal3; NbExp=3; IntAct=EBI-1102463, EBI-1002268;
O42874:peg1; NbExp=4; IntAct=EBI-1102463, EBI-1112382;
P87061:tea1; NbExp=4; IntAct=EBI-1102463, EBI-875376;
Q1MTQ1:tea2; NbExp=5; IntAct=EBI-1102463, EBI-1107767;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11007487, ECO:0000269|PubMed:15177031}.
Note=Located at the microtubule tips.
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EMBL; U59915; AAC33366.1; -; mRNA.
EMBL; CU329670; CAB16742.1; -; Genomic_DNA.
PIR; T38698; T38698.
RefSeq; NP_593613.1; NM_001019044.2.
ProteinModelPortal; P79065; -.
SMR; P79065; -.
BioGrid; 279479; 109.
DIP; DIP-35371N; -.
IntAct; P79065; 8.
STRING; 4896.SPAC3C7.12.1; -.
iPTMnet; P79065; -.
MaxQB; P79065; -.
PaxDb; P79065; -.
PRIDE; P79065; -.
EnsemblFungi; SPAC3C7.12.1; SPAC3C7.12.1:pep; SPAC3C7.12.
GeneID; 2543044; -.
KEGG; spo:SPAC3C7.12; -.
EuPathDB; FungiDB:SPAC3C7.12; -.
PomBase; SPAC3C7.12; tip1.
InParanoid; P79065; -.
OMA; LTCTNMF; -.
OrthoDB; EOG092C2WGB; -.
PhylomeDB; P79065; -.
PRO; PR:P79065; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
GO; GO:0051286; C:cell tip; HDA:PomBase.
GO; GO:1904511; C:cytoplasmic microtubule plus-end; IDA:PomBase.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:1990752; C:microtubule end; IDA:PomBase.
GO; GO:1905721; C:mitotic spindle astral microtubule end; IDA:PomBase.
GO; GO:1905759; C:post-anaphase array microtubule; IDA:PomBase.
GO; GO:0008017; F:microtubule binding; IDA:PomBase.
GO; GO:0051010; F:microtubule plus-end binding; IDA:PomBase.
GO; GO:0034613; P:cellular protein localization; IMP:PomBase.
GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:PomBase.
GO; GO:0071964; P:establishment of cell polarity regulating cell shape; IMP:PomBase.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:PomBase.
GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:PomBase.
GO; GO:1990896; P:protein localization to cell cortex of cell tip; IDA:PomBase.
Gene3D; 2.30.30.190; -; 1.
InterPro; IPR036859; CAP-Gly_dom_sf.
InterPro; IPR000938; CAP-Gly_domain.
Pfam; PF01302; CAP_GLY; 1.
SMART; SM01052; CAP_GLY; 1.
SUPFAM; SSF74924; SSF74924; 1.
PROSITE; PS00845; CAP_GLY_1; 1.
PROSITE; PS50245; CAP_GLY_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule;
Phosphoprotein; Reference proteome.
CHAIN 1 461 Tip elongation protein 1.
/FTId=PRO_0000083544.
DOMAIN 22 69 CAP-Gly. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
COILED 134 418 {ECO:0000255}.
COMPBIAS 77 119 Ser-rich.
MOD_RES 82 82 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 84 84 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 367 367 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
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


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