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Target of rapamycin complex 2 subunit sin1 (TORC2 subunit sin1) (Stress-activated map kinase-interacting protein 1) (SAPK-interacting protein 1)

 SIN1_SCHPO              Reviewed;         665 AA.
Q9P7Y9; Q9Y7F5;
14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 110.
RecName: Full=Target of rapamycin complex 2 subunit sin1 {ECO:0000305|PubMed:18076573};
Short=TORC2 subunit sin1;
AltName: Full=Stress-activated map kinase-interacting protein 1 {ECO:0000303|PubMed:10428959};
Short=SAPK-interacting protein 1;
Name=sin1 {ECO:0000303|PubMed:10428959};
ORFNames=SPAPYUG7.02c {ECO:0000312|PomBase:SPAPYUG7.02c};
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH STY1, AND
PHOSPHORYLATION.
STRAIN=972 / ATCC 24843;
PubMed=10428959; DOI=10.1093/emboj/18.15.4210;
Wilkinson M.G., Soto Pino T., Tournier S., Buck V., Martin H.,
Christiansen J., Wilkinson D.G., Millar J.B.A.;
"Sin1: an evolutionarily conserved component of the eukaryotic SAPK
pathway.";
EMBO J. 18:4210-4221(1999).
[2]
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).
[3]
IDENTIFICATION IN THE TORC2 COMPLEX, PHOSPHORYLATION AT SER-133;
SER-404; SER-490; SER-502 AND SER-530, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18076573; DOI=10.1111/j.1365-2443.2007.01141.x;
Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A.,
Ebe M., Yanagida M.;
"Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant
and organization of two highly phosphorylated TOR complexes by
specific and common subunits.";
Genes Cells 12:1357-1370(2007).
[4]
INTERACTION WITH TOR1.
PubMed=17261596; DOI=10.1128/MCB.01039-06;
Matsuo T., Otsubo Y., Urano J., Tamanoi F., Yamamoto M.;
"Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates
the sexual development pathway in fission yeast.";
Mol. Cell. Biol. 27:3154-3164(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, 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).
[6]
STRUCTURE BY NMR OF 247-400.
PubMed=25428765; DOI=10.1007/s10858-014-9882-7;
Furuita K., Kataoka S., Sugiki T., Hattori Y., Kobayashi N.,
Ikegami T., Shiozaki K., Fujiwara T., Kojima C.;
"Utilization of paramagnetic relaxation enhancements for high-
resolution NMR structure determination of a soluble loop-rich protein
with sparse NOE distance restraints.";
J. Biomol. NMR 61:55-64(2015).
-!- FUNCTION: Component of TORC2, which regulates multiple cellular
processes to control cell growth in response to environmental
signals. TORC2 is required for cell survival under various stress
conditions. TORC2 positively controls G1 cell-cycle arrest, sexual
development and amino acid uptake. Positively regulates amino acid
uptake through the control of expression of amino acid permeases.
{ECO:0000305|PubMed:18076573}.
-!- SUBUNIT: The target of rapamycin complex 2 (TORC2) is composed of
at least bit61, pop3/wat1, sin1, ste20 and tor1 (PubMed:18076573,
PubMed:18257517). Interacts with the sty1 MAP kinase
(PubMed:10428959). {ECO:0000269|PubMed:10428959,
ECO:0000269|PubMed:18076573, ECO:0000269|PubMed:18257517}.
-!- PTM: Phosphorylated; under environmental stress. Either Ser-61 or
Ser-62 and Ser-298, Ser-299 or Ser-301 are phosphorylated as well
(PubMed:18076573). {ECO:0000269|PubMed:10428959,
ECO:0000269|PubMed:18076573, ECO:0000269|PubMed:18257517}.
-!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD37449.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF155208; AAD37449.1; ALT_INIT; Genomic_DNA.
EMBL; CU329670; CAB66311.1; -; Genomic_DNA.
PIR; T50302; T50302.
RefSeq; NP_594703.1; NM_001020130.2.
PDB; 2RUJ; NMR; -; A=247-400.
PDB; 2RVK; NMR; -; A=247-400.
PDBsum; 2RUJ; -.
PDBsum; 2RVK; -.
SMR; Q9P7Y9; -.
BioGrid; 279411; 11.
IntAct; Q9P7Y9; 2.
MINT; MINT-4706703; -.
STRING; 4896.SPAPYUG7.02c.1; -.
iPTMnet; Q9P7Y9; -.
MaxQB; Q9P7Y9; -.
PRIDE; Q9P7Y9; -.
EnsemblFungi; SPAPYUG7.02c.1; SPAPYUG7.02c.1:pep; SPAPYUG7.02c.
GeneID; 2542972; -.
KEGG; spo:SPAPYUG7.02c; -.
EuPathDB; FungiDB:SPAPYUG7.02c; -.
PomBase; SPAPYUG7.02c; sin1.
InParanoid; Q9P7Y9; -.
KO; K20410; -.
OrthoDB; EOG092C0HRG; -.
PhylomeDB; Q9P7Y9; -.
PRO; PR:Q9P7Y9; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0031932; C:TORC2 complex; IDA:PomBase.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IBA:GO_Central.
GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
GO; GO:0000165; P:MAPK cascade; NAS:PomBase.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0038203; P:TORC2 signaling; IMP:PomBase.
InterPro; IPR031567; CRIM_dom.
InterPro; IPR008828; Sin1/Avo1.
InterPro; IPR032679; Sin1_N.
InterPro; IPR031313; Sin1_PH_dom.
PANTHER; PTHR13335; PTHR13335; 1.
Pfam; PF16978; CRIM; 1.
Pfam; PF05422; SIN1; 1.
Pfam; PF16979; SIN1_PH; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Complete proteome; Meiosis; Phosphoprotein;
Reference proteome; Stress response.
CHAIN 1 665 Target of rapamycin complex 2 subunit
sin1.
/FTId=PRO_0000218770.
MOD_RES 62 62 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000269|PubMed:18076573}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000269|PubMed:18076573}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000269|PubMed:18076573}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000269|PubMed:18076573}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000269|PubMed:18076573}.
CONFLICT 152 152 A -> R (in Ref. 1; AAD37449).
{ECO:0000305}.
STRAND 258 260 {ECO:0000244|PDB:2RUJ}.
STRAND 265 267 {ECO:0000244|PDB:2RVK}.
TURN 273 278 {ECO:0000244|PDB:2RUJ}.
HELIX 279 281 {ECO:0000244|PDB:2RUJ}.
TURN 282 285 {ECO:0000244|PDB:2RVK}.
STRAND 290 292 {ECO:0000244|PDB:2RUJ}.
STRAND 308 310 {ECO:0000244|PDB:2RUJ}.
STRAND 312 314 {ECO:0000244|PDB:2RUJ}.
HELIX 317 330 {ECO:0000244|PDB:2RUJ}.
HELIX 338 340 {ECO:0000244|PDB:2RUJ}.
TURN 343 345 {ECO:0000244|PDB:2RUJ}.
STRAND 346 351 {ECO:0000244|PDB:2RUJ}.
STRAND 357 363 {ECO:0000244|PDB:2RUJ}.
HELIX 371 373 {ECO:0000244|PDB:2RUJ}.
STRAND 378 382 {ECO:0000244|PDB:2RUJ}.
HELIX 385 394 {ECO:0000244|PDB:2RUJ}.
SEQUENCE 665 AA; 74079 MW; 367679DF92390835 CRC64;
MELTREKVLL LTFLRMQYSH ILPDSIENRV ISTEAPEWEL DKSLQDLLIH DYDYSKTSFS
SSPPIVANDT VSNVRKPSDT KQVNGAGGQV NHSRAEDSDY ATSDLSESSD VGDDDNSCIF
SFSKVPMQKD VASIKEEERL DPKISTLNNI DAIANLKLTN MVESSQAVNL TSSKQSSINQ
QSSVSTDYDD LRSISEESFH LSQGEIPLTF PMNSSLTDTE ADAVVAVDAL FPGKQRGTHN
TVNKARSVSN AKAPTSALRA LLEHKENSSQ NGPLAENFAT FSGHAESNAL RLNIYFPSSE
SPSKPLFVEL RKNVLVSEAI GYILLQYVNQ QLVPPIEDEA QNPNYWNLRI VEDDGELDED
FPALDRVGPL SKFGFDAFAL VKATPAQIKE NQAAYPFKSK HPTSIPEANN KTHIRHTSST
SSQSQKQAQD VKDTLNTSHV VQVRLPPYGD NARFCNIEIS KTTRLAMVLN QVCWMKQLER
FKYTLRVAGS DTVLPLDKTF SSLDGNPTLE LVKKKVRDKK GSTQQLPTSS PQNSVYGSIK
KDAQSSTYNA TDIMSSNTYQ EFLVWKRQPV SFMGRHERLL AIDGEYVHIM PSESKNIFET
PKTSSIHAGS IILCKQSKKS PCNFKMIVSK NRETKRYDFE VLSALEAAII VSRIRALMNT
VKKIN


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