SIN1_SCHPO
ID SIN1_SCHPO Reviewed; 665 AA.
AC Q9P7Y9; Q9Y7F5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Target of rapamycin complex 2 subunit sin1 {ECO:0000305|PubMed:18076573};
DE Short=TORC2 subunit sin1;
DE AltName: Full=Stress-activated map kinase-interacting protein 1 {ECO:0000303|PubMed:10428959};
DE Short=SAPK-interacting protein 1;
GN Name=sin1 {ECO:0000303|PubMed:10428959};
GN ORFNames=SPAPYUG7.02c {ECO:0000312|PomBase:SPAPYUG7.02c};
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], INTERACTION WITH STY1, AND
RP PHOSPHORYLATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10428959; DOI=10.1093/emboj/18.15.4210;
RA Wilkinson M.G., Soto Pino T., Tournier S., Buck V., Martin H.,
RA Christiansen J., Wilkinson D.G., Millar J.B.A.;
RT "Sin1: an evolutionarily conserved component of the eukaryotic SAPK
RT pathway.";
RL EMBO J. 18:4210-4221(1999).
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 IDENTIFICATION IN THE TORC2 COMPLEX, PHOSPHORYLATION AT SER-133; SER-404;
RP SER-490; SER-502 AND SER-530, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18076573; DOI=10.1111/j.1365-2443.2007.01141.x;
RA Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A.,
RA Ebe M., Yanagida M.;
RT "Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and
RT organization of two highly phosphorylated TOR complexes by specific and
RT common subunits.";
RL Genes Cells 12:1357-1370(2007).
RN [4]
RP INTERACTION WITH TOR1.
RX PubMed=17261596; DOI=10.1128/mcb.01039-06;
RA Matsuo T., Otsubo Y., Urano J., Tamanoi F., Yamamoto M.;
RT "Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates the
RT sexual development pathway in fission yeast.";
RL Mol. Cell. Biol. 27:3154-3164(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, 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).
RN [6]
RP STRUCTURE BY NMR OF 247-400.
RX PubMed=25428765; DOI=10.1007/s10858-014-9882-7;
RA Furuita K., Kataoka S., Sugiki T., Hattori Y., Kobayashi N., Ikegami T.,
RA Shiozaki K., Fujiwara T., Kojima C.;
RT "Utilization of paramagnetic relaxation enhancements for high-resolution
RT NMR structure determination of a soluble loop-rich protein with sparse NOE
RT distance restraints.";
RL J. Biomol. NMR 61:55-64(2015).
CC -!- FUNCTION: Component of TORC2, which regulates multiple cellular
CC processes to control cell growth in response to environmental signals.
CC TORC2 is required for cell survival under various stress conditions.
CC TORC2 positively controls G1 cell-cycle arrest, sexual development and
CC amino acid uptake. Positively regulates amino acid uptake through the
CC control of expression of amino acid permeases.
CC {ECO:0000305|PubMed:18076573}.
CC -!- SUBUNIT: The target of rapamycin complex 2 (TORC2) is composed of at
CC least bit61, pop3/wat1, sin1, ste20 and tor1 (PubMed:18076573,
CC PubMed:18257517). Interacts with the sty1 MAP kinase (PubMed:10428959).
CC {ECO:0000269|PubMed:10428959, ECO:0000269|PubMed:18076573,
CC ECO:0000269|PubMed:18257517}.
CC -!- PTM: Phosphorylated; under environmental stress. Either Ser-61 or Ser-
CC 62 and Ser-298, Ser-299 or Ser-301 are phosphorylated as well
CC (PubMed:18076573). {ECO:0000269|PubMed:10428959,
CC ECO:0000269|PubMed:18076573, ECO:0000269|PubMed:18257517}.
CC -!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD37449.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF155208; AAD37449.1; ALT_INIT; Genomic_DNA.
DR EMBL; CU329670; CAB66311.1; -; Genomic_DNA.
DR PIR; T50302; T50302.
DR RefSeq; NP_594703.1; NM_001020130.2.
DR PDB; 2RUJ; NMR; -; A=247-400.
DR PDB; 2RVK; NMR; -; A=247-400.
DR PDBsum; 2RUJ; -.
DR PDBsum; 2RVK; -.
DR AlphaFoldDB; Q9P7Y9; -.
DR BMRB; Q9P7Y9; -.
DR SMR; Q9P7Y9; -.
DR BioGRID; 279411; 13.
DR IntAct; Q9P7Y9; 2.
DR STRING; 4896.SPAPYUG7.02c.1; -.
DR iPTMnet; Q9P7Y9; -.
DR MaxQB; Q9P7Y9; -.
DR PaxDb; Q9P7Y9; -.
DR PRIDE; Q9P7Y9; -.
DR EnsemblFungi; SPAPYUG7.02c.1; SPAPYUG7.02c.1:pep; SPAPYUG7.02c.
DR GeneID; 2542972; -.
DR KEGG; spo:SPAPYUG7.02c; -.
DR PomBase; SPAPYUG7.02c; sin1.
DR VEuPathDB; FungiDB:SPAPYUG7.02c; -.
DR eggNOG; KOG3739; Eukaryota.
DR HOGENOM; CLU_431582_0_0_1; -.
DR InParanoid; Q9P7Y9; -.
DR OMA; NYWNLRI; -.
DR PhylomeDB; Q9P7Y9; -.
DR Reactome; R-SPO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SPO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR PRO; PR:Q9P7Y9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IDA:PomBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:PomBase.
DR GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0038203; P:TORC2 signaling; IMP:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR031567; CRIM_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008828; Sin1/Avo1.
DR InterPro; IPR032679; Sin1_N.
DR InterPro; IPR031313; Sin1_PH_dom.
DR PANTHER; PTHR13335; PTHR13335; 1.
DR Pfam; PF16978; CRIM; 1.
DR Pfam; PF05422; SIN1; 1.
DR Pfam; PF16979; SIN1_PH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Meiosis; Phosphoprotein; Reference proteome;
KW Stress response.
FT CHAIN 1..665
FT /note="Target of rapamycin complex 2 subunit sin1"
FT /id="PRO_0000218770"
FT REGION 65..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT CONFLICT 152
FT /note="A -> R (in Ref. 1; AAD37449)"
FT /evidence="ECO:0000305"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2RUJ"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2RVK"
FT TURN 273..278
FT /evidence="ECO:0007829|PDB:2RUJ"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2RUJ"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:2RVK"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2RUJ"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2RUJ"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2RUJ"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:2RUJ"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:2RUJ"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2RUJ"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:2RUJ"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:2RUJ"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:2RUJ"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2RUJ"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:2RUJ"
SQ 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
