ID   FAR11_YEAST             Reviewed;         953 AA.
AC   P53917; D6W156;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Factor arrest protein 11;
GN   Name=FAR11; OrderedLocusNames=YNL127W; ORFNames=N1221, N1875;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8619318; DOI=10.1002/yea.320111210;
RA   Mallet L., Bussereau F., Jacquet M.;
RT   "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT   CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT   deaminase gene and 14 new open reading frames.";
RL   Yeast 11:1195-1209(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-953.
RX   PubMed=9090055;
RX   DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA   de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA   Pallavicini A., Lanfranchi G., Valle G.;
RT   "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT   cerevisiae reveals an unusually high number of overlapping open reading
RT   frames.";
RL   Yeast 13:261-266(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=8913737; DOI=10.1093/genetics/144.3.905;
RA   Horecka J., Sprague G.F. Jr.;
RT   "Identification and characterization of FAR3, a gene required for
RT   pheromone-mediated G1 arrest in Saccharomyces cerevisiae.";
RL   Genetics 144:905-921(1996).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH FAR3; FAR7; FAR8; FAR10 AND VPS64.
RX   PubMed=12588993; DOI=10.1128/mcb.23.5.1750-1763.2003;
RA   Kemp H.A., Sprague G.F. Jr.;
RT   "Far3 and five interacting proteins prevent premature recovery from
RT   pheromone arrest in the budding yeast Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 23:1750-1763(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-524, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-527 AND SER-528, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Participates in the control of the reentry into the cell
CC       cycle following pheromone treatment. {ECO:0000269|PubMed:12588993,
CC       ECO:0000269|PubMed:8913737}.
CC   -!- SUBUNIT: Component of a complex at least composed of FAR3, FAR7, FAR8,
CC       FAR10, FAR11 and VPS64.
CC   -!- INTERACTION:
CC       P53917; P46671: FAR3; NbExp=2; IntAct=EBI-28900, EBI-6789;
CC   -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the FAR11 family. {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; Z46843; CAA86898.1; -; Genomic_DNA.
DR   EMBL; Z71402; CAA96008.1; -; Genomic_DNA.
DR   EMBL; Z71403; CAA96009.1; -; Genomic_DNA.
DR   EMBL; Z69382; CAA93376.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10422.1; -; Genomic_DNA.
DR   PIR; S55156; S55156.
DR   RefSeq; NP_014272.3; NM_001182965.3.
DR   AlphaFoldDB; P53917; -.
DR   BioGRID; 35700; 267.
DR   ComplexPortal; CPX-1197; FAR complex.
DR   DIP; DIP-1830N; -.
DR   IntAct; P53917; 21.
DR   MINT; P53917; -.
DR   STRING; 4932.YNL127W; -.
DR   iPTMnet; P53917; -.
DR   MaxQB; P53917; -.
DR   PaxDb; 4932-YNL127W; -.
DR   PeptideAtlas; P53917; -.
DR   EnsemblFungi; YNL127W_mRNA; YNL127W; YNL127W.
DR   GeneID; 855596; -.
DR   KEGG; sce:YNL127W; -.
DR   AGR; SGD:S000005071; -.
DR   SGD; S000005071; FAR11.
DR   VEuPathDB; FungiDB:YNL127W; -.
DR   eggNOG; KOG3680; Eukaryota.
DR   GeneTree; ENSGT00400000022095; -.
DR   HOGENOM; CLU_003184_1_0_1; -.
DR   InParanoid; P53917; -.
DR   OMA; PCLYPSD; -.
DR   OrthoDB; 5491701at2759; -.
DR   BioCyc; YEAST:G3O-33148-MONOMER; -.
DR   BioGRID-ORCS; 855596; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53917; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53917; Protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:ComplexPortal.
DR   GO; GO:0090443; C:FAR/SIN/STRIPAK complex; NAS:ComplexPortal.
DR   GO; GO:0000138; C:Golgi trans cisterna; IDA:SGD.
DR   GO; GO:0071444; P:cellular response to pheromone; NAS:ComplexPortal.
DR   GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
DR   GO; GO:0000321; P:re-entry into mitotic cell cycle after pheromone arrest; IGI:SGD.
DR   GO; GO:0051726; P:regulation of cell cycle; NAS:ComplexPortal.
DR   InterPro; IPR040185; Far11/STRP.
DR   InterPro; IPR021819; Far11/STRP_C.
DR   InterPro; IPR012486; Far11/STRP_N.
DR   PANTHER; PTHR13239:SF4; AT25231P; 1.
DR   PANTHER; PTHR13239; PROTEIN REQUIRED FOR HYPHAL ANASTOMOSIS HAM-2; 1.
DR   Pfam; PF11882; DUF3402; 2.
DR   Pfam; PF07923; N1221; 1.
DR   SMART; SM01293; DUF3402; 1.
DR   SMART; SM01292; N1221; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Phosphoprotein; Reference proteome.
FT   CHAIN           1..953
FT                   /note="Factor arrest protein 11"
FT                   /id="PRO_0000087190"
FT   REGION          104..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..160
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         528
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   953 AA;  109793 MW;  0FA7B36B181D97A3 CRC64;
     MNASGRSHSK GPIIRSVSLE DLKRNSSFKG NLKYKDEVTS HKEPQVGTLS NEELLKDLDN
     MLRGKLNMGR NSFHADKRNK SDGNISALTF KARSGLEGDI RTIDIQQDSS DENDNFKFSD
     DGVNKDRNNE KDNNTDNAVE FQDDAEEAEE ENEDESFANV DELDGFDLNK VSDGKHVPIN
     EKGEVDYNMP VDKEFQKSLD QCAASLEERS SAPYALQRAV DWELKMFYSL EDELSEWFCS
     SDYMHFGQTQ TLFKQKITQP QLFFDDENYA ASVVECLIED IPNSLASNLL ALSYISMGCF
     AFTNSKSEHT KIIRRNNLML VPHIQEIVHA FKKIAISCRD DNRNLKKQTI LLFHSSTILY
     FICSICIEGR GENPEAVNVV IDAFEKTDLL EFLTKYIENW RWNSRLAMRI RNMISLLFKL
     IVLQFGDSSV YKQTKSSIYN LHGLTYPSKH PEKLSISPLH YQAFREDITS RFPDYNMPSS
     GLPKDVDKSE SLSQFLEIPR PKSKNPLNMA LIVPEKHIAT PAPSPPSSPQ LMHLGEGPRP
     RKSFQTNMAY PCLYPSDNEG SEDDTLEDRI DLNIERKPDN DIVIPFSTEE AARILSESLE
     IKLSTKQLWY ERDLFMITER GWKQQLENEP YDYAALNHDA NSSKEEKSAI CIMQRIDKYY
     KSCLSSFNSL VFVLLQTMES SLTNNFHRKS EVSDKNLLNM LTPQLEIVRA KELSLKSAAG
     ILHALLKWFK LSHILKFEHL AVVIHDSRYI NTCASILSKY SEVYPERVFN KYVQTPNSFW
     KECSLSNESY RESYSVDDSG EVDTEIMPSF AYLLRILRKV TGNKTQRLKE LPLSIGILFK
     RYYRLFNLDM YHPILKITRE LTPFKNKRWK SEHMELISGV YLYEKLELTD NWVTGKDISG
     ELSDACGQEI ALRALLQFYN FQHYEISMED LGYGHRNSSS QDLLNKESEY LNI
//