SPC72_YEAST
ID SPC72_YEAST Reviewed; 622 AA.
AC P39723; D6VPG9; E9P941;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Spindle pole component SPC72;
GN Name=SPC72; Synonyms=LDB4, SPI6; OrderedLocusNames=YAL047C; ORFNames=FUN42;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 302.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPC97; SPC98 AND TUB4.
RX PubMed=9670012; DOI=10.1093/emboj/17.14.3952;
RA Knop M., Schiebel E.;
RT "Receptors determine the cellular localization of a gamma-tubulin complex
RT and thereby the site of microtubule formation.";
RL EMBO J. 17:3952-3967(1998).
RN [5]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9585415; DOI=10.1083/jcb.141.4.967;
RA Wigge P.A., Jensen O.N., Holmes S., Soues S., Mann M., Kilmartin J.V.;
RT "Analysis of the Saccharomyces spindle pole by matrix-assisted laser
RT desorption/ionization (MALDI) mass spectrometry.";
RL J. Cell Biol. 141:967-977(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH STU2.
RX PubMed=9606209; DOI=10.1083/jcb.141.5.1169;
RA Chen X.P., Yin H., Huffaker T.C.;
RT "The yeast spindle pole body component Spc72p interacts with Stu2p and is
RT required for proper microtubule assembly.";
RL J. Cell Biol. 141:1169-1179(1998).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9718373; DOI=10.1242/jcs.111.18.2809;
RA Soues S., Adams I.R.;
RT "SPC72: a spindle pole component required for spindle orientation in the
RT yeast Saccharomyces cerevisiae.";
RL J. Cell Sci. 111:2809-2818(1998).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KAR1.
RX PubMed=10428957; DOI=10.1093/emboj/18.15.4180;
RA Pereira G., Grueneberg U., Knop M., Schiebel E.;
RT "Interaction of the yeast gamma-tubulin complex-binding protein Spc72p with
RT Kar1p is essential for microtubule function during karyogamy.";
RL EMBO J. 18:4180-4195(1999).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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 [11]
RP INTERACTION WITH CDC5, AND PHOSPHORYLATION BY CDC5.
RX PubMed=18022565; DOI=10.1016/j.chembiol.2007.09.011;
RA Snead J.L., Sullivan M., Lowery D.M., Cohen M.S., Zhang C., Randle D.H.,
RA Taunton J., Yaffe M.B., Morgan D.O., Shokat K.M.;
RT "A coupled chemical-genetic and bioinformatic approach to Polo-like kinase
RT pathway exploration.";
RL Chem. Biol. 14:1261-1272(2007).
RN [12]
RP FUNCTION, PHOSPHORYLATION BY CDC5, AND INTERACTION WITH KIN4.
RX PubMed=17967947; DOI=10.1083/jcb.200705197;
RA Maekawa H., Priest C., Lechner J., Pereira G., Schiebel E.;
RT "The yeast centrosome translates the positional information of the anaphase
RT spindle into a cell cycle signal.";
RL J. Cell Biol. 179:423-436(2007).
RN [13]
RP IDENTIFICATION BY 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 [14]
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: Spindle pole body component that acts as the gamma-tubulin
CC complex-binding protein of the SPB outer plaque. Anchors cytoplasmic
CC microtubules at the at the half bridge of the spindle pole body (SPB)
CC and accordingly functions in nuclear position and spindle orientation,
CC including anaphase spindle migration into the bud. Recruits KIN4 kinase
CC to both SPBs when cytoplasmic microtubules are defective. Links
CC cytoplasmic microtubules with spindle orientation checkpoint (SPOC)
CC components and, therefore, could function as part of the sensors of
CC spindle orientation defects. Is strictly required for mating and
CC karyogamy. {ECO:0000269|PubMed:10428957, ECO:0000269|PubMed:17967947,
CC ECO:0000269|PubMed:9606209, ECO:0000269|PubMed:9670012,
CC ECO:0000269|PubMed:9718373}.
CC -!- SUBUNIT: Homooligomer. Interacts with CDC5, KAR1, KIN4, SPC97, SPC98,
CC STU2 and TUB4. {ECO:0000269|PubMed:10428957,
CC ECO:0000269|PubMed:17967947, ECO:0000269|PubMed:18022565,
CC ECO:0000269|PubMed:9606209, ECO:0000269|PubMed:9670012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:10428957,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9585415,
CC ECO:0000269|PubMed:9606209, ECO:0000269|PubMed:9670012,
CC ECO:0000269|PubMed:9718373}. Note=localized at the outer plaque and the
CC bridge of the spindle pole body.
CC -!- PTM: Phosphorylated by CDC5. {ECO:0000269|PubMed:17967947,
CC ECO:0000269|PubMed:18022565}.
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U12980; AAC04984.1; -; Genomic_DNA.
DR EMBL; AY723757; AAU09674.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06939.2; -; Genomic_DNA.
DR PIR; S51972; S51972.
DR RefSeq; NP_009352.2; NM_001178192.2.
DR PDB; 6MF5; X-ray; 2.70 A; C/D=227-237.
DR PDBsum; 6MF5; -.
DR AlphaFoldDB; P39723; -.
DR SMR; P39723; -.
DR BioGRID; 31780; 135.
DR DIP; DIP-868N; -.
DR IntAct; P39723; 36.
DR MINT; P39723; -.
DR STRING; 4932.YAL047C; -.
DR iPTMnet; P39723; -.
DR MaxQB; P39723; -.
DR PaxDb; P39723; -.
DR PRIDE; P39723; -.
DR EnsemblFungi; YAL047C_mRNA; YAL047C; YAL047C.
DR GeneID; 851250; -.
DR KEGG; sce:YAL047C; -.
DR SGD; S000000045; SPC72.
DR VEuPathDB; FungiDB:YAL047C; -.
DR eggNOG; ENOG502R9Z8; Eukaryota.
DR HOGENOM; CLU_016740_0_0_1; -.
DR InParanoid; P39723; -.
DR OMA; RKYNTER; -.
DR BioCyc; YEAST:G3O-28854-MON; -.
DR PRO; PR:P39723; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39723; protein.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; IDA:SGD.
DR GO; GO:0061499; C:outer plaque of mitotic spindle pole body; IDA:SGD.
DR GO; GO:0005824; C:outer plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0099609; F:microtubule lateral binding; IDA:SGD.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:1990734; P:astral microtubule anchoring at mitotic spindle pole body; IMP:SGD.
DR GO; GO:0030953; P:astral microtubule organization; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:SGD.
DR GO; GO:0110121; P:gamma-tubulin complex localization to cytoplasmic side of mitotic spindle pole body; IPI:SGD.
DR GO; GO:0000741; P:karyogamy; IEA:UniProtKB-KW.
DR GO; GO:0007020; P:microtubule nucleation; IMP:SGD.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IGI:SGD.
DR InterPro; IPR024545; Mto2p-binding.
DR Pfam; PF12808; Mto2_bdg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Karyogamy; Phosphoprotein; Reference proteome.
FT CHAIN 1..622
FT /note="Spindle pole component SPC72"
FT /id="PRO_0000202421"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 302
FT /note="N -> I (in Ref. 1; AAC04984)"
FT /evidence="ECO:0000305"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6MF5"
SQ SEQUENCE 622 AA; 72106 MW; 33A858B9ADCAD633 CRC64;
MVRRWIPSGR HLRNNDNTGD DDDSEFTNSM DSGMSIPSLR DSMTTRSSHN DPIKPALMND
SNKVKNLEKE LTNAKIKIQV LYEYIRRIPN KDGNAPSLGN DTDFRNSIIE GLNLEINKLK
QDLKAKEVEY QDTLQFVQEN LENSESIVNT INHLLSFILT HFNEQDENAH LLDKEERETL
EETLELSSDY VLEKMDTLSK FIIQFLQDFL HSKSRAESKQ DKEEFLSLAQ SSPAGSQLES
RDSPSSKEEN TDGGYQNDEI HDSNNHIDTE NVMANSTSLP ISAVESRFEK TLDTQLEIVI
ENLHKEYDQF INSIRLKFEK SQKLEKIIAS KLNEQSHLLD SLELEENSSS VIEKQDHLIS
QLKEKIESQS VLINNLEKLK EDIIKMKQNE KVLTKELETQ TKINKLKENN WDSYINDLEK
QINDLQIDKS EEFHVIQNQL DKLDLENYQL KNQLNTLDNQ KLILSQYESN FIKFNQNLLL
HLDSIFNILQ KILQESSIAQ FDRKMKSIKS VPNALKNLNL IQPKLESLYT FIETALESII
NSYISSLISM ETPEQPHQQG NELTATPNKE LTLRIEELQR RWISERERRK LDANASEARI
KALEQENESL RSKLFNLSIN NP
