SPC97_YEAST
ID SPC97_YEAST Reviewed; 823 AA.
AC P38863; D3DLC1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Spindle pole body component SPC97;
GN Name=SPC97; OrderedLocusNames=YHR172W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP CHARACTERIZATION.
RX PubMed=9130700; DOI=10.1093/emboj/16.7.1550;
RA Knop M., Pereira G., Geissler S., Grein K., Schiebel E.;
RT "The spindle pole body component Spc97p interacts with the gamma-tubulin of
RT Saccharomyces cerevisiae and functions in microtubule organization and
RT spindle pole body duplication.";
RL EMBO J. 16:1550-1564(1997).
RN [4]
RP INTERACTION WITH SPC72.
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 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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in microtubule organization by the microtubule
CC organizing center, the spindle pole body (SPB). Probably part of the
CC microtubule attachment site at the SPB.
CC -!- SUBUNIT: Interacts with TUB4, SPC72 and SPC98.
CC {ECO:0000269|PubMed:9670012}.
CC -!- INTERACTION:
CC P38863; P53540: SPC98; NbExp=7; IntAct=EBI-17786, EBI-17794;
CC P38863; P53378: TUB4; NbExp=8; IntAct=EBI-17786, EBI-19013;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body.
CC -!- MISCELLANEOUS: Present with 2230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
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DR EMBL; U00027; AAB68017.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06865.1; -; Genomic_DNA.
DR PIR; S48911; S48911.
DR RefSeq; NP_012042.1; NM_001179303.1.
DR PDB; 5FLZ; EM; 6.90 A; A=1-823.
DR PDB; 5FM1; EM; 8.00 A; A=1-823.
DR PDB; 7M2W; EM; 3.00 A; E/G=1-823.
DR PDB; 7M2X; EM; 3.60 A; C=1-823.
DR PDB; 7M2Y; EM; 4.03 A; D=1-823.
DR PDB; 7M2Z; EM; 3.70 A; D=1-823.
DR PDBsum; 5FLZ; -.
DR PDBsum; 5FM1; -.
DR PDBsum; 7M2W; -.
DR PDBsum; 7M2X; -.
DR PDBsum; 7M2Y; -.
DR PDBsum; 7M2Z; -.
DR AlphaFoldDB; P38863; -.
DR SMR; P38863; -.
DR BioGRID; 36606; 159.
DR ComplexPortal; CPX-1198; Gamma tubulin small complex.
DR DIP; DIP-826N; -.
DR IntAct; P38863; 15.
DR MINT; P38863; -.
DR STRING; 4932.YHR172W; -.
DR iPTMnet; P38863; -.
DR MaxQB; P38863; -.
DR PaxDb; P38863; -.
DR PRIDE; P38863; -.
DR EnsemblFungi; YHR172W_mRNA; YHR172W; YHR172W.
DR GeneID; 856577; -.
DR KEGG; sce:YHR172W; -.
DR SGD; S000001215; SPC97.
DR VEuPathDB; FungiDB:YHR172W; -.
DR eggNOG; KOG2001; Eukaryota.
DR GeneTree; ENSGT00940000156697; -.
DR HOGENOM; CLU_007738_2_0_1; -.
DR InParanoid; P38863; -.
DR OMA; TSQMMLQ; -.
DR BioCyc; YEAST:G3O-31206-MON; -.
DR PRO; PR:P38863; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38863; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0008275; C:gamma-tubulin small complex; IDA:SGD.
DR GO; GO:0005822; C:inner plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005824; C:outer plaque of spindle pole body; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0005816; C:spindle pole body; HDA:SGD.
DR GO; GO:0043015; F:gamma-tubulin binding; IPI:SGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IDA:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.20.120.1900; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Microtubule; Nucleus;
KW Reference proteome.
FT CHAIN 1..823
FT /note="Spindle pole body component SPC97"
FT /id="PRO_0000078117"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 100..126
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 182..205
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 338..360
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 389..411
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 415..426
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 432..451
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 576..608
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 610..613
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 621..624
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 626..650
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 652..662
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 669..684
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 687..691
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 693..716
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 717..720
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 722..725
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 755..787
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 802..811
FT /evidence="ECO:0007829|PDB:7M2W"
SQ SEQUENCE 823 AA; 96825 MW; A3F7018957D96E8D CRC64;
MEIKEVDDRA ELLRYTNNIP LLGKLVNHQP LWSTNPKLKS FSLEKISAPD QRRVQEALVV
KDLLNVLIGL EGTYIRYFND YEPSDPETPI EFKIAKKMDP SFKTFSRRIV RYGKQYMILT
RAYEKWSDTS FGMVLQRFAY EIRRFLEDVY LKTLVERLER DFNKVPNFSI RELEQIINET
EVNKQMELLY NIYEEIFREI EERRTNQSSQ EDFNNFMDSM KNESSLHLRL MVAFDTTVYP
VPKGGAILKI FQQKILENLG DRSSVMFLKK LLNNISQDYC TMLYEWLTQG ILNDPYQEFM
TYDDLEGKTD NIFDTRDRAW DTQYFIRKDV LLRDCDSEED KNLLFKMLRT GILLKVVRAS
LQIPTIPSNS SDITIQEIND FADLMEGSNL ELYVDKCYSR ANEIFLKLFF QGYDLINVLK
HLQQIFLGYQ SGHNVLKFLT KNMGELTKHY RNDNNANYDK LLQNFELERQ SENPNNLMRQ
LLMIQFDTET LPQVLSHYLQ IYPEVPENNS ANDDSDPLMH ANNFKNMNAI LFDELSKERT
GAYHGSNLEL YTPKSAIYHL KFDINIPYPL NIIISRTCMI KYQIILRYQL VLQYHSRLLD
ETWMDLNKTP SWKYRGYSHT VKRRIVRATR VLHAKMNHFI KTIMEYFNQN VIDKEVYSLE
KCYRNPTLAV AIQNELEGGL TNIMTNRCLS DLIPLQLQIF DIVYKFCKFI KSMRAKLCQL
DPVLYEKHKS GMMKTLNEGY RTNNGGQEDV GYQEDAALEL IQKLIEYISN ASSIFRKCLI
NFTQELSTEK FDFYDSSSVD AAGIERVLYS IVPPRSASAS SQR
