GIC1_YEAST
ID GIC1_YEAST Reviewed; 314 AA.
AC P38785; D3DL10;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=GTPase-interacting component 1;
GN Name=GIC1; OrderedLocusNames=YHR061C;
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=9367979; DOI=10.1101/gad.11.22.2958;
RA Chen G.C., Kim Y.J., Chan C.S.;
RT "The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for
RT polarized cell growth in Saccharomyces cerevisiae.";
RL Genes Dev. 11:2958-2971(1997).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9367980; DOI=10.1101/gad.11.22.2972;
RA Brown J.L., Jaquenoud M., Gulli M.P., Chant J., Peter M.;
RT "Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in
RT yeast.";
RL Genes Dev. 11:2972-2982(1997).
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).
CC -!- FUNCTION: Required for cell size and shape control, bud site selection,
CC bud emergence, actin cytoskeletal organization, mitotic spindle
CC orientation/positioning, and mating projection formation in response to
CC mating pheromone.
CC -!- SUBUNIT: Interacts with GTP-bound CDC42.
CC -!- INTERACTION:
CC P38785; P47113: BFA1; NbExp=2; IntAct=EBI-7575, EBI-3586;
CC P38785; P26448: BUB2; NbExp=5; IntAct=EBI-7575, EBI-3824;
CC P38785; P32458: CDC11; NbExp=2; IntAct=EBI-7575, EBI-4178;
CC P38785; P32468: CDC12; NbExp=5; IntAct=EBI-7575, EBI-4182;
CC P38785; Q00684: CDC14; NbExp=2; IntAct=EBI-7575, EBI-4192;
CC P38785; P32457: CDC3; NbExp=2; IntAct=EBI-7575, EBI-4429;
CC -!- SUBCELLULAR LOCATION: Bud neck. Bud tip. Cytoplasm, cell cortex.
CC Cytoplasm, cytoskeleton. Note=Concentrated at the incipient bud site of
CC unbudded cells, at the bud tip and mother-bud neck of budded cells, and
CC at cortical sites on large-budded cells that may delimit future bud
CC sites in the two progeny cells.
CC -!- MISCELLANEOUS: Present with 1100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
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DR EMBL; U00061; AAB68388.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06754.1; -; Genomic_DNA.
DR PIR; S46709; S46709.
DR RefSeq; NP_011928.1; NM_001179191.1.
DR AlphaFoldDB; P38785; -.
DR BioGRID; 36493; 117.
DR DIP; DIP-1217N; -.
DR IntAct; P38785; 28.
DR MINT; P38785; -.
DR STRING; 4932.YHR061C; -.
DR iPTMnet; P38785; -.
DR PaxDb; P38785; -.
DR PRIDE; P38785; -.
DR EnsemblFungi; YHR061C_mRNA; YHR061C; YHR061C.
DR GeneID; 856458; -.
DR KEGG; sce:YHR061C; -.
DR SGD; S000001103; GIC1.
DR VEuPathDB; FungiDB:YHR061C; -.
DR eggNOG; ENOG502SSPG; Eukaryota.
DR GeneTree; ENSGT00940000176666; -.
DR HOGENOM; CLU_045871_0_0_1; -.
DR InParanoid; P38785; -.
DR OMA; HHISHAN; -.
DR BioCyc; YEAST:G3O-31114-MON; -.
DR PRO; PR:P38785; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38785; protein.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:SGD.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IGI:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0031106; P:septin ring organization; IGI:SGD.
DR InterPro; IPR000095; CRIB_dom.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..314
FT /note="GTPase-interacting component 1"
FT /id="PRO_0000212659"
FT DOMAIN 126..139
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 112..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 35238 MW; C6B2FE253799500B CRC64;
MTEGKRLQQM ELPQMKSIWI DEDQEMEKLY GFQVRQRFMN GPSTDSDEDA DEDLGIVLVD
SKKLALPNKN NIKLPPLPNY MTINPNINSN HKSLTNKKKN FLGMFKKKDL LSRRHGSAKT
AKQSSISTPF DFHHISHANG KREDNPLESH EEKHDVESLV KFTSLAPQPR PDSNVSSKYS
NVVMNDSSRI VSSSTIATTM DSHHDGNETN NTPNGNKQLD SPTDLEMTLE DLRNYTFPSV
LGDSVSEKTN PSSPSVSSFS GKFKPRELSA LHTPELGNCF NVDQSLNSPG NRISVDDVLK
FYYQCSETST PRNT
