CASP_YEAST
ID CASP_YEAST Reviewed; 679 AA.
AC P34237; D6VX22; P34236;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein CASP;
GN Name=COY1; OrderedLocusNames=YKL179C;
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].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 IDENTIFICATION.
RX PubMed=9332351; DOI=10.1016/s0378-1119(97)00243-6;
RA Lievens P.M.-J., Tufarelli C., Donady J.J., Stagg A., Neufeld E.J.;
RT "CASP, a novel, highly conserved alternative-splicing product of the
RT CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and
RT interacts with full-length CDP in vitro.";
RL Gene 197:73-81(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-619 AND HIS-624.
RX PubMed=12429822; DOI=10.1091/mbc.e02-06-0349;
RA Gillingham A.K., Pfeifer A.C., Munro S.;
RT "CASP, the alternatively spliced product of the gene encoding the CCAAT-
RT displacement protein transcription factor, is a Golgi membrane protein
RT related to giantin.";
RL Mol. Biol. Cell 13:3761-3774(2002).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-450, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; SER-450; SER-453 AND
RP SER-555, AND 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: May be involved in intra-Golgi transport.
CC {ECO:0000269|PubMed:12429822}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12429822}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:12429822}.
CC -!- MISCELLANEOUS: Present with 2650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CASP family. {ECO:0000305}.
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DR EMBL; X74151; CAA52259.1; -; Genomic_DNA.
DR EMBL; Z28179; CAA82021.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08988.1; -; Genomic_DNA.
DR PIR; S38011; S38011.
DR RefSeq; NP_012742.1; NM_001179745.1.
DR AlphaFoldDB; P34237; -.
DR SMR; P34237; -.
DR BioGRID; 33960; 161.
DR DIP; DIP-2851N; -.
DR IntAct; P34237; 2.
DR MINT; P34237; -.
DR STRING; 4932.YKL179C; -.
DR iPTMnet; P34237; -.
DR MaxQB; P34237; -.
DR PaxDb; P34237; -.
DR PRIDE; P34237; -.
DR EnsemblFungi; YKL179C_mRNA; YKL179C; YKL179C.
DR GeneID; 853675; -.
DR KEGG; sce:YKL179C; -.
DR SGD; S000001662; COY1.
DR VEuPathDB; FungiDB:YKL179C; -.
DR eggNOG; KOG0963; Eukaryota.
DR GeneTree; ENSGT00940000172657; -.
DR HOGENOM; CLU_016758_0_0_1; -.
DR InParanoid; P34237; -.
DR OMA; DNWEAKE; -.
DR BioCyc; YEAST:G3O-31945-MON; -.
DR PRO; PR:P34237; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34237; protein.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0048211; P:Golgi vesicle docking; IDA:SGD.
DR GO; GO:0048193; P:Golgi vesicle transport; IGI:SGD.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR012955; CASP_C.
DR Pfam; PF08172; CASP_C; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..679
FT /note="Protein CASP"
FT /id="PRO_0000071795"
FT TOPO_DOM 1..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..679
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 14..90
FT /evidence="ECO:0000255"
FT COILED 178..341
FT /evidence="ECO:0000255"
FT COILED 385..444
FT /evidence="ECO:0000255"
FT COILED 492..540
FT /evidence="ECO:0000255"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 619
FT /note="Y->L: Retained in the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:12429822"
FT MUTAGEN 624
FT /note="H->L: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:12429822"
SQ SEQUENCE 679 AA; 77514 MW; CA849F6F4C88A4A9 CRC64;
MDTSVYSHAL DIWAKADLTN LQRELDADVI EIKDKETLSL NSRKSLATET KKFKKLEPEE
KLNNVNKIIK QYQREIDNLT QRSKFSEKVL FDVYEKLSEA PDPQPLLQSS LEKLGKIDDS
KELKEKISYL EDKLAKYADY ETLKSRLLDL EQSSAKTLAK RLTAKTQEIN STWEEKGRNW
KEREADLLKQ LTNVQEQNKA LEAKISKNID IEGNGNEDGD QENNQKEVST RIAEYNLVTQ
ELETTQARIY QLEKRNEELS GALAKATSEA EKETELHAKE LKLNQLESEN ALLSASYEQE
RKSTSHAINE LKEQLNSVVA ESESYKSELE TVRRKLNNYS DYNKIKEELS ALKKIEFGVN
EDDSDNDIRS EDKNDNTFES SLLSANKKLQ ATLAEYRSKS TAQEEERNEL KKSVDQLKQQ
IATLKEANEK LETDLEKVEN VSPHFNETAS MMSGVTRQMN NRTSHKMSPT SSIIGIPEDG
ELSGNQSTIL PIVTKQRDRF RSRNMDLEKQ LRQGNSEKGK LKLEISKLKG DNTKLYERIR
YLQSYNNNNA PVNQSTERID VESQYSRVYD ESLHPMANFR QNELNHYKNK KLSALEKLFS
SFAKVILQNK MTRMVFLFYC IGLHGLVFMM SMYVINISGY MTPEVGIVQS AKSSSNLNGG
LGGAEKVAAG VGSVHGINR
