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SHY1_YEAST
ID   SHY1_YEAST              Reviewed;         389 AA.
AC   P53266; D6VUP5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Cytochrome oxidase assembly protein SHY1;
DE   AltName: Full=SURF1 homolog of Yeast;
DE   AltName: Full=SURF1-like protein;
GN   Name=SHY1; OrderedLocusNames=YGR112W; ORFNames=G6150;
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=8905931;
RX   DOI=10.1002/(sici)1097-0061(19960930)12:12<1273::aid-yea21>3.0.co;2-j;
RA   Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
RA   Schreer A., Schaefer B., Zimmermann M., Wolf K.;
RT   "The sequence of a 23.4 kb segment on the right arm of chromosome VII from
RT   Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3
RT   element and 11 new open reading frames.";
RL   Yeast 12:1273-1277(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   CHARACTERIZATION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=9162072; DOI=10.1074/jbc.272.22.14356;
RA   Mashkevich G., Repetto B., Glerum D.M., Jin C., Tzagoloff A.;
RT   "SHY1, the yeast homolog of the mammalian SURF-1 gene, encodes a
RT   mitochondrial protein required for respiration.";
RL   J. Biol. Chem. 272:14356-14364(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=11782424; DOI=10.1093/emboj/21.1.43;
RA   Barrientos A., Korr D., Tzagoloff A.;
RT   "Shy1p is necessary for full expression of mitochondrial COX1 in the yeast
RT   model of Leigh's syndrome.";
RL   EMBO J. 21:43-52(2002).
RN   [6]
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   [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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [9]
RP   INTERACTION WITH COA1.
RX   PubMed=17882260; DOI=10.1038/sj.emboj.7601861;
RA   Pierrel F., Bestwick M.L., Cobine P.A., Khalimonchuk O., Cricco J.A.,
RA   Winge D.R.;
RT   "Coa1 links the Mss51 post-translational function to Cox1 cofactor
RT   insertion in cytochrome c oxidase assembly.";
RL   EMBO J. 26:4335-4346(2007).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH COX14 AND MSS51.
RX   PubMed=17882259; DOI=10.1038/sj.emboj.7601862;
RA   Mick D.U., Wagner K., van der Laan M., Frazier A.E., Perschil I.,
RA   Pawlas M., Meyer H.E., Warscheid B., Rehling P.;
RT   "Shy1 couples Cox1 translational regulation to cytochrome c oxidase
RT   assembly.";
RL   EMBO J. 26:4347-4358(2007).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH COA2.
RX   PubMed=18541668; DOI=10.1128/mcb.00057-08;
RA   Pierrel F., Khalimonchuk O., Cobine P.A., Bestwick M.L., Winge D.R.;
RT   "Coa2 is an assembly factor for yeast cytochrome C oxidase biogenesis that
RT   facilitates the maturation of cox1.";
RL   Mol. Cell. Biol. 28:4927-4939(2008).
CC   -!- FUNCTION: Required for efficient assembly of cytochrome c oxidase in
CC       the mitochondrial inner membrane. Involved in a step that couples
CC       MSS51-COX14-dependent regulation of COX1 translation to early steps of
CC       cytochrome c oxidase assembly. {ECO:0000269|PubMed:11782424,
CC       ECO:0000269|PubMed:17882259, ECO:0000269|PubMed:18541668}.
CC   -!- SUBUNIT: Interacts with COA1, COX14 and MSS51.
CC       {ECO:0000269|PubMed:17882259, ECO:0000269|PubMed:17882260,
CC       ECO:0000269|PubMed:18541668}.
CC   -!- INTERACTION:
CC       P53266; P40452: COA1; NbExp=5; IntAct=EBI-17111, EBI-25287;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC       ECO:0000269|PubMed:9162072}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC       ECO:0000269|PubMed:9162072}.
CC   -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SURF1 family. {ECO:0000305}.
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DR   EMBL; Z72897; CAA97120.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08206.1; -; Genomic_DNA.
DR   PIR; S64420; S64420.
DR   RefSeq; NP_011627.1; NM_001181241.1.
DR   AlphaFoldDB; P53266; -.
DR   BioGRID; 33359; 145.
DR   IntAct; P53266; 15.
DR   MINT; P53266; -.
DR   STRING; 4932.YGR112W; -.
DR   TCDB; 3.D.4.8.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR   MaxQB; P53266; -.
DR   PaxDb; P53266; -.
DR   PRIDE; P53266; -.
DR   DNASU; 853009; -.
DR   EnsemblFungi; YGR112W_mRNA; YGR112W; YGR112W.
DR   GeneID; 853009; -.
DR   KEGG; sce:YGR112W; -.
DR   SGD; S000003344; SHY1.
DR   VEuPathDB; FungiDB:YGR112W; -.
DR   eggNOG; KOG1563; Eukaryota.
DR   GeneTree; ENSGT00530000064194; -.
DR   HOGENOM; CLU_047737_4_0_1; -.
DR   InParanoid; P53266; -.
DR   OMA; MFVGPRV; -.
DR   BioCyc; YEAST:G3O-30821-MON; -.
DR   PRO; PR:P53266; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53266; protein.
DR   GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:SGD.
DR   CDD; cd06662; SURF1; 1.
DR   InterPro; IPR002994; Surf1/Shy1.
DR   InterPro; IPR045214; Surf1/Surf4.
DR   PANTHER; PTHR23427; PTHR23427; 1.
DR   Pfam; PF02104; SURF1; 1.
DR   PROSITE; PS50895; SURF1; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..389
FT                   /note="Cytochrome oxidase assembly protein SHY1"
FT                   /id="PRO_0000215659"
FT   TOPO_DOM        1..71
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..341
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..389
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REGION          292..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  45056 MW;  2C95E607B7507321 CRC64;
     MSLLGARSTY RWFSIAASIP TKNAIGKSTY LLASRNQQYR GIITSTVDWK PIKTGKSPND
     DSRRERSFGK KIVLGLMFAM PIISFYLGTW QVRRLKWKTK LIAACETKLT YEPIPLPKSF
     TPDMCEDWEY RKVILTGHFL HNEEMFVGPR KKNGEKGYFL FTPFIRDDTG EKVLIERGWI
     SEEKVAPDSR NLHHLSLPQE EHLKVVCLVR PPKKRGSLQW AKKDPNSRLW QVPDIYDMAR
     SSGCTPIQFQ ALYDMKDHPI IEEHTRNEAS QNNSTSSLWK FWKREPTTAV NGTQAVDNNT
     SKPRSRQEMP TDQTIEFDER QFIKAGVPIG RKPTIDLKNN HLQYLVTWYG LSFLSTIFLI
     VALRKAKRGG VVSQDQLMKE KLKHSRKYM
 
 
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