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PIC2_YEAST
ID   PIC2_YEAST              Reviewed;         300 AA.
AC   P40035; D3DLV5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Mitochondrial phosphate carrier protein 2;
DE   AltName: Full=Phosphate transport protein 2;
DE            Short=PTP 2;
DE   AltName: Full=Pi carrier isoform 2;
DE   AltName: Full=mPic 2;
GN   Name=PIC2; OrderedLocusNames=YER053C;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
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   FUNCTION.
RX   PubMed=11328608; DOI=10.1093/oxfordjournals.jbchem.a002926;
RA   Takabatake R., Siddique A.B., Kouchi H., Izui K., Hata S.;
RT   "Characterization of a Saccharomyces cerevisiae gene that encodes a
RT   mitochondrial phosphate transporter-like protein.";
RL   J. Biochem. 129:827-833(2001).
RN   [4]
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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14756774; DOI=10.1046/j.1365-2958.2003.03810.x;
RA   Hamel P., Saint-Georges Y., de Pinto B., Lachacinski N., Altamura N.,
RA   Dujardin G.;
RT   "Redundancy in the function of mitochondrial phosphate transport in
RT   Saccharomyces cerevisiae and Arabidopsis thaliana.";
RL   Mol. Microbiol. 51:307-317(2004).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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: Transport of phosphate groups from the cytosol to the
CC       mitochondrial matrix. {ECO:0000269|PubMed:11328608,
CC       ECO:0000269|PubMed:14756774}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14756774}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14756774}.
CC   -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; U18796; AAB64588.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07709.1; -; Genomic_DNA.
DR   PIR; S50556; S50556.
DR   RefSeq; NP_010973.3; NM_001178944.3.
DR   AlphaFoldDB; P40035; -.
DR   SMR; P40035; -.
DR   BioGRID; 36792; 66.
DR   DIP; DIP-5340N; -.
DR   IntAct; P40035; 40.
DR   MINT; P40035; -.
DR   STRING; 4932.YER053C; -.
DR   TCDB; 2.A.29.4.4; the mitochondrial carrier (mc) family.
DR   iPTMnet; P40035; -.
DR   MaxQB; P40035; -.
DR   PaxDb; P40035; -.
DR   PRIDE; P40035; -.
DR   EnsemblFungi; YER053C_mRNA; YER053C; YER053C.
DR   GeneID; 856779; -.
DR   KEGG; sce:YER053C; -.
DR   SGD; S000000855; PIC2.
DR   VEuPathDB; FungiDB:YER053C; -.
DR   eggNOG; KOG0767; Eukaryota.
DR   HOGENOM; CLU_039456_2_0_1; -.
DR   InParanoid; P40035; -.
DR   OMA; YKTGVFL; -.
DR   BioCyc; MetaCyc:G3O-30231-MON; -.
DR   BioCyc; YEAST:G3O-30231-MON; -.
DR   PRO; PR:P40035; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40035; protein.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005375; F:copper ion transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IMP:SGD.
DR   GO; GO:0035434; P:copper ion transmembrane transport; IDA:SGD.
DR   GO; GO:1990547; P:mitochondrial phosphate ion transmembrane transport; IEA:InterPro.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:SGD.
DR   Gene3D; 1.50.40.10; -; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR044677; Pic2/Mir1-like.
DR   PANTHER; PTHR45671; PTHR45671; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..300
FT                   /note="Mitochondrial phosphate carrier protein 2"
FT                   /id="PRO_0000090640"
FT   TRANSMEM        22..42
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..192
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          16..100
FT                   /note="Solcar 1"
FT   REPEAT          107..193
FT                   /note="Solcar 2"
FT   REPEAT          209..293
FT                   /note="Solcar 3"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   300 AA;  33528 MW;  D8A54864F06F8264 CRC64;
     MESNKQPRKI QLYTKEFYAT CTLGGIIACG PTHSSITPLD LVKCRLQVNP KLYTSNLQGF
     RKIIANEGWK KVYTGFGATF VGYSLQGAGK YGGYEYFKHL YSSWLSPGVT VYLMASATAE
     FLADIMLCPF EAIKVKQQTT MPPFCNNVVD GWKKMYAESG GMKAFYKGIV PLWCRQIPYT
     MCKFTSFEKI VQKIYSVLPK KKEEMNALQQ ISVSFVGGYL AGILCAAVSH PADVMVSKIN
     SERKANESMS VASKRIYQKI GFTGLWNGLM VRIVMIGTLT SFQWLIYDSF KAYVGLPTTG
 
 
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