INP1_YEAST
ID INP1_YEAST Reviewed; 420 AA.
AC Q03694; D6W029;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Inheritance of peroxisomes protein 1;
GN Name=INP1; OrderedLocusNames=YMR204C; ORFNames=YM8325.05C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [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, SUBCELLULAR LOCATION, AND INTERACTION WITH PEX25; PEX30 AND VPS1.
RX PubMed=15928207; DOI=10.1083/jcb.200503083;
RA Fagarasanu M., Fagarasanu A., Tam Y.Y.C., Aitchison J.D., Rachubinski R.A.;
RT "Inp1p is a peroxisomal membrane protein required for peroxisome
RT inheritance in Saccharomyces cerevisiae.";
RL J. Cell Biol. 169:765-775(2005).
RN [6]
RP FUNCTION.
RX PubMed=16678774; DOI=10.1016/j.devcel.2006.04.012;
RA Fagarasanu A., Fagarasanu M., Eitzen G.A., Aitchison J.D.,
RA Rachubinski R.A.;
RT "The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor
RT for the myosin V motor Myo2p of Saccharomyces cerevisiae.";
RL Dev. Cell 10:587-600(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY
RP 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 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: Required for peroxisome inheritance.
CC {ECO:0000269|PubMed:15928207, ECO:0000269|PubMed:16678774}.
CC -!- SUBUNIT: Interacts with PEX25, PEX30 and VPS1.
CC {ECO:0000269|PubMed:15928207}.
CC -!- INTERACTION:
CC Q03694; P28795: PEX3; NbExp=6; IntAct=EBI-27445, EBI-13164;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15928207}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15928207}.
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the INP1 family. {ECO:0000305}.
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DR EMBL; Z48755; CAA88645.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10103.1; -; Genomic_DNA.
DR PIR; S59445; S59445.
DR RefSeq; NP_013931.1; NM_001182711.1.
DR AlphaFoldDB; Q03694; -.
DR SMR; Q03694; -.
DR BioGRID; 35382; 74.
DR DIP; DIP-4415N; -.
DR IntAct; Q03694; 5.
DR MINT; Q03694; -.
DR STRING; 4932.YMR204C; -.
DR iPTMnet; Q03694; -.
DR MaxQB; Q03694; -.
DR PaxDb; Q03694; -.
DR PRIDE; Q03694; -.
DR EnsemblFungi; YMR204C_mRNA; YMR204C; YMR204C.
DR GeneID; 855244; -.
DR KEGG; sce:YMR204C; -.
DR SGD; S000004817; INP1.
DR VEuPathDB; FungiDB:YMR204C; -.
DR eggNOG; ENOG502S7ZC; Eukaryota.
DR HOGENOM; CLU_056604_0_0_1; -.
DR InParanoid; Q03694; -.
DR OMA; RFWEIEF; -.
DR BioCyc; YEAST:G3O-32890-MON; -.
DR PRO; PR:Q03694; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03694; protein.
DR GO; GO:0005780; C:extrinsic component of intraperoxisomal membrane; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0045033; P:peroxisome inheritance; IMP:SGD.
DR InterPro; IPR024758; Inp1.
DR Pfam; PF12634; Inp1; 1.
DR PRINTS; PR02103; INPROXISOME1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..420
FT /note="Inheritance of peroxisomes protein 1"
FT /id="PRO_0000203328"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 420 AA; 47315 MW; A11EF51211DEF675 CRC64;
MVLSRGETKK NSVRLTAKQE KKPQSTFQTL KQSLKLSNNK KLKQDSTQHS NDTNKSVKAK
KNGTSSKKTG TQRKRISTQR FSLFTYGNVQ VMNSFVPIHN DIPNSSCIRR NSQVSANNVT
ESSGVFFNDT QSQDSQNTIK LKPTSLMAKG PIEIYQICTG FDKLKENIAP FQKSSKASSH
DGHVVNYLSI GRHGDIVHPV LPKLQITRLN GAGFKYFISF YNPERYWEIE FLPLISQSQS
ELENSVKAFE NVISKICQFS HINEGATIGN NESLSDKFKL PPTSDIEPPN TEIINNDDDN
DDDDDNYDDD DLNYLLDEEY EQGCTDNSFS VISNTCSNLN ASFLYPSDPT DAVSISINEA
FKNAIRRTAP VLNIPIAAPS IHSKQQNKRY SSYPFIDSPP YLQDRHRRFQ RRSISGLGDL
