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YOL4_SCHPO
ID   YOL4_SCHPO              Reviewed;         675 AA.
AC   Q9P7P0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Uncharacterized acyltransferase C1718.04;
DE            EC=2.3.-.-;
GN   ORFNames=SPBC1718.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB75994.1; -; Genomic_DNA.
DR   PIR; T50332; T50332.
DR   RefSeq; NP_596450.1; NM_001022369.2.
DR   AlphaFoldDB; Q9P7P0; -.
DR   SMR; Q9P7P0; -.
DR   STRING; 4896.SPBC1718.04.1; -.
DR   iPTMnet; Q9P7P0; -.
DR   MaxQB; Q9P7P0; -.
DR   PaxDb; Q9P7P0; -.
DR   PRIDE; Q9P7P0; -.
DR   EnsemblFungi; SPBC1718.04.1; SPBC1718.04.1:pep; SPBC1718.04.
DR   GeneID; 2540110; -.
DR   KEGG; spo:SPBC1718.04; -.
DR   PomBase; SPBC1718.04; -.
DR   VEuPathDB; FungiDB:SPBC1718.04; -.
DR   eggNOG; ENOG502QQ2N; Eukaryota.
DR   HOGENOM; CLU_007860_1_0_1; -.
DR   InParanoid; Q9P7P0; -.
DR   OMA; NIRDHQV; -.
DR   PhylomeDB; Q9P7P0; -.
DR   PRO; PR:Q9P7P0; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; ISO:PomBase.
DR   GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; ISO:PomBase.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..675
FT                   /note="Uncharacterized acyltransferase C1718.04"
FT                   /id="PRO_0000317313"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          616..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   675 AA;  76628 MW;  388E126EDC7A57E8 CRC64;
     MQHTFIYDTC LWILSILIDF FFREVKTRGS FRVPRKGPLI LVAAPHANQF VDPLILMLQL
     RREVGRRTSI LVAAKSYRQR FIGLMSRAFG AIPVERAQDL AIRGEGKIFV VAEGDKTAIH
     GKDTLFTKHS VGDTLLLPNN YGSSHIASIK SDTLLYVKRE FRGEDAERVL LSPEGSSYKV
     APEIDQTYVY NEVRRRLVKG ACIALFPEGG SHDRPEMLPL KAGVAIMALE TLSQHPDCGL
     QLLPCGMNYF HPHRFRSRAV LEFGSPLSIP TEYVELYKAK KRREAIQGVL DMIYDALLSV
     TVQAPDYETL MVIQACRRLY KPAHIQFALP KVVDLNRKLI VGYNHFKHDP RVIRLHDKIL
     LYNRQLYRLG LRDHQVQSLQ YSRFMILYKL VYRCCKLFLL ALGALPGAIL FSPVFIAAHR
     ISVKKAAAAL KASSVKIQGR DILATWKLLV ALGMTPILYS FYALLCCYYI YSYKLIPHSS
     IFVYTVPIIS TFLFPMVTYA ALRFGEVAVD IYKSIRPLFL ALIPSKANAV YILKDERKQL
     VAEVTDLINK LGPELFPDFD PDRITTTIEK PERPSRFARR LSSSVASDVD NLSQLHDTDL
     NSEVSAPAPL QNVYLYSPNP SALPPSDEEE KDINDKAKLI RNALRQRMGQ RMTEIRSRDT
     PPEEVFSESD EELSD
 
 
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