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PEX11_DICDI
ID   PEX11_DICDI             Reviewed;         254 AA.
AC   Q54H86;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Peroxisomal membrane protein 11 homolog;
DE   AltName: Full=Peroxin-11;
GN   Name=pex11; ORFNames=DDB_G0289623;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Involved in peroxisomal proliferation. Could participate in
CC       peroxisomal elongation or fission. May be involved in parceling of
CC       peroxisomes into regular quanta (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR   EMBL; AAFI02000147; EAL62629.1; -; Genomic_DNA.
DR   RefSeq; XP_636138.1; XM_631046.1.
DR   AlphaFoldDB; Q54H86; -.
DR   STRING; 44689.DDB0238054; -.
DR   PaxDb; Q54H86; -.
DR   EnsemblProtists; EAL62629; EAL62629; DDB_G0289623.
DR   GeneID; 8627241; -.
DR   KEGG; ddi:DDB_G0289623; -.
DR   dictyBase; DDB_G0289623; pex11.
DR   eggNOG; KOG4186; Eukaryota.
DR   HOGENOM; CLU_049216_2_1_1; -.
DR   InParanoid; Q54H86; -.
DR   OMA; LVHWHVE; -.
DR   PhylomeDB; Q54H86; -.
DR   Reactome; R-DDI-9603798; Class I peroxisomal membrane protein import.
DR   PRO; PR:Q54H86; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
DR   GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR   GO; GO:0044375; P:regulation of peroxisome size; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   InterPro; IPR008733; PEX11.
DR   Pfam; PF05648; PEX11; 1.
PE   3: Inferred from homology;
KW   Membrane; Peroxisome; Peroxisome biogenesis; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..254
FT                   /note="Peroxisomal membrane protein 11 homolog"
FT                   /id="PRO_0000328183"
FT   TOPO_DOM        1..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..227
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  28720 MW;  509ACE523D47E074 CRC64;
     MAGILSKPNY NQFLESLIKL LAQTSGKDKI AKILQYGAKL LGYIFLKRSK HWVDVMKKLE
     TTSGSARKVW RLGNTLAEQQ KILALFKVKN PFAFLNILAL IRQSGMYFYW VFDHLILGTN
     IGLCKFDTVK LGWYSSVSWF FGLLCSIIID LNTLAIMLKK EKSLRLTITQ NKINANNNNI
     DTHTITSEVE NKAIIDQFNE VIKKKNEIYL NCAKNGSDLI IASTLLKIYP FSQGTIGISG
     IISALIGAYQ MWPK
 
 
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